徳島大学 / 教育研究者総覧 --- 伊藤孝司

個人のホームページ

https://researchmap.jp/kitoh3212 (researchmap)

https://orcid.org/0000-0002-2953-5530 (ORCID)

専門分野

○	分子生物学 (Molecular Biology), 分子病理学 (Molecular Pathology), 分子治療学 (Molecular Therapy), 糖鎖生物学 (Glycobiology)

研究テーマ

○	遺伝子疾患の発症機構の解明と治療法開発に関する研究, 糖鎖工学および幹細胞工学に基く医薬資源開発 (糖鎖分解酵素(リソソーム酵素)欠損症, 酵素補充療法, 幹細胞工学, 糖鎖工学, 胃がん·大腸がんのプロテオミクス) (糖鎖分解酵素(リソソーム酵素)欠損症·がんの発症の分子機構の解明と診断·治療法開発を目的とし，表現型に及ぼす遺伝子変異や酵素(タンパク質)の機能異常の影響に対する分子病理学的解析と，バイオインフォーマティクスを利用した高機能化酵素分子のデザインや分子間相互作用に関する研究を進めている．またリソソーム酵素欠損症のモデルマウスを対象に，糖鎖工学や幹細胞工学を利用した，組換え酵素の脳内補充療法や細胞移植治療法に関する基礎研究を行っている．さらに医学部·薬学部との共同研究プロジェクトとして消化器がんのプロテオミクス解析と分子標的の探索を進めている．)

著書・論文

著書:

1.	月本準, 伊藤孝司 : ガラクトシアリドーシス, 2023年10月.
2.	湯浅康弘, 沖津宏, 後藤正和, 枝川広志, 大森理佐, 谷亮太郎, 増田有理, 蔵本俊輔, 松本大資, 富林敦司, 浜田陽子, 山下留理子, 藤井義幸, 伊藤孝司 : 癌と化学療法, --- 術前2週間のS-1投与によりGrade2の治療効果が得られた進行胃癌の1例 ---, 株式会社癌と化学療法社, 東京, 2015年5月. (要約) In our hospital, a clinical trial on the effects of preoperative 2-week S-1 administration for advanced gastric cancer is being conducted. A7 5-year-old man presented to our hospital with a type 2 tumor(poorly differentiated adenocarcinoma)in the pyloric antrum. Subpyloric lymph node enlargement and a c-T2(MP), N1, M0, Stage II A tumor (according to the gastric cancer handling agreement, 14th edition)were diagnosed, and S-1(100mg/day)was subsequently administered for 14 days. On day 15, we performed laparoscopy-assisted distal gastrectomy, with D2 dissection. Analysis of the resected specimen, ie the primary tumor and metastatic lymph nodes, confirmed the effect of the treatment as Grade 2, and revealed a type 2 gastric cancer of 30×20mm in size; this tumor was downstaged to yp-T1b(SM), N1, Stage I B. No adverse events associated with perioperative S-1 were observed, and the postoperative course was good. At the latest follow-up(6 years after treatment), no recurrence was observed. (キーワード) Adenocarcinoma / Aged / Antimetabolites, Antineoplastic / Drug Combinations / Gastrectomy / Humans / Lymph Node Excision / Male / Neoadjuvant Therapy / Neoplasm Staging / Oxonic Acid / Stomach Neoplasms / Tegafur (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25981663 ● Search Scopus @ Elsevier (PMID): 25981663 (PubMed: 25981663)
3.	伊藤孝司 : シアリドーシス, 日本臨牀社, 東京, 2014年12月.
4.	伊藤孝司 : ガラクトシアリドーシス, 日本臨牀社, 東京, 2014年12月.
5.	伊藤孝司 : ガラクトシアリドーシス, 日本臨牀社, 東京, 2014年12月.
6.	Daisuke Tsuji and Kouji Itou : Molecular Therapy for Lysosomal Storage Diseases., Intech, Rijeka,Croatia, Mar. 2013. (キーワード) リソソーム病
7.	伊藤孝司 : 「ガラクトシアリドーシス」先天代謝異常ハンドブック, 株式会社中山書店, 東京, 2013年2月.
8.	Nakayama Yoshiaki, Nakamura Naosuke, Daisuke Tsuji, Kouji Itou and Kurosaka Akira : Genetic Diseases Associated with Protein Glycosylation Disorders in Mammals., Intech, Rijeka,Croatia, Jan. 2013.
9.	伊藤孝司 : 先天代謝異常症候群(第2版) 下, --- 病因・病態研究，診断・治療の進歩 Ⅶライソゾーム病糖タンパク代謝異常症ガラクトシアリドーシス ---, 日本臨牀社, 東京, 2012年12月.
10.	伊藤孝司 : 第4章新規生産基材を利用した組換えリソソーム病治療薬の開発, 株式会社シーエムシー出版監修:山口照英, 東京, 2012年4月.
11.	伊藤孝司 : バイオ医薬品開発における糖鎖技術, --- リソソーム病治療への応用を目指した糖鎖修飾型組換えリソソーム酵素の開発 ---, 株式会社シーエムシー出版, 東京, 2011年11月.
12.	伊藤孝司 : ガラクトシアリドーシス, 株式会社診断と治療社, 東京, 2011年6月.
13.	伊藤孝司 : シアリドーシス, イーエスメディックス, 東京, 2011年.
14.	辻大輔, 伊藤孝司 : 細胞の構造とオルガネラ:第3章-4 リソソーム蓄積症(リソソーム病), 株式会社廣川書店, 東京, 2010年.
15.	Kouji Itou : Recent Advances in Enzyme Replacement Therapy for Lysosomal Diseases, Springer, New York, Aug. 2008.

学術論文(審査論文):

1.	Naonobu Tanaka, Itsukoh Shibata, Yusuke Tasaki, Yuki Yoshino, Daisuke Tsuji, Lu Fen-Lai, Yang Xia-Jie, Yang Xue-Rong, Kouji Itou, Akagi Reiko and Yoshiki Kashiwada : Acylated iridoid glucoside and xanthones from Canscora lucidissima: Their structures and ferroptosis inhibitory activity, Fitoterapia, Vol.168, 105539, 2023. (要約) Phytochemical study on the whole plants of a Gentianaceous medicinal plant, Canscora lucidissima, gave one new acylated iridoid glucoside, canscorin A (1), and two new xanthone glycosides (2 and 3) together with 17 known compounds including five xanthones, eight xanthone glycosides, two benzophenone glucosides, caffeic acid, and loganic acid. Canscorin A (1) was assigned as a loganic acid derivative having a hydroxyterephthalic acid moiety by spectroscopic analysis together with chemical evidence, while 2 and 3 were elucidated to be a rutinosylxanthone and a glucosylxanthone, respectively. The absolute configurations of the sugar moieties of 2 and 3 were determined by HPLC analysis. The isolated compounds were evaluated for their inhibitory activities against erastin-induced ferroptosis on human hepatoma Hep3B cells and LPS-stimulated IL-1β production from murine microglial cells. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.fitote.2023.105539 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37178810 ● Search Scopus @ Elsevier (PMID): 37178810 ● Search Scopus @ Elsevier (DOI): 10.1016/j.fitote.2023.105539 (DOI: 10.1016/j.fitote.2023.105539, PubMed: 37178810)
2.	Yuki Yoshino, Naonobu Tanaka, Daisuke Tsuji, Kouji Itou and Yoshiki Kashiwada : Communiferulins, farnesylated coumarins from the roots of Ferula communis and their anti-neuroinflammatory activity, Journal of Natural Medicines, Vol.77, No.1, 173-179, 2023. (要約) Three new farnesylated coumarins, communiferulins A-C (1-3), and a farnesylated chromone, ferchromone (4), were isolated from the roots of an Apiaceous plant Ferula communis. Their structures including the relative configurations were elucidated by a combination of spectroscopic analyses and calculations of the NMR data. Communiferulins A-C (1-3) had dihydrofuran rings fused to C-3 and C-4 of their coumarin moieties, while 3 possessed one additional furan ring. HPLC analyses using a chiral column showed 1-4 to be racemates, and the absolute configurations of (+)-1, (-)-1, (+)-2, and (-)-2 were deduced by comparison of their ECD spectra with TDDFT-calculated spectra. Communiferulins A (1) and B (2), and ferchromone (4) showed inhibitory activities on IL-1β production from LPS-stimulated microglial cells. (キーワード) Ferula / 分子構造 (molecular structure) / Plant Extracts / Magnetic Resonance Spectroscopy / Coumarins / Plant Roots (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s11418-022-01657-8 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36289185 ● Summary page in Scopus @ Elsevier: 2-s2.0-85140649347 (DOI: 10.1007/s11418-022-01657-8, PubMed: 36289185, Elsevier: Scopus)
3.	OHNISHI Yukiya, Daisuke Tsuji and Kouji Itou : Oxidative Stress Impairs AutophagyviaInhibition of Lysosomal Transport of VAMP8, Biological & Pharmaceutical Bulletin, Vol.45, No.11, 1609-1615, 2022. (要約) Autophagy is a highly conserved intracellular degrading system and its dysfunction is considered related to the cause of neurodegenerative disorders. A previous study showed that the inhibition of endocytosis transport attenuates soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein transport to lysosomes and block autophagy. The other studies demonstrated oxidative stress, one of the inducers of neurodegenerative diseases inhibits endocytosis transport. Thus, we hypothesized that oxidative stress-induced endocytosis inhibition causes alteration of SNARE protein transport to lysosomes and impairs autophagy. Here, we demonstrated that oxidative stress inhibits endocytosis and decreased the lysosomal localization of VAMP8, one of the autophagy-related SNARE proteins in a human neuroblastoma cell line. Moreover, this oxidative stress induction blocked the autophagosome-lysosome fusion step. Since we also observed decreased lysosomal localization of VAMP8 and inhibition of autophagosome-lysosome fusion in endocytosis inhibitor-treated cells, oxidative stress may inhibit VAMP8 trafficking by suppressing endocytosis and impair autophagy. Our findings suggest that oxidative stress-induced inhibition of VAMP8 trafficking to lysosomes is associated with the development of neurodegenerative diseases due to the blocked autophagosome-lysosome fusion, and may provide a new therapeutic target for restoring the autophagic activity. (キーワード) Humans / Autophagy / Lysosomes / Membrane Fusion / Oxidative Stress / R-SNARE Proteins / SNARE Proteins / Biological Transport (出版サイトへのリンク) ● Publication site (DOI): 10.1248/bpb.b22-00131 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36328496 ● Search Scopus @ Elsevier (PMID): 36328496 ● Search Scopus @ Elsevier (DOI): 10.1248/bpb.b22-00131 (DOI: 10.1248/bpb.b22-00131, PubMed: 36328496)
4.	Tanaka Hiroki, Daisuke Tsuji, Watanabe Ryosuke, Ohnishi Yukiya, Kitaguchi Shindai, Nakae Ryuto, Teramoto Hiromi, Jun Tsukimoto, Horii Yuto and Kouji Itou : Aberrant autophagy in lysosomal storage disorders marked by a lysosomal SNARE protein shortage due to suppression of endocytosis, Journal of Inherited Metabolic Disease, Vol.45, No.6, 1191-1202, 2022. (要約) Lysosomal storage disorders (LSDs) are inherited metabolic diseases caused by genetic defects in lysosomal enzymes or related factors. LSDs are associated with excessive accumulation of natural substrates in lysosomes leading to central nervous system and peripheral tissue damage. Abnormal autophagy is also involved in pathogenesis, although the underlying mechanisms remain unclear. We demonstrated that impairment of lysosome-autophagosome fusion is due to suppressed endocytosis in LSDs. The fusion was reduced in several LSD cells and the brains of LSD model mice, suggesting that the completion of autophagy is suppressed by the accumulation of substrates. In this brain, the expression of the soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) proteins, VAMP8 and Syntaxin7, was decreased on the lysosomal surface but not intracellular. This aberrant autophagy preceded the development of pathological phenotypes in LSD-model mice. Furthermore, the enzyme deficiency leading to the substrate accumulation could suppress endocytosis, and the inhibited endocytosis decreased SNARE proteins localized on lysosomes. These findings suggest that the shortage of SNARE proteins on lysosomes is one of the reasons for the impairment of lysosome-autophagosome fusion in LSD cells. Defects in lysosomal enzyme activity suppress endocytosis and decrease the supply of intracellular SNARE proteins recruited to lysosomes. This shortage of lysosomal SNARE proteins impairs lysosome-autophagosome fusion in lysosomal storage disorders. (キーワード) Animals / Mice / Autophagy / Endocytosis / Lysosomal Storage Diseases / Lysosomes / SNARE Proteins (出版サイトへのリンク) ● Publication site (DOI): 10.1002/jimd.12558 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36102069 ● Search Scopus @ Elsevier (PMID): 36102069 ● Search Scopus @ Elsevier (DOI): 10.1002/jimd.12558 (DOI: 10.1002/jimd.12558, PubMed: 36102069)
5.	Yuto Horii, Toshiki Iniwa, Masayoshi Onitsuka, Jun Tsukimoto, Yuki Tanaka, Hironobu Ike, Yuri Fukushi, Haruna Andoh, Yoshie Takeuchi, So-ichiro Nishioka, Daisuke Tsuji, Mariko Ikuo, Naoshi Yamazaki, Yoshiharu Takiguchi, Naozumi Ishimaru and Kouji Itou : Reversal of neuroinflammation in novel galactosialidosis model mice by single intracerebroventricular administration of CHO-derived human recombinant cathepsin A precursor protein., Molecular Therapy. Methods & Clinical Development, Vol.25, No.June, 297-310, 2022. (徳島大学機関リポジトリ) ● Metadata: 117739 (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.omtm.2022.04.001 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1016/j.omtm.2022.04.001 (徳島大学機関リポジトリ: 117739, DOI: 10.1016/j.omtm.2022.04.001)
6.	Naonobu Tanaka, Yuki Yoshino, Fusako Nakano, Shin-ichiro Kurimoto, Kazuyoshi Kawazoe, Daisuke Tsuji, Kouji Itou, Shun-Lin Li, Han-Dong Sun, Yoshihisa Takaishi and Yoshiki Kashiwada : Lanicepines A and B, sesquiterpenes with amino acid-derived substituents from the flowering aerial parts of Saussurea laniceps, Journal of Natural Products, Vol.85, No.4, 1180-1185, 2022. (出版サイトへのリンク) ● Publication site (DOI): 10.1021/acs.jnatprod.1c01069 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1021/acs.jnatprod.1c01069 (DOI: 10.1021/acs.jnatprod.1c01069)
7.	Jun Tsukimoto, Yoshie Takeuchi, Yuto Horii, Toshiki Iniwa, Yuri Fukushi, So-ichiro Nishioka and Kouji Itou : In Cellulo Crystallization of Human Neuraminidase 1 and Biological Roles of N-Glycans, ACS Applied Bio Materials, Vol.5, No.1, 205-231, 2021. (出版サイトへのリンク) ● Publication site (DOI): 10.1021/acsabm.1c01043 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1021/acsabm.1c01043 (DOI: 10.1021/acsabm.1c01043)
8.	Kanji Niwa, Naonobu Tanaka, Shimomoto Yusei, Daisuke Tsuji, Kim Sang-Yong, Kojoma Mareshige, Kouji Itou, Chen Chin-Ho, Lee Kuo-Hsing and Yoshiki Kashiwada : Hyperdioxanes, dibenzo-1,4-dioxane derivatives from the roots of Hypericum ascyron, Journal of Natural Medicines, Vol.75, No.4, 907-914, 2021. (要約) Six dibenzo-1,4-dioxane derivatives (1-6) were isolated from the roots of a Hypericaceous plant Hypericum ascyron. Spectroscopic analyses revealed 2 and 4-6 to be new compounds. The partial racemic natures of 1-3 were concluded by chiral HPLC analyses, while 5 was confirmed to be a racemate. The absolute configurations 1-4 were deduced on the basis of ECD calculations. Biological activity evaluation of the dibenzo-1,4-dioxane derivatives along with two related compounds: hyperdioxanes A (7) and B (8), previously isolated from the same plant material by our group demonstrated that 7 exhibit an anti-HIV activity (IC 5.3 μM, TI 7.2) while 8 showed an inhibitory effect on IL-1β production (inhibition rate: 72.3% at 6.3 μM) from LPS-stimulated microglial cells. (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s11418-021-01540-y (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34142303 ● Search Scopus @ Elsevier (PMID): 34142303 ● Search Scopus @ Elsevier (DOI): 10.1007/s11418-021-01540-y (DOI: 10.1007/s11418-021-01540-y, PubMed: 34142303)
9.	Naonobu Tanaka, Amuti Saidanxia, Sakura Takahashi, Daisuke Tsuji, Kouji Itou and Yoshiki Kashiwada : Studies on non-medicinal parts of plant materials: Triterpenes from the roots of Schisandra chinensis, Fitoterapia, Vol.152, 104939, 2021. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.fitote.2021.104939 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-85106474288 (DOI: 10.1016/j.fitote.2021.104939, Elsevier: Scopus)
10.	Naonobu Tanaka, Sakura Takahashi, Seita Kajihara, Daisuke Tsuji, Kouji Itou, Nilufar Z. Mamadalieva and Yoshiki Kashiwada : Diterpenes from an Uzbek medicinal plant Perovskia scrophulariifolia: their structures and anti-neuroinflammatory activity, Fitoterapia, Vol.149, 104826, 2021. (要約) Phytochemical investigation on the aerial parts of a Lamiaceous medicinal plant Perovskia scrophulariifolia collected in Uzbekistan resulted in the isolation of two new 20-norabietane diterpenes, along with thirteen known diterpenes including one 20-norabietane, eight abietanes, one 6,7-secoabietane, and three icetexanes. The structures of new 20-norabietane diterpenes, perovsfolins C (1) and D (2), were elucidated by spectroscopic analyses aided with calculations of ECD spectra. Perovsfolin C (1) is the first 20-norabietane diterpene possessing a 1,11-epoxy moiety, while perovsfolin D (2) is a 20-norabitetane diterpene with a 2-hydroxy-1,4-quinone moiety as C-ring. Anti-neuroinflammatory activity of the isolated diterpenes on microglial cells was evaluated. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.fitote.2021.104826 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33429024 ● Search Scopus @ Elsevier (PMID): 33429024 ● Search Scopus @ Elsevier (DOI): 10.1016/j.fitote.2021.104826 (DOI: 10.1016/j.fitote.2021.104826, PubMed: 33429024)
11.	Naonobu Tanaka, Kanji Niwa, Seita Kajihara, Daisuke Tsuji, Kouji Itou, Nilufar Z. Mamadalieva and Yoshiki Kashiwada : C28 Terpenoids from Lamiaceous plant Perovskia scrophulariifolia: their structures and anti-neuroinflammatory activity, Organic Letters, Vol.22, No.19, 7667-7670, 2020. (要約) Structurally unique C terpenoids, perovsfolins A () and B (), were isolated from the aerial parts of an Uzbek medicinal plant, (Lamiaceae). Their chemical structures including an unprecedented 6/8/6/6/6 pentacyclic carbon skeleton with a C-C ester moiety were elucidated on the basis of spectroscopic analyses aided by density functional theory calculations as well as chemical evidence. Perovsfolin B () exhibited an anti-neuroinflammatory activity. (出版サイトへのリンク) ● Publication site (DOI): 10.1021/acs.orglett.0c02855 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32941043 ● Search Scopus @ Elsevier (PMID): 32941043 ● Search Scopus @ Elsevier (DOI): 10.1021/acs.orglett.0c02855 (DOI: 10.1021/acs.orglett.0c02855, PubMed: 32941043)
12.	Lee Sanghoon, Naonobu Tanaka, TAKAHASHI Sakura, Daisuke Tsuji, KIM Sang-Yong, KOJOMA Mareshige, Kouji Itou, Kobayashi Jun'ichi and Yoshiki Kashiwada : Agesasines A and B, Bromopyrrole Alkaloids from Marine Sponges Agelas spp., Marine Drugs, Vol.18, No.9, 455, 2020. (要約) Exploration for specialized metabolites of Okinawan marine sponges spp. resulted in the isolation of five new bromopyrrole alkaloids, agesasines A () and B (), 9-hydroxydihydrodispacamide (), 9-hydroxydihydrooroidin (), and 9-keramadine (). Their structures were elucidated on the basis of spectroscopic analyses. Agesasines A () and B () were assigned as rare bromopyrrole alkaloids lacking an aminoimidazole moiety, while - were elucidated to be linear bromopyrrole alkaloids with either aminoimidazolone, aminoimidazole, or -methylated aminoimidazole moieties. (徳島大学機関リポジトリ) ● Metadata: 116231 (出版サイトへのリンク) ● Publication site (DOI): 10.3390/md18090455 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32872586 ● Search Scopus @ Elsevier (PMID): 32872586 ● Search Scopus @ Elsevier (DOI): 10.3390/md18090455 (徳島大学機関リポジトリ: 116231, DOI: 10.3390/md18090455, PubMed: 32872586)
13.	Naonobu Tanaka, Kenta Yamada, Yusei Shimomoto, Daisuke Tsuji, Kouji Itou, Kazuyoshi Kawazoe, Davaadagva Damdinjav, Enkhjargal Dorjval and Yoshiki Kashiwada : Lophachinins A-E, abietane diterpenes from a Mongolian traditional herbal medicine Lophanthus chinensis, Fitoterapia, Vol.146, 104702, 2020. (要約) Five new abietane diterpenes, lophachinins A-E (1-5), and eleven known related diterpenes were isolated from a Mongolian traditional herbal medicine, the aerial parts of Lophanthus chinensis (Lamiaceae). The structures of new diterpenes were assigned by spectroscopic analyses. Lophachinins A (1) and B (2) were abietane diterpene possessing an endoperoxy bridge at C-ring. In contrast, lophachinins C-E (3-5) had an abietane skeleton with an aromatized C-ring. The absolute configuration of 1 was elucidated by application of the modified Mosher's method, while those of 2, 3, and 5 were assigned by chemical conversions. The absolute configuration of lophachinin D (4) was deduced by ECD calculation. Anti-inflammatory activity of isolated diterpenes on microglial cells were evaluated. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.fitote.2020.104702 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32763363 ● Summary page in Scopus @ Elsevier: 2-s2.0-85089268104 (DOI: 10.1016/j.fitote.2020.104702, PubMed: 32763363, Elsevier: Scopus)
14.	XueRong Yang, Naonobu Tanaka, Daisuke Tsuji, Feng-Lai Lu, Xiao-Jie Yan, Kouji Itou, Dian-Peng Li and Yoshiki Kashiwada : Sarcaglabrin A, a conjugate of C15 and C10 terpenes from the aerial parts of Sarcandra glabra, Tetrahedron Letters, Vol.61, No.25, 151916, 2020. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.tetlet.2020.151916 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-85085004730 (DOI: 10.1016/j.tetlet.2020.151916, Elsevier: Scopus)
15.	Atsushi Nakayama, Akira Ohtani, Tsubasa Inokuma, Daisuke Tsuji, Haruka Mukaiyama, Nakayama Akira, Kouji Itou, Akira Otaka, Tanino Keiji and Kosuke Namba : Development of a 1,3a,6a-triazapentalene derivatives as a compact and thiol-specific fluorescent labeling reagent, Communications Chemistry, Vol.3, 6, 2020. (徳島大学機関リポジトリ) ● Metadata: 115071 (出版サイトへのリンク) ● Publication site (DOI): 10.1038/s42004-019-0250-0 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-85077692885 (徳島大学機関リポジトリ: 115071, DOI: 10.1038/s42004-019-0250-0, Elsevier: Scopus)
16.	Kanji Niwa, REN YI, Naonobu Tanaka, Shindai Kitaguchi, Daisuke Tsuji, Sang-Yong Kim, Ariuntuya Tsogtbaatar, Perleidulam Bunddulam, Kazuyoshi Kawazoe, Mareshige Kojoma, Davaadagva Damdinjav, Kouji Itou and Yoshiki Kashiwada : Linaburiosides A-D, acylated iridoid glucosides from Linaria buriatica, Phytochemistry, Vol.171, 112247, 2020. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.phytochem.2019.112247 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-85077471922 (DOI: 10.1016/j.phytochem.2019.112247, Elsevier: Scopus)
17.	Kei Kiriyama and Kouji Itou : Glycan Recognition and Application of P-Type Lectins, Methods in Molecular Biology, Vol.2132, 267-276, 2020. (要約) Cation-dependent mannose 6-phosphate receptor (CD-MPR) and cation-independent MPR (CI-MPR) belong to the P-type lectin family. Both intracellular and cell surface MPRs can recognize and bind with the terminal mannose 6-phospahte (M6P) residues of N-glycans attached to the mammalian lysosomal enzymes and the related co-factors. Domain9 (Dom9), which is one of the extracytoplasmic region of the CI-MPR, has relatively higher affinity for M6P residues. Here we describe the production of recombinant Dom9-His protein by Pichia pastris, purification, and application as a probe for lectin blotting. (キーワード) Amino Acid Sequence / Binding Sites / Cloning, Molecular / Humans / Lysosomes / Mannosephosphates / Pichia / Polysaccharides / Protein Domains / Receptor, IGF Type 2 (出版サイトへのリンク) ● Publication site (DOI): 10.1007/978-1-0716-0430-4_26 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32306334 ● Summary page in Scopus @ Elsevier: 2-s2.0-85083755542 (DOI: 10.1007/978-1-0716-0430-4_26, PubMed: 32306334, Elsevier: Scopus)
18.	Xuerong Yang, Naonobu Tanaka, Daisuke Tsuji, Lu Feng-Lai, Yan Xiao-Jie, Kouji Itou, Li Dian-Peng and Yoshiki Kashiwada : Limonoids from the aerial parts of Munronia pinnata, Tetrahedron, Vol.75, No.52, 130779, 2019. (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.tet.2019.130779 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1016/j.tet.2019.130779 (DOI: 10.1016/j.tet.2019.130779)
19.	Kotaro Koiwai, Jun Tsukimoto, Tetsuya Higashi, Fumitaka Mafune, Ken Miyajima, Takanori Nakane, Naoshiro Matsugaki, Ryuichi Kato, Serena Sirigu, Arjen J Jakobi, Matthias Wilmanns, Michihiro Sugahara, Tomoyuki Tanaka, Kensuke Tono, Yasumasa Joti, Makina Yabashi, Osamu Nureki, Eiichi Mizohata, Toru Nakatsu, Eriko Nango, So Iwata, Leonard Chavas, Toshiya Senda, Kouji Itou and Fumiaki Yumoto : Improvement of production and isolation of human neuraminidase-1 in cellulo crystals., ACS Applied Bio Materials, Vol.2, No.11, 4941-4952, 2019. (要約) crystallization is a developing technique to provide crystals for protein structure determination, particularly for proteins that are difficult to prepare by crystallization. This method has a key advantage: it requires neither a protein purification step nor a crystallization step. However, there is still no systematic strategy for improving the technique of crystallization because the process occurs spontaneously. Here we report a protocol to produce and extract crystals of human lysosomal neuraminidase-1 (NEU1) in human cultured cells. Overexpression of NEU1 protein by the retransfection of cells pretransfected with -overexpressing plasmid improved the efficiency of NEU1 crystallization. Microscopic analysis revealed that NEU1 proteins were not crystallized in the lysosome but in the endoplasmic reticulum (ER). Screening of the buffer conditions used to extract crystals from cells further improved the crystal yield. The optimal pH was 7.0, which corresponds to the pH in the ER. Use of a high-yield flask with a large surface area also yielded more crystals. These optimizations enabled us to execute a serial femtosecond crystallography experiment with a sufficient number of crystals to generate a complete data set. Optimization of the crystallization method was thus shown to be possible. (出版サイトへのリンク) ● Publication site (DOI): 10.1021/acsabm.9b00686 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35021494 ● Summary page in Scopus @ Elsevier: 2-s2.0-85073832529 (DOI: 10.1021/acsabm.9b00686, PubMed: 35021494, Elsevier: Scopus)
20.	Chiaki Komiya, Akira Shigenaga, Jun Tsukimoto, Masahiro Ueda, Takuya Morisaki, Tsubasa Inokuma, Kouji Itou and Akira Otaka : Traceless synthesis of protein thioesters using enzyme-mediated hydrazinolysis and subsequent self-editing of cysteinyl prolyl sequence, Chemical Communications, Vol.55, 7029-7032, 2019. (徳島大学機関リポジトリ) ● Metadata: 113348 (出版サイトへのリンク) ● Publication site (DOI): 10.1039/C9CC03583D (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31140482 ● Summary page in Scopus @ Elsevier: 2-s2.0-85067257026 (徳島大学機関リポジトリ: 113348, DOI: 10.1039/C9CC03583D, PubMed: 31140482, Elsevier: Scopus)
21.	Nakajima Hideki, Ueno Miki, Adachi Kaori, Nanba Eiji, Narita Aya, Tsukimoto Jun, Kouji Itou and Kawakami Atsushi : A new heterozygous compound mutation in the CTSA gene in galactosialidosis, Human Genome Variation, Vol.6, 22, 2019. (要約) Galactosialidosis is an autosomal recessive lysosomal storage disease caused by the combined deficiency of lysosomal β-galactosidase and neuraminidase due to a defect in the protective protein/cathepsin A. Patients present with various clinical manifestations and are classified into three types according to the age of onset: the early infantile type, the late infantile type, and the juvenile/adult type. We report a Japanese female case of juvenile/adult type galactosialidosis. Clinically, she presented with short stature, coarse facies, angiokeratoma, remarkable action myoclonus, and cerebellar ataxia. The patient was diagnosed with galactosialidosis with confirmation of impaired β-galactosidase and neuraminidase function in cultured skin fibroblasts. Sanger sequencing for CTSA identified a compound heterozygous mutation consisting of NM_00308.3(CTSA):c.746 + 3A>G and c.655-1G>A. Additional analysis of her mother's DNA sequence indicated that the former mutation originated from her mother, and therefore the latter was estimated to be from the father or was a de novo mutation. Both mutations are considered pathogenic owing to possible splicing abnormalities. One of them (c.655-1G>A) is novel because it has never been reported previously. (徳島大学機関リポジトリ) ● Metadata: 114568 (出版サイトへのリンク) ● Publication site (DOI): 10.1038/s41439-019-0054-x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31044084 ● Summary page in Scopus @ Elsevier: 2-s2.0-85069296817 (徳島大学機関リポジトリ: 114568, DOI: 10.1038/s41439-019-0054-x, PubMed: 31044084, Elsevier: Scopus)
22.	Naoshi Yamazaki, Keisuke Kanazawa, Maria Kimura, Hironobu Ike, Makiko Shinomiya, Shouko Tanaka, Yasuo Shinohara, Noriaki Minakawa, Kouji Itou and Yoshiharu Takiguchi : Use of modified U1 small nuclear RNA for rescue from exon 7 skipping caused by 5-splice site mutation of human cathepsin A gene, Gene, Vol.677, 41-48, 2018. (要約) Cathepsin A (CTSA) is a multifunctional lysosomal enzyme, and its hereditary defect causes an autosomal recessive disorder called galactosialidosis. In a certain number of galactosialidosis patients, a base substitution from adenine to guanine is observed at the +3 position of the 7th intron (IVS7 +3a>g) of the CTSA gene. With this mutation, a splicing error occurs; and consequently mRNA lacking the 7th exon is produced. This skipping of exon 7 causes a frame shift of the transcripts, resulting in a non-functional CTSA protein and hence galactosialidosis. This mutation seems to make the interaction between the 5'-splice site of intron 7 of pre-mRNA and U1 small nuclear RNA (U1 snRNA) much weaker. In the present study, to produce properly spliced mRNA from the CTSA gene harboring this IVS7 +3a>g mutation, we examined the possible usefulness of modified U1 snRNA that could interact with the mutated 5'-splice site. Toward this goal, we first prepared a model system using a mutant CTSA mini gene plasmid for delivery into HeLa cells. Then, we examined the effectiveness of modified U1 snRNA on the formation of properly spliced mRNA from this mutant CTSA mini gene. As a result, we succeeded in obtaining improved formation of properly spliced CTSA mRNA. Our results suggest the usefulness of modified U1 snRNA for rescue from exon 7 skipping caused by the IVS7 +3a>g mutation of the CTSA gene. (キーワード) Cathepsin A / Cell Line, Tumor / Exons / HeLa Cells / Humans / Introns / Mutation / RNA Precursors / RNA Splice Sites / RNA Splicing / RNA, Messenger / RNA, Small Nuclear (徳島大学機関リポジトリ) ● Metadata: 111998 (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.gene.2018.07.030 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30010039 ● Summary page in Scopus @ Elsevier: 2-s2.0-85050244217 (徳島大学機関リポジトリ: 111998, DOI: 10.1016/j.gene.2018.07.030, PubMed: 30010039, Elsevier: Scopus)
23.	Hirokazu Miki, Shingen Nakamura, Asuka Oda, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Ariunzaya Bat-Erdene, Yusaku Maeda, Masahiro Oura, Mamiko Takahashi, Masami Iwasa, Takeshi Harada, Shiroh Fujii, Kiyoe Kurahashi, Sumiko Yoshida, Kumiko Kagawa, Itsuro Endo, Aihara Kenichi, Mariko Ikuo, Kouji Itou, Koichiro Hayashi, Michihiro Nakamura and Masahiro Abe : Effective impairment of myeloma cells and their progenitors by hyperthermia., Oncotarget, Vol.9, No.12, 10307-10316, 2017. (要約) Multiple myeloma (MM) remains incurable, and MM-initiating cells or MM progenitors are considered to contribute to disease relapse through their drug-resistant nature. In order to improve the therapeutic efficacy for MM, we recently developed novel superparamagnetic nanoparticles which selectively accumulate in MM tumors and extirpate them by heat generated with magnetic resonance. We here aimed to clarify the therapeutic effects on MM cells and their progenitors by hyperthermia. Heat treatment at 43°C time-dependently induced MM cell death. The treatment upregulated endoplasmic reticulum (ER) stress mediators, ATF4 and CHOP, while reducing the protein levels of Pim-2, IRF4, c-Myc and Mcl-1. Combination with the proteasome inhibitor bortezomib further enhanced ER stress to potentiate MM cell death. The Pim inhibitor SMI-16a also enhanced the reduction of the Pim-2-driven survival factors, IRF4 and c-Myc, in combination with the heat treatment. The heat treatment almost completely eradicated "side population" fractions in RPMI8226 and KMS-11 cells and suppressed their clonogenic capacity as determined by colony formation and tumorigenic capacity in SCID mice. These results collectively demonstrated that hyperthermia is able to impair clonogenic drug-resistant fractions of MM cells and enhance their susceptibility to chemotherapeutic drugs. (徳島大学機関リポジトリ) ● Metadata: 113059 (出版サイトへのリンク) ● Publication site (DOI): 10.18632/oncotarget.23121 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29535808 ● Summary page in Scopus @ Elsevier: 2-s2.0-85041952629 (徳島大学機関リポジトリ: 113059, DOI: 10.18632/oncotarget.23121, PubMed: 29535808, Elsevier: Scopus)
24.	Ogawa Yasuhiro, Sano Takafumi, Irisa Masahiro, Kodama Takashi, Saito Takahiro, Furusawa Eiri, Kaizu Katsutoshi, Yanagi Yusuke, Tsukimura Takahiro, Togawa Tadayasu, Yamanaka Shoji, Kouji Itou, Sakuraba Hitoshi and Oishi Kazuhiko : FcR-dependent immune activation initiates astrogliosis during the asymptomatic phase of Sandhoff disease model mice., Scientific Reports, Vol.7, 40518, 2017. (要約) Sandhoff disease (SD) is caused by the loss of β-hexosaminidase (Hex) enzymatic activity in lysosomes resulting from Hexb mutations. In SD patients, the Hex substrate GM2 ganglioside accumulates abnormally in neuronal cells, resulting in neuronal loss, microglial activation, and astrogliosis. Hexb mice, which manifest a phenotype similar to SD, serve as animal models for examining the pathophysiology of SD. Hexb mice reach ~8 weeks without obvious neurological defects; however, trembling begins at 12 weeks and is accompanied by startle reactions and increased limb tone. These symptoms gradually become severe by 16-18 weeks. Immune reactions caused by autoantibodies have been recently associated with the pathology of SD. The inhibition of immune activation may represent a novel therapeutic target for SD. Herein, SD mice (Hexb) were crossed to mice lacking an activating immune receptor (FcRγ) to elucidate the potential relationship between immune responses activated through SD autoantibodies and astrogliosis. Microglial activation and astrogliosis were observed in cortices of Hexb mice during the asymptomatic phase, and were inhibited in Hexb FcRγ mice. Moreover, early astrogliosis and impaired motor coordination in Hexb mice could be ameliorated by immunosuppressants, such as FTY720. Our findings demonstrate the importance of early treatment and the therapeutic effectiveness of immunosuppression in SD. (徳島大学機関リポジトリ) ● Metadata: 112431 (出版サイトへのリンク) ● Publication site (DOI): 10.1038/srep40518 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28084424 ● Search Scopus @ Elsevier (PMID): 28084424 ● Search Scopus @ Elsevier (DOI): 10.1038/srep40518 (徳島大学機関リポジトリ: 112431, DOI: 10.1038/srep40518, PubMed: 28084424)
25.	Eri Kawakita, Daisuke Tsuji, Yosuke Kanno, Kaho Tsuchida and Kouji Itou : Enhancement by Uridine Diphosphate of Macrophage Inflammatory Protein-1 Alpha Production in Microglia Derived from Sandhoff Disease Model Mice., JIMD Reports, Vol.28, 85-93, 2016. (要約) Sandhoff disease (SD) is a lysosomal β-hexosaminidase (Hex) deficiency involving excessive accumulation of undegraded substrates, including GM2 ganglioside, and progressive neurodegeneration. Macrophage inflammatory protein-1α (MIP-1α) is a crucial factor for microglia-mediated neuroinflammation in the onset or progression of SD. However, the transmitter-mediated production of MIP-1α in SD is still poorly understood.Extracellular nucleotides, including uridine diphosphate (UDP), leaked by either injured or damaged neuronal cells activate microglia to trigger chemotaxis, phagocytosis, macropinocytosis, and cytokine production.In this study, we demonstrated that UDP enhanced the production of MIP-1α by microglia derived from SD mice (SD-Mg), but not that from wild-type mice (WT-Mg). The UDP-induced MIP-1α production was mediated by the activation of P2Y6 receptor, ERK, and JNK. We also found the amount of dimeric P2Y6 receptor protein to have increased in SD-Mg in comparison to WT-Mg. In addition, we demonstrated that the disruption of lipid rafts enhanced the effect of UDP on MIP-1α production and the disordered maintenance of the lipid rafts in SD-Mg. Thus, the accumulation of undegraded substrates might cause the enhanced effect of UDP in SD-Mg through the increased expression of the dimeric P2Y6 receptors and the disordered maintenance of the lipid rafts. These findings provide new insights into the pathogenic mechanism and therapeutic strategies for SD. (出版サイトへのリンク) ● Publication site (DOI): 10.1007/8904_2015_496 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26545879 ● Search Scopus @ Elsevier (PMID): 26545879 ● Search Scopus @ Elsevier (DOI): 10.1007/8904_2015_496 (DOI: 10.1007/8904_2015_496, PubMed: 26545879)
26.	Keisuke Kitakaze, Chikako Tasaki, Youichi Tajima, Takatsugu Hirokawa, Daisuke Tsuji, Hitoshi Sakuraba and Kouji Itou : Combined replacement effects of human modified -hexosaminidase B and GM2 activator protein on GM2 gangliosidoses fibroblasts, Biochemistry and Biophysics Reports, No.7, 157-163, 2016. (徳島大学機関リポジトリ) ● Metadata: 115018 (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbrep.2016.04.012 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrep.2016.04.012 (徳島大学機関リポジトリ: 115018, DOI: 10.1016/j.bbrep.2016.04.012)
27.	Takahiro Nakamura, Kohei Sato, Naoto Naruse, Keisuke Kitakaze, Tsubasa Inokuma, Takatsugu Hirokawa, Akira Shigenaga, Kouji Itou and Akira Otaka : Back Cover: Tailored synthesis of 162-residue S-monoglycosylated GM2-activator protein (GM2AP) analogues that allows access to protein library, ChemBioChem, Vol.17, No.20, 1994, 2016. (出版サイトへのリンク) ● Publication site (DOI): 10.1002/cbic.201600521 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1002/cbic.201600521 (DOI: 10.1002/cbic.201600521)
28.	Takahiro Nakamura, Kohei Sato, Naoto Naruse, Keisuke Kitakaze, Tsubasa Inokuma, Takatsugu Hirokawa, Akira Shigenaga, Kouji Itou and Akira Otaka : Tailored synthesis of 162-residue S-monoglycosylated GM2-activator protein (GM2AP) analogues that allows access to protein library, ChemBioChem, Vol.17, No.20, 1986-1992, 2016. (徳島大学機関リポジトリ) ● Metadata: 111880 (出版サイトへのリンク) ● Publication site (DOI): 10.1002/cbic.201600400 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27428709 ● Summary page in Scopus @ Elsevier: 2-s2.0-84991661622 (徳島大学機関リポジトリ: 111880, DOI: 10.1002/cbic.201600400, PubMed: 27428709, Elsevier: Scopus)
29.	Takuya Morisaki, Masaya Denda, Jun Yamamoto, Daisuke Tsuji, Kouji Itou, Tsubasa Inokuma, Akira Shigenaga and Akira Otaka : An N-Sulfanylethylanilide-based traceable linker for enrichment and selective labelling of target proteins, Chemical Communications, Vol.52, 6911-6913, 2016. (徳島大学機関リポジトリ) ● Metadata: 111925 (出版サイトへのリンク) ● Publication site (DOI): 10.1039/C6CC01229A (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1039/C6CC01229A (徳島大学機関リポジトリ: 111925, DOI: 10.1039/C6CC01229A)
30.	Kitakaze Keisuke, Mizutani Yasumichi, Sugiyama Eiji, Tasaki Chikako, Daisuke Tsuji, Nobuo Maita, Hirokawa Takatsugu, Asanuma Daisuke, Kamiya Mako, Sato Kohei, Setou Mitsutoshi, Urano Yasuteru, Togawa Tadayasu, Akira Otaka, Sakuraba Hitoshi and Kouji Itou : Protease-resistant modified human β-hexosaminidase B ameliorates symptoms in GM2 gangliosidosis model, The Journal of Clinical Investigation, Vol.126, No.5, 1691-1703, 2016. (要約) GM2 gangliosidoses, including Tay-Sachs and Sandhoff diseases, are neurodegenerative lysosomal storage diseases that are caused by deficiency of β-hexosaminidase A, which comprises an αβ heterodimer. There are no effective treatments for these diseases; however, various strategies aimed at restoring β-hexosaminidase A have been explored. Here, we produced a modified human hexosaminidase subunit β (HexB), which we have termed mod2B, composed of homodimeric β subunits that contain amino acid sequences from the α subunit that confer GM2 ganglioside-degrading activity and protease resistance. We also developed fluorescent probes that allow visualization of endocytosis of mod2B via mannose 6-phosphate receptors and delivery of mod2B to lysosomes in GM2 gangliosidosis models. In addition, we applied imaging mass spectrometry to monitor efficacy of this approach in Sandhoff disease model mice. Following i.c.v. administration, mod2B was widely distributed and reduced accumulation of GM2, asialo-GM2, and bis(monoacylglycero)phosphate in brain regions including the hypothalamus, hippocampus, and cerebellum. Moreover, mod2B administration markedly improved motor dysfunction and a prolonged lifespan in Sandhoff disease mice. Together, the results of our study indicate that mod2B has potential for intracerebrospinal fluid enzyme replacement therapy and should be further explored as a gene therapy for GM2 gangliosidoses. (出版サイトへのリンク) ● Publication site (DOI): 10.1172/JCI85300 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27018595 ● Search Scopus @ Elsevier (PMID): 27018595 ● Search Scopus @ Elsevier (DOI): 10.1172/JCI85300 (DOI: 10.1172/JCI85300, PubMed: 27018595)
31.	Kohei Sato, Keisuke Kitakaze, Takahiro Nakamura, Naoto Naruse, Keisuke Aihara, Akira Shigenaga, Tsubasa Inokuma, Daisuke Tsuji, Kouji Itou and Akira Otaka : The total chemical synthesis of the monoglycosylated GM2 ganglioside activator using a novel cysteine surrogate, Chemical Communications, Vol.51, No.49, 9946-9948, 2015. (要約) We describe a novel peptide ligation/desulfurization strategy using a -mercapto-N-glycosylated asparagine derivative. The newly developed procedure was successfully applied to the total chemical synthesis of the GM2 ganglioside activator protein bearing a monosaccharide on the native glycosylation site. (徳島大学機関リポジトリ) ● Metadata: 111882 (出版サイトへのリンク) ● Publication site (DOI): 10.1039/C5CC02967H (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26006093 ● Summary page in Scopus @ Elsevier: 2-s2.0-84931274683 (徳島大学機関リポジトリ: 111882, DOI: 10.1039/C5CC02967H, PubMed: 26006093, Elsevier: Scopus)
32.	Yusuke Tsuda, Akira Shigenaga, Masaya Denda, Kohei Sato, Keisuke Kitakaze, Takahiro Nakamura, Tsubasa Inokuma, Kouji Itou and Akira Otaka : Development of chemical methodology for preparation of peptide thioesters applicable to naturally occurring peptides using a sequential quadruple acyl transfer system, ChemistryOpen, Vol.4, No.4, 448-452, 2015. (徳島大学機関リポジトリ) ● Metadata: 111883 (出版サイトへのリンク) ● Publication site (DOI): 10.1002/open.201500086 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-84942501459 (徳島大学機関リポジトリ: 111883, DOI: 10.1002/open.201500086, Elsevier: Scopus)
33.	Gallat Francois-Xavier, Matsugaki Naihiro, P. Coussens Nathan, Yagi J. koichiro, Boudes Marion, Higashi Tetsuya, Daisuke Tsuji, Tatano Yutaka, Suzuki Mamoru, Mizohata Eiichi, Tono Kensuke, Hatui Yasumasa, Yabashi Makina, Nango Eriko, Kouji Itou, Coulibaly Fasseli, Tobe Stephen, Ramaswamy S., Iwata So and Chavas M. Leonard : In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?, Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, Vol.369, No.1647, 20130497, 2014. (要約) The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography. (キーワード) Animals / Biology / CHO Cells / Cockroaches / Cricetinae / Cricetulus / Crystallography, X-Ray / Electrons / Humans / Lasers / Nanoparticles / Proteins / X-Ray Diffraction (出版サイトへのリンク) ● Publication site (DOI): 10.1098/rstb.2013.0497 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24914164 ● Search Scopus @ Elsevier (PMID): 24914164 ● Search Scopus @ Elsevier (DOI): 10.1098/rstb.2013.0497 (DOI: 10.1098/rstb.2013.0497, PubMed: 24914164)
34.	Masahiro Hiasa, Jumpei Teramachi, A Oda, Ryota Amachi, T Harada, Shingen Nakamura, Hirokazu Miki, Shiroh Fujii, Kumiko Kagawa, Keiichiro Watanabe, Itsuro Endo, Y Kuroda, T Yoneda, Daisuke Tsuji, Michiyasu Nakao, Eiji Tanaka, Kenichi Hamada, Shigeki Sano, Kouji Itou, Toshio Matsumoto and Masahiro Abe : Pim-2 kinase is an important target of treatment for tumor progression and bone loss in myeloma., Leukemia, 2014. (要約) Pim-2 kinase is overexpressed in multiple myeloma (MM) cells to enhance their growth and survival, and regarded as a novel therapeutic target in MM. However, the impact of Pim-2 inhibition on bone disease in MM remains unknown. We demonstrated here that Pim-2 expression was also upregulated in bone marrow stromal cells and MC3T3-E1 preosteoblastic cells in the presence of cytokines known as the inhibitors of osteoblastogenesis in MM, including interleukin-3 (IL-3), IL-7, tumor necrosis factor-, transforming growth factor- (TGF-) and activin A, as well as MM cell conditioned media. The enforced expression of Pim-2 abrogated in vitro osteoblastogenesis by BMP-2, which suggested Pim-2 as a negative regulator for osteoblastogenesis. Treatment with Pim-2 short-interference RNA as well as the Pim inhibitor SMI-16a successfully restored osteoblastogenesis suppressed by all the above inhibitory factors and MM cells. The SMI-16a treatment potentiated BMP-2-mediated anabolic signaling while suppressing TGF- signaling. Furthermore, treatment with the newly synthesized thiazolidine-2,4-dione congener, 12a-OH, as well as its prototypic SMI-16a effectively prevented bone destruction while suppressing MM tumor growth in MM animal models. Thus, Pim-2 may have a pivotal role in tumor progression and bone loss in MM, and Pim-2 inhibition may become an important therapeutic strategy to target the MM cell-bone marrow interaction.Leukemia advance online publication, 30 May 2014; doi:10.1038/leu.2014.147. (出版サイトへのリンク) ● Publication site (DOI): 10.1038/leu.2014.147 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24787487 ● Search Scopus @ Elsevier (PMID): 24787487 ● Search Scopus @ Elsevier (DOI): 10.1038/leu.2014.147 (DOI: 10.1038/leu.2014.147, PubMed: 24787487)
35.	Takeshi Harada, Shuji Ozaki, Asuka Oda, Daisuke Tsuji, Akishige Ikegame, Masami Iwasa, Kengo Udaka, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Yoshiaki Kuroda, Shigeto Kawai, Kouji Itou, Hisafumi Yamada-Okabe, Toshio Matsumoto and Masahiro Abe : Combination with a Defucosylated Anti-HM1.24 Monoclonal Antibody plus Lenalidomide Induces Marked ADCC against Myeloma Cells and Their Progenitors, PLoS ONE, Vol.8, No.12, e83905, 2013. (要約) The immunomodulatory drug lenalidomide (Len) has drawn attention to potentiate antibody-dependent cellular cytotoxicity (ADCC)-mediated immunotherapies. We developed the defucosylated version (YB-AHM) of humanized monoclonal antibody against HM1.24 (CD317) overexpressed in multiple myeloma (MM) cells. In this study, we evaluated ADCC by YB-AHM and Len in combination against MM cells and their progenitors. YB-AHM was able to selectively kill via ADCC MM cells in bone marrow samples from patients with MM with low effector/target ratios, which was further enhanced by treatment with Len. Interestingly, Len also up-regulated HM1.24 expression on MM cells in an effector-dependent manner. HM1.24 was found to be highly expressed in a drug-resistant clonogenic "side population" in MM cells; and this combinatory treatment successfully reduced SP fractions in RPMI 8226 and KMS-11 cells in the presence of effector cells, and suppressed a clonogenic potential of MM cells in colony-forming assays. Collectively, the present study suggests that YB-AHM and Len in combination may become an effective therapeutic strategy in MM, warranting further study to target drug-resistant MM clonogenic cells. (キーワード) Aged / Aged, 80 and over / Antibodies, Monoclonal, Humanized / Antibody-Dependent Cell Cytotoxicity / Antigens, CD / Antineoplastic Combined Chemotherapy Protocols / Cell Line, Tumor / Drug Synergism / Female / GPI-Linked Proteins / Glycosylation / Humans / 免疫療法 (immunotherapy) / Lenalidomide / Male / Middle Aged / Multiple Myeloma / Neoplastic Stem Cells / Side-Population Cells / Thalidomide / Up-Regulation (徳島大学機関リポジトリ) ● Metadata: 106068 (出版サイトへのリンク) ● Publication site (DOI): 10.1371/journal.pone.0083905 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24386306 ● Summary page in Scopus @ Elsevier: 2-s2.0-84891280322 (徳島大学機関リポジトリ: 106068, DOI: 10.1371/journal.pone.0083905, PubMed: 24386306, Elsevier: Scopus)
36.	Kohei Sato, Akira Shigenaga, Keisuke Kitakaze, Ken Sakamoto, Daisuke Tsuji, Kouji Itou and Akira Otaka : Chemical synthesis of biologically active monoglycosylated GM2-activator protein analog using N-sulfanylethylanilide peptide, Angewandte Chemie International Edition, Vol.52, No.30, 7855-7859, 2013. (要約) Going to SEA(lide): Total chemical synthesis of a 162-residue glycoprotein analogue of the monoglycosylated human GM2-activator protein (GM2AP) was achieved. Key steps were the use of N-sulfanylethylanilide (SEAlide) peptides in the kinetic chemical ligation synthesis of a large peptide fragment, and a convergent native chemical ligation for final fragment assembly. (キーワード) Amino Acid Sequence / Anilides / G(M2) Activator Protein / G(M2) Ganglioside / Glycosylation / Humans / Kinetics / Molecular Sequence Data / Peptide Fragments / Sulfhydryl Compounds (出版サイトへのリンク) ● Publication site (DOI): 10.1002/anie.201303390 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23765733 ● Summary page in Scopus @ Elsevier: 2-s2.0-84880361310 (DOI: 10.1002/anie.201303390, PubMed: 23765733, Elsevier: Scopus)
37.	Yusaku Kikuchi, Naoshi Yamazaki, Noriko Tarashima, Kazuhiro Furukawa, Yoshiharu Takiguchi, Kouji Itou and Noriaki Minakawa : Gene suppression via U1 small nuclear RNA interference (U1i) machinery using oligonucleotides containing 2'-modified-4'-thionucleosides, Bioorganic & Medicinal Chemistry, Vol.21, No.17, 5292-5296, 2013. (要約) Gene suppression via U1 small nuclear RNA interference (U1i) is considered to be one of the most attractive approaches, and takes the place of general antisense, RNA interference (RNAi), and anti-micro RNA machineries. Since the U1i can be induced by short oligonucleotides (ONs), namely U1 adaptors consisting of a 'target domain' and a 'U1 domain', we prepared adaptor ONs using 2'-modified-4'-thionucleosides developed by our group, and evaluated their U1i activity. As a result, the desired gene suppression via U1i was observed in ONs prepared as a combination of 2'-fluoro-4'-thionucleoside and 2'-fluoronucleoside units as well as only 2'-fluoronucleoside units, while those prepared as combination of 2'-OMe nucleoside/2'-OMe-4'-thionucleoside and 2'-fluoronucleoside units did not show significant activity. Measurement of Tm values indicated that a higher hybridization ability of adaptor ONs with complementary RNA is one of the important factors to show potent U1i activity. (徳島大学機関リポジトリ) ● Metadata: 113344 (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bmc.2013.06.023 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23871495 ● Search Scopus @ Elsevier (PMID): 23871495 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bmc.2013.06.023 (徳島大学機関リポジトリ: 113344, DOI: 10.1016/j.bmc.2013.06.023, PubMed: 23871495)
38.	MM Rahman, Daisuke Tsuji, K Suzuki, J Sakamoto, K Matsuoka, F Matsuzawa, S Aikawa and Kouji Itou : Inhibitory effects and specificity of synthetic sialyldendrimers toward recombinant human cytosolic sialidase 2 (NEU2)., Glycobiology, Vol.23, No.4, 495-504, 2013. (要約) Human sialidase 2 (NEU2) is a cytoplasmic sialidase that degrades sialylglycoconjugates, including glycoproteins and gangliosides, via hydrolysis of terminal sialic acids to produce asialo-type molecules. Here, we first report the inhibitory effects of a series of synthetic sialyldendrimers comprising three types [Dumbbell(1)6-S-Neu5Ac(6), Fan(0)3-S-Neu5Ac(3) and Ball(0)4-S-NeuAc(4)] toward recombinant human NEU2 in vitro. Among them, Dumbbell(1)6-S-Neu5Ac(6) exhibited the most potent inhibitory activity (concentration causing 50% inhibition (IC(50)), 0.4 ∼ 0.5 mM). In addition, NeuSLac and NeuSCel carrying thiosialyltrisaccharide moieties exhibited more potent inhibitory effects than NeuSGal and NeuSGlc carrying thiosialyldisaccharides. Docking models composed of NEU2 and the thiosialyloligosaccharide suggested that the active pocket of NEU2 prefers the second galactose-β (Galβ) to the glucose-β (Glcβ) residue in the trisaccharide structure, there being a hydrogen bond between the 4-hydroxy group of the second Galβ and the side chain of the D46 residue of NEU2. The third Glcβ residues of NeuSLac and NeuSCel were also predicted to be stabilized by hydrogen bonds with the side chains of the R21, R304, D358 and Y359 residues of NEU2. NEU2 mutants (D358A and Y359A) exhibited reduced affinity for NeuSLac carrying thiosialyltrisaccharide moieties, suggesting the significant roles of D358 and Y359 residues in recognition of thiosialyltrisaccharide moieties of NeuSLac bound in the active pocket of NEU2. Thus, the present sialyldendrimers could be utilized not only as a new class of NEU2 inhibitors but also as molecular probes for evaluating the biological functions of NEU2, including the catalytic activity and mechanism as to natural substrates carrying sialyloligosaccharides. (キーワード) Amino Acid Sequence / Binding Sites / Carbohydrate Sequence / Dendrimers / Enzyme Inhibitors / Galactose / Glucose / Hydrogen Bonding / Molecular Docking Simulation / Molecular Sequence Data / Mutation, Missense / N-Acetylneuraminic Acid / Neuraminidase / Recombinant Proteins / Substrate Specificity / Trisaccharides (出版サイトへのリンク) ● Publication site (DOI): 10.1093/glycob/cws221 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23363739 ● Search Scopus @ Elsevier (PMID): 23363739 ● Search Scopus @ Elsevier (DOI): 10.1093/glycob/cws221 (DOI: 10.1093/glycob/cws221, PubMed: 23363739)
39.	Seiji Hitaoka, Yuto Shibata, Hiroshi Matoba, Akihiro Kawano, Masataka Harada, Rahman Motiur M, Daisuke Tsuji, Takatsugu Hirokawa, Kouji Itou, Tatsusada Yoshida and Hiroshi Chuman : Modeling of Human Neuraminidase-1 and Its Validation by LERE-Correlation Analysis, Chem-Bio Informatics Journal, Vol.13, 30-40, 2013. (要約) Four human neuraminidases (hNEUs1-4) have been identified. Among them, hNEU1 has been studied extensively as a target for sialidosis. It has been desired to understand the biological functions of hNEU1 at the molecular and atomic levels. The three-dimensional structure of hNEU1 is not known at present. In the present work, we constructed a three-dimensional structure of hNEU1 by homology modeling, and then performed correlation analyses between observed and calculated free-energy changes (quantitative structure-activity relationship (QSAR) analyses), coupled with LERE (linear expression by representative energy terms) procedure using the modeled three-dimensional structure in order to confirm the validity of the modeled structure. The atomic coordinates of all atoms in the verified model of hNEU1 are available. The proposed structure of hNEU1 will be useful and helpful for further studies concerning the biological and chemical functions of hNEU1. The present article is one of continuous works derived from the one that won the CBI Award for the best presentation in the CBI/JSBi 2011 Joint Conference (presented by Seiji Hitaoka). (キーワード) 抗インフルエンザ剤 / ホモロジーモデリング / ヒト・ノイラミニダーゼ-1 / 代表エネルギー項による自由エネルギーの線形表現 / 定量的構造活性相関 / シアル酸アナログ (出版サイトへのリンク) ● Publication site (DOI): 10.1273/cbij.13.30 (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1390001205102817664 ● Search Scopus @ Elsevier (DOI): 10.1273/cbij.13.30 (DOI: 10.1273/cbij.13.30, CiNii: 1390001205102817664)
40.	Akishige Ikegame, Shuji Ozaki, Daisuke Tsuji, T harada, Tatsuya Fujii, S Nakamura, H Miki, A Nakano, K Kagawa, K Takeuchi, M Abe, K Watanabe, M Hiasa, N Kimura, Y Kikuchi, A Sakamoto, K Habu, M Endo, Kouji Itou, H Yamada-Okabe and T Matsumoto : Small molecule antibody targeting HLA class I inhibits myeloma cancer stem cells by repressing pluripotency-associated transcription factors., Leukemia, Vol.26, No.9, 2124-2134, 2012. (要約) Cancer stem cells have been proposed to be responsible for tumorigenesis and recurrence in various neoplastic diseases, including multiple myeloma (MM). We have previously reported that MM cells specifically express HLA class I at high levels and that single-chain Fv diabody against this molecule markedly induces MM cell death. Here we investigated the effect of a new diabody (C3B3) on cancer stem cell-like side population (SP) cells. SP fraction of MM cells highly expressed ABCG2 and exhibited resistance to chemotherapeutic agents; however, C3B3 induced cytotoxicity in both SP cells and main population (MP) cells to a similar extent. Moreover, C3B3 suppressed colony formation and tumorigenesis of SP cells in vitro and in vivo. Crosslinking of HLA class I by C3B3 mediated disruption of lipid rafts and actin aggregation, which led to inhibition of gene expression of -catenin and pluripotency-associated transcription factors such as Sox2, Oct3/4 and Nanog. Conversely, knockdown of Sox2 and Oct3/4 mRNA reduced the proportion of SP cells, suggesting that these factors are essential in maintenance of SP fraction in MM cells. Thus, our findings reveal that immunotherapeutic approach by engineered antibodies can overcome drug resistance, and provide a new basis for development of cancer stem cell-targeted therapy. (キーワード) ATP-Binding Cassette Transporters / Animals / Antineoplastic Agents / Blotting, Western / Cell Line, Tumor / Cell Proliferation / Flow Cytometry / HLA Antigens / Humans / Immunoenzyme Techniques / Mice / Mice, SCID / Multiple Myeloma / Neoplasm Proteins / Neoplastic Stem Cells / RNA, Messenger / Real-Time Polymerase Chain Reaction / Reverse Transcriptase Polymerase Chain Reaction / Side-Population Cells / Single-Chain Antibodies / beta Catenin (出版サイトへのリンク) ● Publication site (DOI): 10.1038/leu.2012.78 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22430632 ● Search Scopus @ Elsevier (PMID): 22430632 ● Search Scopus @ Elsevier (DOI): 10.1038/leu.2012.78 (DOI: 10.1038/leu.2012.78, PubMed: 22430632)
41.	Takashi Kodama, Tadayasu Togawa, Takahiro Tsukimura, Ikuo Kawashima, Kazuhiko Matsuoka, Keisuke Kitakaze, Daisuke Tsuji, Kouji Itou, Yo-Ichi Ishida, Minoru Suzuki, Toshihiro Suzuki and Hitoshi Sakuraba : Lyso-GM2 ganglioside: a possible biomarker of Tay-Sachs disease and Sandhoff disease., PLoS ONE, Vol.6, No.12, 2011. (要約) To find a new biomarker of Tay-Sachs disease and Sandhoff disease. The lyso-GM2 ganglioside (lyso-GM2) levels in the brain and plasma in Sandhoff mice were measured by means of high performance liquid chromatography and the effect of a modified hexosaminidase (Hex) B exhibiting Hex A-like activity was examined. Then, the lyso-GM2 concentrations in human plasma samples were determined. The lyso-GM2 levels in the brain and plasma in Sandhoff mice were apparently increased compared with those in wild-type mice, and they decreased on intracerebroventricular administration of the modified Hex B. The lyso-GM2 levels in plasma of patients with Tay-Sachs disease and Sandhoff disease were increased, and the increase in lyso-GM2 was associated with a decrease in Hex A activity. Lyso-GM2 is expected to be a potential biomarker of Tay-Sachs disease and Sandhoff disease. (キーワード) Adult / Animals / Biological Markers / Brain / G(M2) Activator Protein / G(M2) Ganglioside / Hexosaminidases / Humans / Infant / Mice / Sandhoff Disease / Tay-Sachs Disease (出版サイトへのリンク) ● Publication site (DOI): 10.1371/journal.pone.0029074 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22205997 ● Search Scopus @ Elsevier (PMID): 22205997 ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0029074 (DOI: 10.1371/journal.pone.0029074, PubMed: 22205997)
42.	Ayako Nakano, Daisuke Tsuji, Hirokazu Miki, Qu Cui, Mohamed Sayed Salah El, Akishige Ikegame, Asuka Oda, Hiroe Amou, Shingen Nakamura, Takeshi Harada, Shiro Fujii, Kumiko Kagawa, Kyoko Takeuchi, Akira Sakai, Shuji Ozaki, Kazuma Okano, Takahiro Nakamura, Kouji Itou, Toshio Matsumoto and Masahiro Abe : Glycolysis inhibition inactivates ABC transporters to restore drug sensitivity in malignant cells., PLoS ONE, Vol.6, No.11, 2011. (要約) Cancer cells eventually acquire drug resistance largely via the aberrant expression of ATP-binding cassette (ABC) transporters, ATP-dependent efflux pumps. Because cancer cells produce ATP mostly through glycolysis, in the present study we explored the effects of inhibiting glycolysis on the ABC transporter function and drug sensitivity of malignant cells. Inhibition of glycolysis by 3-bromopyruvate (3BrPA) suppressed ATP production in malignant cells, and restored the retention of daunorubicin or mitoxantrone in ABC transporter-expressing, RPMI8226 (ABCG2), KG-1 (ABCB1) and HepG2 cells (ABCB1 and ABCG2). Interestingly, although side population (SP) cells isolated from RPMI8226 cells exhibited higher levels of glycolysis with an increased expression of genes involved in the glycolytic pathway, 3BrPA abolished Hoechst 33342 exclusion in SP cells. 3BrPA also disrupted clonogenic capacity in malignant cell lines including RPMI8226, KG-1, and HepG2. Furthermore, 3BrPA restored cytotoxic effects of daunorubicin and doxorubicin on KG-1 and RPMI8226 cells, and markedly suppressed subcutaneous tumor growth in combination with doxorubicin in RPMI8226-implanted mice. These results collectively suggest that the inhibition of glycolysis is able to overcome drug resistance in ABC transporter-expressing malignant cells through the inactivation of ABC transporters and impairment of SP cells with enhanced glycolysis as well as clonogenic cells. (キーワード) ATP-Binding Cassette Transporters / Adenosine Triphosphate / Antineoplastic Agents / Base Sequence / Cell Line, Tumor / DNA Primers / Daunorubicin / Doxorubicin / Flow Cytometry / Glycolysis / Humans / Mitoxantrone / Real-Time Polymerase Chain Reaction (出版サイトへのリンク) ● Publication site (DOI): 10.1371/journal.pone.0027222 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22073292 ● Search Scopus @ Elsevier (PMID): 22073292 ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0027222 (DOI: 10.1371/journal.pone.0027222, PubMed: 22073292)
43.	Seiji Hitaoka, Hiroshi Matoba, Masataka Harada, Tatsusada Yoshida, Takatsugu Hirokawa, Kouji Itou and Hiroshi Chuman : Correlation Analyses on Binding Affinity of Sialic Acid Analogues and Antiinfluenza Drugs with Human Neuraminidase Using ab Initio MO Calculations on Their Complex Structures - LERE-QSAR Analysis (IV), Journal of Chemical Information and Modeling, Vol.51, No.10, 2706-2716, 2011. (要約) We carried out full ab initio fragment molecular orbital (FMO) calculations for complexes comprising human neuraminidase-2 (hNEU2) and sialic acid analogues including anti-influenza drugs zanamivir (Relenza) and oseltamivir (Tamiflu) in order to examine the variation in the observed inhibitory activity toward hNEU2 at the atomic and electronic levels. We recently proposed the LERE (linear expression by representative energy terms)-QSAR (quantitative structure-activity relationship) procedure. LERE-QSAR analysis quantitatively revealed that the complex formation is driven by hydrogen-bonding and electrostatic interaction of hNEU2 with sialic acid analogues. The most potent inhibitory activity, that of zanamivir, is attributable to the strong electrostatic interaction of a positively charged guanidino group in zanamivir with negatively charged amino acid residues in hNEU2. After we confirmed that the variation in the observed inhibitory activity among sialic acid analogues is excellently reproducible with the LERE-QSAR equation, we examined the reason for the remarkable difference between the inhibitory potencies of oseltamivir as to hNEU2 and influenza A virus neuraminidase-1 (N1-NA). Several amino acid residues in close contact with a positively charged amino group in oseltamivir are different between hNEU2 and N1-NA. FMO-IFIE (interfragment interaction energy) analysis showed that the difference in amino acid residues causes a remarkably large difference between the overall interaction energies of oseltamivir with hNEU2 and N1-NA. The current results will be useful for the development of new anti-influenza drugs with high selectivity and without the risk of adverse side effects. (キーワード) Antiviral Agents / Electrons / Humans / Influenza A virus / 分子動力学シミュレーション (molecular dynamics simulation) / N-Acetylneuraminic Acid / Neuraminidase / Protein Binding / Protein Conformation / Quantitative Structure-Activity Relationship / 量子論 (quantum theory) / Static Electricity / 熱力学 (thermodynamics) / Zanamivir (出版サイトへのリンク) ● Publication site (DOI): 10.1021/ci2002395 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21870866 ● Summary page in Scopus @ Elsevier: 2-s2.0-80054930148 (DOI: 10.1021/ci2002395, PubMed: 21870866, Elsevier: Scopus)
44.	Nunuk Purwanti, Daisuke Tsuji, Ahmad Azlina, Mileva Ratko Karabasil, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi : Induction of Sca-1 in the duct cells of the mouse submandibular gland by obstruction of the main excretory duct, Journal of Oral Pathology & Medicine, Vol.40, No.8, 651-658, 2011. (要約) The effect of ligation of the main excretory duct (MED) of the mouse submandibular gland (SMG) on the expression of Sca-1, a stem cell antigen, was examined by Western blotting and immunohistochemistry. By Western blotting, the expression of Sca-1 with a molecular weight of 18 kDa was identified in the normal gland. At 1 day post-ligation, the expression level of Sca-1 was strongly increased in the experimental gland and weakly in the contralateral gland, and such expression in both glands decreased at 6 days. By immunohistochemistry, Sca-1 was detected weakly in the apical membrane of excretory duct (ED) cells of the SMG under the normal condition. By duct ligation, Sca-1 became expressed strongly in most cells of the two major duct systems, i.e., the striated duct (SD) and granular convoluted tubules (GCT), but was not detected in the acinar (Ac) cells. By fluorescence-activated cell sorter (FACS) analysis, the number of side population (SP) cells in this gland was found to be increased by ligation. These results imply that Sca-1-positive cells may have a role in the duct cell proliferation in the regeneration step elicited by MED ligation-induced injury. (キーワード) Animals / Antigens, Ly / Cell Count / Cell Proliferation / Ligation / Male / Membrane Proteins / Mice / Mice, Inbred C57BL / Regeneration / Salivary Ducts / Salivation / Side-Population Cells / Submandibular Gland (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1600-0714.2011.01011.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21884259 ● Search Scopus @ Elsevier (PMID): 21884259 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1600-0714.2011.01011.x (DOI: 10.1111/j.1600-0714.2011.01011.x, PubMed: 21884259)
45.	Rumi Kawabata, Shinji Oie, Masayuki Takahashi, Hiro-omi Kanayama, Toshinori Oka and Kouji Itou : Up-regulation of insulin-like growth factor-binding protein 3 by 5-fluorouracil (5-FU) leads to the potent anti-proliferative effect of androgen deprivation therapy combined with 5-FU in human prostate cancer cell lines., International Journal of Oncology, Vol.38, No.6, 1489-1500, 2011. (要約) In this study, we investigated the synergistic mechanism of anti-androgen and 5-fluorouracil (5-FU) combination therapy against castration-resistant prostate cancer (CRPC). Four prostate cancer cell lines, LNCaP, 22Rv1, DU145 and PC3, were examined for their growth dependency on androgens and the insulin-like growth factor 1 (IGF1). We assessed the expression changes of certain growth factor receptors and regulating proteins when treated with 5-FU, and found that 5-FU increased the expression of the IGF-binding protein 3 (IGFBP3). Furthermore, 5-FU inhibited the phosphorylation of Akt and p70 S6K, while the knockdown of IGFBP3 reduced the levels of poly (ADP-ribose) polymerase cleaved by 5-FU in PC3 cells. Therefore, the up-regulation of IGFBP3 by 5-FU not only inhibits cell growth by reducing the IGF1 signal but also induces apoptosis in PC3 cells. The synergistic effect of bicalutamide and 5-FU on 22Rv1 cells was reduced by IGFBP3 gene silencing using small-interfering RNA. These results suggest that the up-regulation of IGFBP3 induced by 5-FU plays an important role in the potent anti-tumor effect of 5-FU combined with anti-androgens on CRPC. Androgen-deprivation therapy combined with 5-FU could therefore be an appropriate therapy for CRPC patients. (キーワード) Androgen Antagonists / Androgens / Anilides / Antineoplastic Agents / アポトーシス (apoptosis) / Cell Line, Tumor / Cell Proliferation / Drug Synergism / Fluorouracil / Gene Expression Profiling / Gene Expression Regulation, Neoplastic / Humans / Insulin-Like Growth Factor Binding Protein 3 / Insulin-Like Growth Factor I / Male / Nitriles / Prostatic Neoplasms / RNA Interference / Receptors, Growth Factor / Signal Transduction / Tosyl Compounds / Up-Regulation (出版サイトへのリンク) ● Publication site (DOI): 10.3892/ijo.2011.991 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21455575 ● Search Scopus @ Elsevier (PMID): 21455575 ● Search Scopus @ Elsevier (DOI): 10.3892/ijo.2011.991 (DOI: 10.3892/ijo.2011.991, PubMed: 21455575)
46.	Kazuhiko Matsuoka, Tomomi Tamura, Daisuke Tsuji, Yukie Dohzono, Keisuke Kitakaze, Kazuki Ohno, Seiji Saito, Hitoshi Sakuraba and Kouji Itou : Therapeutic Potential of Intracerebroventricular Replacement of Modified Human β-Hexosaminidase B for GM2 Gangliosidosis, Molecular Therapy, Vol.19, No.6, 1017-1024, 2011. (要約) To develop a novel enzyme replacement therapy for neurodegenerative Tay-Sachs disease (TSD) and Sandhoff disease (SD), which are caused by deficiency of β-hexosaminidase (Hex) A, we designed a genetically engineered HEXB encoding the chimeric human β-subunit containing partial amino acid sequence of the α-subunit by structure-based homology modeling. We succeeded in producing the modified HexB by a Chinese hamster ovary (CHO) cell line stably expressing the chimeric HEXB, which can degrade artificial anionic substrates and GM2 ganglioside in vitro, and also retain the wild-type (WT) HexB-like thermostability in the presence of plasma. The modified HexB was efficiently incorporated via cation-independent mannose 6-phosphate receptor into fibroblasts derived from Tay-Sachs patients, and reduced the GM2 ganglioside accumulated in the cultured cells. Furthermore, intracerebroventricular administration of the modified HexB to Sandhoff mode mice restored the Hex activity in the brains, and reduced the GM2 ganglioside storage in the parenchyma. These results suggest that the intracerebroventricular enzyme replacement therapy involving the modified HexB should be more effective for Tay-Sachs and Sandhoff than that utilizing the HexA, especially as a low-antigenic enzyme replacement therapy for Tay-Sachs patients who have endogenous WT HexB. (キーワード) Animals / CHO Cells / Cells, Cultured / Cricetinae / Cricetulus / G(M2) Ganglioside / Humans / Immunoblotting / Mice / Models, Molecular / Protein Structure, Secondary / Sandhoff Disease / Tay-Sachs Disease / beta-Hexosaminidase beta Chain (出版サイトへのリンク) ● Publication site (DOI): 10.1038/mt.2011.27 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21487393 ● Search Scopus @ Elsevier (PMID): 21487393 ● Search Scopus @ Elsevier (DOI): 10.1038/mt.2011.27 (DOI: 10.1038/mt.2011.27, PubMed: 21487393)
47.	Kazuhiko Matsuoka, Daisuke Tsuji, Takao Taki and Kouji Itou : Thymic involution and corticosterone level in Sandhoff disease model mice: new aspects the pathogenesis of GM2 gangliosidosis., Journal of Inherited Metabolic Disease, Vol.34, No.5, 1061-1068, 2011. (要約) Sandhoff disease (SD) is a lysosomal disease caused by a mutation of the HEXB gene associated with excessive accumulation of GM2 ganglioside (GM2) in lysosomes and neurological manifestations. Production of autoantibodies against the accumulated gangliosides has been reported to be involved in the progressive pathogenesis of GM2 gangliosidosis, although the underlying mechanism has not been fully elucidated. The thymus is the key organ in the acquired immune system including the development of autoantibodies. We showed here that thymic involution and an increase in cell death in the organ occur in SD model mice at a late stage of the pathogenesis. Dramatic increases in the populations of Annexin-V(+) cells and terminal deoxynucletidyl transferase dUTP nick end labeling (TUNEL) (+) cells were observed throughout the thymuses of 15-week old SD mice. Enhanced caspase-3/7 activation, but not that of caspase-1/4, -6 ,-8, or -9, was also demonstrated. Furthermore, the serum level of corticosterone, a potent inducer of apoptosis of thymocytes, was elevated during the same period of apoptosis. Our studies suggested that an increase in endocrine corticosterone may be one of the causes that accelerate the apoptosis of thymocytes leading to thymic involution in GM2 gangliosidosis, and thus can be used as a disease marker for evaluation of the thymic condition and disease progression. (キーワード) Age Factors / Animals / Apoptosis / Atrophy / Caspases / Corticosterone / Disease Models, Animal / Disease Progression / G(M2) Ganglioside / Mice / Mice, Inbred C57BL / Mice, Knockout / Phenotype / Sandhoff Disease / Thymus Gland / beta-Hexosaminidase alpha Chain (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s10545-011-9316-6 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21598013 ● Search Scopus @ Elsevier (PMID): 21598013 ● Search Scopus @ Elsevier (DOI): 10.1007/s10545-011-9316-6 (DOI: 10.1007/s10545-011-9316-6, PubMed: 21598013)
48.	Akira Shigenaga, Hiroko Hirakawa, Jun Yamamoto, Keiji Ogura, Masaya Denda, Keiko Yamaguchi, Daisuke Tsuji, Kouji Itou and Akira Otaka : Design and synthesis of caged ceramide: UV-responsive ceramide releasing system based on UV-induced amide bond cleavage followed by O-N acyl transfer, Tetrahedron, Vol.67, No.22, 3984-3990, 2011. (徳島大学機関リポジトリ) ● Metadata: 111907 (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.tet.2011.04.048 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1016/j.tet.2011.04.048 (徳島大学機関リポジトリ: 111907, DOI: 10.1016/j.tet.2011.04.048)
49.	Daisuke Tsuji, Hiromi Akeboshi, Kazuhiko Matsuoka, Hiroko Yasuoka, Eri Miyasaki, Yoshiko Kasahara, Ikuo Kawashima, Yasunori Chiba, Yoshifumi Jigami, Takao Taki, Hitoshi Sakuraba and Kouji Itou : Highly phosphomannosylated enzyme replacement therapy for GM2 gangliosidosis., Annals of Neurology, Vol.69, No.4, 691-701, 2011. (要約) Novel recombinant human lysosomal β-hexosaminidase A (HexA) was developed for enzyme replacement therapy (ERT) for Tay-Sachs and Sandhoff diseases, ie, autosomal recessive GM2 gangliosidoses, caused by HexA deficiency. A recombinant human HexA (Om4HexA) with a high mannose 6-phosphate (M6P)-type-N-glycan content, which was produced by a methylotrophic yeast strain, Ogataea minuta, overexpressing the OmMNN4 gene, was intracerebroventricularly (ICV) administered to Sandhoff disease model mice (Hexb / mice) at different doses (0.5-2.5 mg/kg), and then the replacement and therapeutic effects were examined. The Om4HexA was widely distributed across the ependymal cell layer, dose-dependently restored the enzyme activity due to uptake via cell surface cation-independent M6P receptor (CI-M6PR) on neural cells, and reduced substrates, including GM2 ganglioside (GM2), asialo GM2 (GA2), and oligosaccharides with terminal N-acetylglucosamine residues (GlcNAc-oligosaccharides), accumulated in brain parenchyma. A significant inhibition of chemokine macrophage inflammatory protein-1 α (MIP-1α) induction was also revealed, especially in the hindbrain (< 63%). The decrease in central neural storage correlated with an improvement of motor dysfunction as well as prolongation of the lifespan. This lysosome-directed recombinant human enzyme drug derived from methylotrophic yeast has the high therapeutic potential to improve the motor dysfunction and quality of life of the lysosomal storage diseases (LSDs) patients with neurological manifestations. We emphasize the importance of neural cell surface M6P receptor as a delivery target of neural cell-directed enzyme replacement therapy (NCDERT) for neurodegenerative metabolic diseases. (キーワード) Animals / Disease Models, Animal / Dose-Response Relationship, Drug / Enzyme Replacement Therapy / Gangliosidoses, GM2 / Hexosaminidase A / Hexosaminidase B / Humans / Injections, Intraventricular / Lysosomes / Mannose-6-Phosphate Isomerase / Mice / Mice, Knockout / Receptors, CCR1 / Recombinant Proteins / Sandhoff Disease / Tay-Sachs Disease / Treatment Outcome / Yeasts (出版サイトへのリンク) ● Publication site (DOI): 10.1002/ana.22262 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21520232 ● Search Scopus @ Elsevier (PMID): 21520232 ● Search Scopus @ Elsevier (DOI): 10.1002/ana.22262 (DOI: 10.1002/ana.22262, PubMed: 21520232)
50.	Eri Kawashita, Daisuke Tsuji, Masahiro Toyoshima, Yosuke Kanno, Hiroyuki Matsuno and Kouji Itou : Prostaglandin E2 Reverses Aberrant Production of an Inflammatory Chemokine by Microglia from Sandhoff Disease Model Mice through the cAMP-PKA Pathway, PLoS ONE, Vol.6, No.1, e16269, 2011. (要約) Sandhoff disease (SD) is a neurodegenerative lysosomal β-hexosaminidase (Hex) deficiency involving excessive accumulation of undegraded substrates, including terminal GlcNAc-oligosaccharides and GM2 ganglioside. Microglia-mediated neuroinflammation contributes to the pathogenesis and progression of SD. Our previous study demonstrated that MIP-1α, a putative pathogenic factor for SD, is up-regulated in microglial cells derived from SD model mice (SD-Mg) through activation of Akt and JNK. In this study, we first demonstrated that prostaglandin E2 (PGE2), which is one of the lipid mediators derived from arachidonic acid and is known to suppress activation of microglia, reduced the aberrant MIP-1α production by SD-Mg to the same level as by WT-Mg. PGE2 also attenuated the activation of Akt and JNK. The inhibition of MIP-1α production and the activation of Akt and JNK occurred through the EP2 and 4/cAMP/PKA signaling pathway in the murine microglia derived from SD model mice. We propose that PGE2 plays a role as a negative regulator of MIP-1α production in the pathogenesis of SD, and that PGE2-EP2 and 4/cAMP/PKA signaling could be a target pathway for therapy for SD. (キーワード) Animals / Chemokine CCL3 / Chemokines / Cyclic AMP-Dependent Protein Kinases / Dinoprostone / Disease Models, Animal / Inflammation / Mice / Microglia / Sandhoff Disease / Signal Transduction (出版サイトへのリンク) ● Publication site (DOI): 10.1371/journal.pone.0016269 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21298000 ● Search Scopus @ Elsevier (PMID): 21298000 ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0016269 (DOI: 10.1371/journal.pone.0016269, PubMed: 21298000)
51.	Rumi Kawabata, Shinji Oie, Toshinori Oka, Masayuki Takahashi, Hiro-omi Kanayama and Kouji Itou : Hydroxyflutamide enhances cellular sensitivity to 5-fluorouracil by suppressing thymidylate synthase expression in bicalutamide-resistant human prostate cancer cells, International Journal of Oncology, Vol.38, No.3, 665-676, 2011. (要約) We investigated the antitumor effects of combination therapy with anti-androgens and 5-fluorouracil (5-FU), and examined the underlying mechanism of the treatment. Initially, we established the bicalutamide-resistant subline CDX25R from the androgen receptor (AR)-positive human prostate cancer cell line LNCaP through continuous exposure to bicalutamide. CDX25R cells lost the ability to respond to androgens, but still expressed AR. They showed significant resistance to bicalutamide, but had high sensitivity to hydroxyflutamide (OH-flutamide) compared with LNCaP cells. The CDX25R subline was thus considered to be a suitable model for prostate cancer that has developed resistance to first-line hormonal therapy but shows sensitivity to an alternative approach. Combined treatment with 5-FU and OH-flutamide had a synergistic effect on CDX25R cells. OH-flutamide decreased expression of the transcription factor E2F1, and subsequently of thymidylate synthase (TS), in CDX25R cells but not in AR-negative DU145 cells. This suggested that OH-flutamide enhanced the growth-inhibitory activity of 5-FU in CDX25R cells by reducing TS expression through the AR pathway. Combined therapy with 5-FU and OH-flutamide may, therefore, be appropriate for patients with prostate cancer that has acquired resistance to initial hormone therapy including bicalutamide. (キーワード) Androgen Antagonists / Anilides / Antimetabolites, Antineoplastic / Carcinoma / Cell Line, Tumor / Drug Evaluation, Preclinical / Drug Resistance, Neoplasm / Drug Synergism / Fluorouracil / Flutamide / Gene Expression Regulation, Enzymologic / Gene Expression Regulation, Neoplastic / Humans / Male / Models, Biological / Neoplasms, Hormone-Dependent / Nitriles / Prostatic Neoplasms / Thymidylate Synthase / Tosyl Compounds (出版サイトへのリンク) ● Publication site (DOI): 10.3892/ijo.2011.909 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21243325 ● Search Scopus @ Elsevier (PMID): 21243325 ● Search Scopus @ Elsevier (DOI): 10.3892/ijo.2011.909 (DOI: 10.3892/ijo.2011.909, PubMed: 21243325)
52.	Tatsuo Ito, Haruka Kitamura, Chisana Uwatoko, Tamitake Itoh, Makiko Azumano, Kouji Itou and Jun Kuwahara : Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1, Biochemical and Biophysical Research Communications, Vol.403, No.2, 161-166, 2010. (要約) Transcription factor Sp1 is localized in the nucleus and regulates the expression of many cellular genes, but the nuclear transport mechanism of Sp1 is not well understood. In this study, we revealed that GST-fused Sp1 protein bound to endogenous importin α in HeLa cells via the Sp1 zinc finger domains, which comprise the DNA binding domain of Sp1. It was found that the Sp1 zinc finger domains directly interacted with a wide range of importin α including the armadillo (arm) repeat domain and the C-terminal acidic domain. Furthermore, it turned out that all three zinc fingers of Sp1 are essential for binding to importin α. Taken together, these results suggest that the Sp1 zinc finger domains play an essential role as a NLS and Sp1 can be transported into the nucleus in an importin-dependent manner even though it possesses no classical NLSs. (キーワード) Active Transport, Cell Nucleus / Cell Nucleus / HeLa Cells / Humans / Nuclear Localization Signals / Sequence Deletion / Sp1 Transcription Factor / Zinc Fingers / alpha Karyopherins (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbrc.2010.10.036 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20946882 ● Summary page in Scopus @ Elsevier: 2-s2.0-78649965849 (DOI: 10.1016/j.bbrc.2010.10.036, PubMed: 20946882, Elsevier: Scopus)
53.	Keiko Miyoshi, Daisuke Tsuji, Keiko Kudoh, Kazuhito Satomura, Taro Muto, Kouji Itou and Takafumi Noma : Generation of human induced pluripotent stem cells from oral mucosa, Journal of Bioscience and Bioengineering, Vol.110, No.3, 345-350, 2010. (要約) Induced pluripotent stem (iPS) cells are one of the most promising sources for cell therapy in regenerative medicine. Using a patient's own genetically identical and histocompatible cells is the ideal way to practice personalized regenerative medicine. For personalized iPS cell therapy, the prerequisites for cell source preparation are a simple and safe procedure, no aesthetic or functional damage, and quick wound healing. Oral mucosa fibroblasts (OFs) may have high potential to fulfill these requirements. In this study, biopsy was performed in a dental chair; no significant incisional damage was recognized and rapid wound healing (within a week) was observed. We generated human iPS cells from the isolated OFs via the retroviral gene transfer of OCT4, SOX2, c-MYC, and KLF4. Reprogrammed cells showed ES-like morphology and expressed undifferentiated markers such as OCT4, NANOG, SSEA4, TRA-1-60, and TRA-1-81. Subsequent in vitro and in vivo analyses confirmed the pluripotency of resultant iPS cells, which matched the criteria for iPS cells. In addition, we found that the endogenous expression levels of c-MYC and KLF4 in OFs were similar to those in dermal fibroblasts. Taken together, we propose that OFs could be a practical source for preparing iPS cells to achieve personalized regenerative medicine in the near future. (キーワード) Adult / Cell Culture Techniques / Cell Differentiation / Female / Genetic Enhancement / Humans / Male / Mouth Mucosa / Pluripotent Stem Cells / Tissue Engineering (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.jbiosc.2010.03.004 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20547351 ● Search Scopus @ Elsevier (PMID): 20547351 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbiosc.2010.03.004 (DOI: 10.1016/j.jbiosc.2010.03.004, PubMed: 20547351)
54.	Kazuhiko Matsuoka, Daisuke Tsuji, Sei-ichi Aikawa, Fumiko Matsuzawa, Hitoshi Sakuraba and Kouji Itou : Introduction of an N-Glycan Sequon Into HEXA Enhances Human -Hexosaminidase Cellular Uptake in a Model of Sandhoff Disease, Molecular Therapy, Vol.18, No.8, 1519-1526, 2010. (要約) Human lysosomal beta-hexosaminidase A is a heterodimer composed of alpha- and beta-subunits encoded by HEXA and HEXB, respectively. We genetically introduced an additional N-glycosylation sequon into HEXA, which caused amino acid substitutions (S51 to N and A53 to T) at homologous positions to N84 and T86 in the beta-subunit. The mutant HexA (NgHexA) obtained from a Chinese hamster ovary (CHO) cell line co-expressing the mutated HEXA and wild-type HEXB complementary DNAs was demonstrated to contain an additional mannose-6-phosphate (M6P)-type-N-glycan. NgHexA was more efficiently taken up than the wild-type HexA and delivered to lysosomes, where it degraded accumulated substrates including GM2 ganglioside (GM2) when administered to cultured fibroblasts derived from a Sandhoff disease (SD) patient. On intracerebroventricular (i.c.v.) administration of NgHexA to SD model mice, NgHexA more efficiently restored the HexA activity and reduced the GM2 and GA2 (asialoGM2) accumulated in neural cells of the brain parenchyma than the wild-type HexA. These findings indicate that i.c.v. administration of the modified human HexA with an additional M6P-type N-glycan is applicable for enzyme replacement therapy (ERT) involving an M6P-receptor as a molecular target for HexA deficiencies including Tay-Sachs disease and SD. (キーワード) Animals / CHO Cells / Cells, Cultured / Chromatography, Thin Layer / Cricetinae / Cricetulus / G(M2) Ganglioside / Glycosylation / Humans / Immunoblotting / Mice / Polysaccharides / Sandhoff Disease / beta-Hexosaminidase alpha Chain / beta-Hexosaminidase beta Chain / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1038/mt.2010.113 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20571546 ● Search Scopus @ Elsevier (PMID): 20571546 ● Search Scopus @ Elsevier (DOI): 10.1038/mt.2010.113 (DOI: 10.1038/mt.2010.113, PubMed: 20571546)
55.	Nagako Kawashima, Kenichi Nakayama, Kouji Itou, Tamitake Itoh, Mitsuru Ishikawa and Vasudevanpillai Biju : Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots, Chemistry - A European Journal, Vol.16, No.4, 1186-1192, 2010. (要約) The current work explores intermolecular interactions involved in the lateral propagation of cell-signaling by epidermal growth factor receptors (EGFRs). Activation of EGFRs by binding an EGF ligand in the extracellular domain of the EGFR and subsequent dimerization of the EGFR initiates cell-signaling. We investigated interactions between EGFRs in living cells by using single-molecule microscopy, Förster resonance energy transfer (FRET), and atomic force microscopy. By analyzing time-correlated intensity and propagation trajectories of quantum dot (QD)-labeled EGFR single molecules, we found that signaling dimers of EGFR [(EGF-EGFR)(2)] are continuously formed in cell membrane through reversible association of heterodimers [EGF(EGFR)(2)]. Also, we found that the lateral propagation of EGFR activation takes place through transient association of a heterodimer with predimers [(EGFR)(2)]. We varified the transient association between activated EGFR and predimers using FRET from QD-labeled heterodimers to Cy5-labeled predimers and correlated topography and fluorescence imaging. Without extended single-molecule fluorescence imaging and by using bio-conjugated QDs, reversible receptor dimerization in the lateral activation of EGFR remained obscured. (キーワード) Cell Line, Tumor / Dimerization / Fluorescence Resonance Energy Transfer / Fluorescent Dyes / Humans / Ligands / Microscopy, Atomic Force / Protein Binding / Quantum Dots / Receptor, Epidermal Growth Factor / Signal Transduction (出版サイトへのリンク) ● Publication site (DOI): 10.1002/chem.200902963 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20024999 ● Search Scopus @ Elsevier (PMID): 20024999 ● Search Scopus @ Elsevier (DOI): 10.1002/chem.200902963 (DOI: 10.1002/chem.200902963, PubMed: 20024999)
56.	Yousuke Fukui, Masao Kato, Yohji Inoue, Akio Matsubara and Kouji Itou : A metabonomic approach identifies human urinary phenylacetylglutamine as a novel marker of interstitial cystitis, Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, Vol.877, No.30, 3806-3812, 2009. (要約) An ultra-performance liquid chromatography-mass spectrometry (UPLC-MS) based metabonomic approach was applied to identify a candidate metabolite with not known to be associated with interstitial cystitis (IC). IC is a chronic clinical syndrome associated with urinary frequency and urgency and/or pelvic pain. The ability to non-invasively diagnose the early stage of IC would be important for improving the patient's quality of life. The current standard IC diagnosis is cystoscopy, which is invasive and painful. Urine samples from the following were taken and analyzed: 10 IC patients, 10 bacterial cystitis (BC) patients, and 10 healthy volunteers (HVs) to identify an IC marker; and subsequently analyzed 5 IC patients and 5 HVs for marker validation. The urinary marker of IC was identified as phenylacetylglutamine (PAGN) using NMR and MS/MS analysis. In addition, quantitative methods were developed to determining the urinary PAGN levels using UPLC-UV. The urinary level of PAGN measured relative to creatinine (Cr) was significantly elevated in IC patients (mean 0.47mg/mg Cr) compared with BC patients (mean 0.25mg/mg Cr) and HVs (mean 0.11mg/mg Cr). Interestingly, urinary PAGN/Cr ratios in patients with mild IC (grade I) and moderate IC (grade II) were higher than for patients with severe IC (grade III). Moreover, urinary PAGN/Cr ratios with mild and moderate IC patients (mean 0.30mg/mg Cr) were higher than HVs (mean 0.059mg/mg Cr), in the validation set. These findings establish urinary PAGN/Cr ratios as a novel urinary marker of IC, and may contribute to early diagnosis of IC patients. (キーワード) Adolescent / Adult / Aged / Aged, 80 and over / Biological Markers / Case-Control Studies / Child / Cystitis, Interstitial / Female / Glutamine / Humans / Male / Metabolomics / Middle Aged / Young Adult (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.jchromb.2009.09.025 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19815468 ● Search Scopus @ Elsevier (PMID): 19815468 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jchromb.2009.09.025 (DOI: 10.1016/j.jchromb.2009.09.025, PubMed: 19815468)
57.	Youichi Tajima, Ikuo Kawashima, Takahiro Tsukimura, Kanako Sugawara, Mayuko Kuroda, Toshihiro Suzuki, Tadayasu Togawa, Yasunori Chiba, Yoshifumi Jigami, Kazuki Ohno, Tomoko Fukushige, Takuro Kanekura, Kouji Itou, Toya Ohashi and Hitoshi Sakuraba : Use of a Modified alpha-N-Acetylgalactosaminidase in the Development of Enzyme Replacement Therapy for Fabry Disease, American Journal of Human Genetics, Vol.85, No.5, 569-580, 2009. (要約) A modified alpha-N-acetylgalactosaminidase (NAGA) with alpha-galactosidase A (GLA)-like substrate specificity was designed on the basis of structural studies and was produced in Chinese hamster ovary cells. The enzyme acquired the ability to catalyze the degradation of 4-methylumbelliferyl-alpha-D-galactopyranoside. It retained the original NAGA's stability in plasma and N-glycans containing many mannose 6-phosphate (M6P) residues, which are advantageous for uptake by cells via M6P receptors. There was no immunological cross-reactivity between the modified NAGA and GLA, and the modified NAGA did not react to serum from a patient with Fabry disease recurrently treated with a recombinant GLA. The enzyme cleaved globotriaosylceramide (Gb3) accumulated in cultured fibroblasts from a patient with Fabry disease. Furthermore, like recombinant GLA proteins presently used for enzyme replacement therapy (ERT) for Fabry disease, the enzyme intravenously injected into Fabry model mice prevented Gb3 storage in the liver, kidneys, and heart and improved the pathological changes in these organs. Because this modified NAGA is hardly expected to cause an allergic reaction in Fabry disease patients, it is highly promising as a new and safe enzyme for ERT for Fabry disease. (キーワード) Amino Acid Substitution / Animals / Binding Sites / CHO Cells / Catalysis / Cells, Cultured / Cricetinae / Cricetulus / Culture Media, Conditioned / DNA, Complementary / Disease Models, Animal / Drug Stability / Enzyme Replacement Therapy / Fabry Disease / Fibroblasts / Fluorescent Dyes / Galactosides / Genetic Vectors / Humans / Hydrogen-Ion Concentration / Hymecromone / 免疫組織化学 (immunohistochemistry) / Kidney / Liver / Mice / Mice, Knockout / Models, Molecular / 分子量 (molecular weight) / 心筋 (myocardium) / Recombinant Proteins / Retroviridae / Transfection / Trihexosylceramides / alpha-N-Acetylgalactosaminidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.ajhg.2009.09.016 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19853240 ● Search Scopus @ Elsevier (PMID): 19853240 ● Search Scopus @ Elsevier (DOI): 10.1016/j.ajhg.2009.09.016 (DOI: 10.1016/j.ajhg.2009.09.016, PubMed: 19853240)
58.	Nagako Kawashima, Daisuke Tsuji, Tetsuya Okuda, Kouji Itou and Ken-ichi Nakayama : Mechanism of abnormal growth in astrocytes derived from a mouse model of GM2 gangliosidosis, Journal of Neurochemistry, Vol.111, No.4, 1031-1041, 2009. (要約) Sandhoff disease is a progressive neurodegenerative disorder caused by mutations in the HEXB gene which encodes the beta-subunit of N-acetyl-beta-hexosaminidase A and B, resulting in the accumulation of the ganglioside GM2. We isolated astrocytes from the neonatal brain of Sandhoff disease model mice in which the N-acetyl-beta-hexosaminidase beta-subunit gene is genetically disrupted (ASD). Glycolipid profiles revealed that GM2/GA2 accumulated in the lysosomes and not on the cell surface of ASD astrocytes. In addition, GM3 was increased on the cell surface. We found remarkable differences in the cell proliferation of ASD astrocytes when compared with cells isolated from wild-type mice, with a faster growth rate of ASD cells. In addition, we observed increased extracellular, signal-regulated kinase (ERK) phosphorylation in ASD cells, but Akt phosphorylation was decreased. Furthermore, the phosphorylation of ERK in ASD cells was not dependent upon extracellular growth factors. Treatment of ASD astrocytes with recombinant N-acetyl-beta-hexosaminidase A resulted in a decrease of their growth rate and ERK phosphorylation. These results indicated that the up-regulation of ERK phosphorylation and the increase in proliferation of ASD astrocytes were dependent upon GM2/GA2 accumulation. These findings may represent a mechanism in linking the nerve cell death and reactive gliosis observed in Sandhoff disease. (キーワード) Animals / Animals, Newborn / Astrocytes / Cell Proliferation / Cells, Cultured / Chromatography, High Pressure Liquid / Disease Models, Animal / Extracellular Signal-Regulated MAP Kinases / Flow Cytometry / Gangliosides / Gangliosidoses, GM2 / Glial Fibrillary Acidic Protein / Hexosaminidase A / Hexosaminidase B / Lectins / Lysosomes / Mice / Mice, Inbred C57BL / Mice, Knockout / O Antigens / Sandhoff Disease / Signal Transduction / Spinal Cord (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1471-4159.2009.06391.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19765188 ● Search Scopus @ Elsevier (PMID): 19765188 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1471-4159.2009.06391.x (DOI: 10.1111/j.1471-4159.2009.06391.x, PubMed: 19765188)
59.	Tatsusada Yoshida, Y Kadota, S Hitaoka, E Kori, Yuta Horikawa, M Taguchi, Daisuke Tsuji, Mitsuyoshi Hirokawa, Hiroshi Chuman and Kouji Itou : Expression and molecular dynamics studies on effect of amino acid substitutions at Arg344 in human cathepsin A on the protein local conformation., Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol.1794, No.11, 1693-1699, 2009. (要約) Human lysosomal protective protein/cathepsin A (CathA) is a multifunctional protein that exhibits not only protective functions as to lysosomal glycosidases, i.e., neuraminidase 1 (NEU1) and beta-galactosidase (GLB), but also its own serine carboxypeptidase activity, and exhibits conserved structural similarity to yeast and wheat homologs (CPY and CPW). Our previous study revealed that the R344 (Arg344) residue in CathA could contribute to the binding and recognition of the serine peptidase inhibitor chymostatin. We examined here the effects of substitution of R344 with other amino acids, including A, D, E, G, I, K, M, N, P, Q, S, and V, denoted as R344X, including the wild-type CathA, on expression of CathA activity and intracellular processing. Among the mutant gene products, the 54-kDa precursor/zymogen with the R344D substitution was not processed to the 32/20-kDa mature form with CathA activity in a fibroblastic cell line derived from a galactosialidosis patient. Molecular dynamics (MD) simulations on the total twelve R344X mutants and the wild-type revealed that only R344D takes on a significantly different conformation of S293-D295 in the excision peptide (M285-R298) compared to the other R344X mutants; the side chains of S293 and D295 in R344D are exposed on the molecular surface, although those in the other twelve R344X mutants are buried inside the protein. The results of the current work strongly suggest that the distinct conformational change of the S293-D295 region in the R344D protein causes the processing defect of the 54-kDa precursor of the R344D mutant gene product in cultured cells. (キーワード) Amino Acid Substitution / Cathepsin A / Humans / Models, Molecular / Molecular Dynamics Simulation / Mucolipidoses / Protein Conformation / Water (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbapap.2009.08.004 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19679197 ● Search Scopus @ Elsevier (PMID): 19679197 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbapap.2009.08.004 (DOI: 10.1016/j.bbapap.2009.08.004, PubMed: 19679197)
60.	Hiromi Akeboshi, Yoshiko Kasahara, Daisuke Tsuji, Kouji Itou, Hitoshi Sakuraba, Yasunori Chiba and Yoshifumi Jigami : Production of human β-Hexosaminidase A with highly phosphorylated N-glycans by the overexpression of the Ogataea minuta MNN4 gene., Glycobiology, Vol.19, No.9, 1002-1009, 2009. (要約) Effective enzyme replacement therapy for lysosomal storage diseases requires a recombinant enzyme with highly phosphorylated N-glycans. Recombinant human beta-hexosaminidase A is a potentially therapeutic enzyme for GM2-gangliosidosis. Recombinant HexA has been produced by using the methylotrophic yeast Ogataea minuta as a host, and the purified enzyme was tested for its replacement effect on cultured fibroblasts derived from GM2-gangliosidosis patients. Although the therapeutic effect was observed, in order to obtain the higher therapeutic effect with a little dose as possible, increased phosphorylation of recombinant beta-hexosaminidase A N-glycans is suggested to be prerequisite. In the budding yeast Saccharomyces cerevisiae, the overexpression of MNN4, which encodes a positive regulator of mannosylphosphate transferase, led to increased mannosylphosphate contents. In the present study, we cloned OmMNN4, a homologous gene to ScMNN4, based on the genomic sequence of O. minuta. We overexpressed the cloned gene under the control of the alcohol oxidase promoter in a beta-hexosaminidase A-producing yeast strain. Structural analysis of pyridylamine-labeled N-glycans by high-performance liquid chromatography revealed that the overexpression of MNN4 caused a 3-fold increase in phosphorylated N-glycans of recombinant beta-hexosaminidase A. The recombinant enzyme prepared from strains overexpressing OmMNN4 was more effectively incorporated into cultured fibroblasts and neural cells, and it more rapidly degraded the accumulated GM2-ganglioside as compared to the control enzyme. These results suggest that beta-hexosaminidase A produced in a strain that overexpresses OmMNN4 will act as an effective enzyme for use in replacement therapy of GM2-gangliosidosis. (キーワード) Amino Acid Sequence / Humans / Molecular Sequence Data / Phosphorylation / Polysaccharides / Saccharomyces cerevisiae / Sequence Homology, Amino Acid / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1093/glycob/cwp080 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19506294 ● Search Scopus @ Elsevier (PMID): 19506294 ● Search Scopus @ Elsevier (DOI): 10.1093/glycob/cwp080 (DOI: 10.1093/glycob/cwp080, PubMed: 19506294)
61.	Eri Kawashita, Daisuke Tsuji, Nagako Kawashima, Ken-ichi Nakayama, Hiroyuki Matsuno and Kouji Itou : Abnormal production of macrophage inflammatory protein-1α by microglial cell lines derived from neonatal brains of Sandhoff disease model mice., Journal of Neurochemistry, Vol.109, No.5, 1215-1224, 2009. (要約) Sandhoff disease (SD) is a lysosomal beta-hexosaminidase deficiency involving excessive accumulation of undegraded substrates, including terminal N-acetylglucosamine-oligosaccharides and GM2 ganglioside, and progressive neurodegeneration. Our previous study demonstrated remarkable induction of macrophage inflammatory factor-1alpha (MIP-1alpha) in microglia in the brains of SD model mice as a putative pathogenic factor for SD via microglia-mediated neuroinflammation. In this study, we established microglial cell lines (WT- and SD-Mg) from wild-type and SD mice, and first demonstrated the enhanced production of MIP-1alpha in SD-Mg. Inhibitors of protein kinase C (PKC) and Akt reduced the production of MIP-1alpha by SD-Mg. Elevated activation of Akt and partial translocation of PKC isozymes (alpha, betaI, betaII, and delta) from the cytoplasm to the membrane in SD-Mg were also revealed by means of immunoblotting. Furthermore, it was demonstrated that intracellular extracellular signal-regulated kinase, c-Jun N-terminal kinase, and phospholipase C (PLC), but not phosphoinositide 3-kinase, should contribute to the induction of MIP-1alpha in SD-Mg, and that PLC could independently regulate the activation of both PKC and Akt. We proposed here that the deregulated activation of PLC should cause the enhanced MIP-1alpha production via plural signaling pathways mediated by PKC and Akt, followed by extracellular signal-regulated kinase and c-Jun N-terminal kinase, in SD-Mg. (キーワード) Animals / Animals, Newborn / Brain / Cells, Cultured / Chemokine CCL3 / Disease Models, Animal / Enzyme Inhibitors / Enzyme-Linked Immunosorbent Assay / Gene Expression Regulation / Mice / Mice, Knockout / Microglia / Mitogen-Activated Protein Kinase 3 / Oncogene Protein v-akt / Protein Kinase C / Protein Transport / RNA, Messenger / Sandhoff Disease / Signal Transduction / Subcellular Fractions / beta-Hexosaminidase beta Chain (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1471-4159.2009.06041.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19302485 ● Search Scopus @ Elsevier (PMID): 19302485 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1471-4159.2009.06041.x (DOI: 10.1111/j.1471-4159.2009.06041.x, PubMed: 19302485)
62.	Nagako Kawashima, Yoon Seon-Joo, Kouji Itou and Ken-ichi Nakayama : Tyrosine Kinase Activity of Epidermal Growth Factor Receptor Is Regulated by GM3 Binding through Carbohydrate to Carbohydrate Interactions., The Journal of Biological Chemistry, Vol.284, No.10, 6147-6155, 2009. (要約) Epidermal growth factor receptor (EGFR), an N-glycosylated transmembrane protein with an intracellular kinase domain, undergoes dimerization by ligand binding resulting in activation of the kinase domain and phosphorylation. Ganglioside GM3 containing sialyllactose inhibits the tyrosine kinase activity of EGFR through carbohydrate to carbohydrate interactions (CCI) between N-glycans with GlcNAc termini on EGFR and oligosaccharides on GM3. In this study, we provide further evidence for CCI between EGFR and GM3. (i) In vitro and in situ, the inhibitory effect of GM3 on EGFR tyrosine kinase was much higher in A431 cells upon exposure of the GlcNAc termini of the N-glycans to glycosidase treatment (neuraminidase and beta-galactosidase) than in untreated A431 cells. Furthermore, the GM3-mediated inhibition was abrogated by co-incubation with N-glycan containing terminal GlcNAc. (ii) In situ, inhibition of EGFR phosphorylation by GM3 was not observed in alpha-mannosidase IB (ManIB)-knocked down A431 cells that accumulate high mannose-type N-glycans. (iii) EGFR binding to GM3 was enhanced in glycosidase-treated cells that accumulated GlcNAc termini, whereas GM3 did not bind to EGFR from ManIB-knocked down cells that accumulated high mannose-type N-glycans. These results indicate that GM3-mediated inhibition of EGFR phosphorylation is caused by interaction of GM3 with GlcNAc-terminated N-glycan on EGFR. (キーワード) Acetylglucosamine / Cell Line, Tumor / G(M3) Ganglioside / Humans / Phosphorylation / Protein Binding / Protein Structure, Tertiary / Receptor, Epidermal Growth Factor (出版サイトへのリンク) ● Publication site (DOI): 10.1074/jbc.M808171200 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19124464 ● Search Scopus @ Elsevier (PMID): 19124464 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M808171200 (DOI: 10.1074/jbc.M808171200, PubMed: 19124464)
63.	Tatsuo Ito, Makiko Azumano, Chisana Uwatoko, Kouji Itou and Jun Kuwahara : Role of zinc finger structure in nuclear localization of transcription factor Sp1, Biochemical and Biophysical Research Communications, Vol.380, No.1, 28-32, 2009. (要約) Transcription factor Sp1 is localized in the nucleus and regulates gene expression. Our previous study demonstrated that the carboxyl terminal region of Sp1 containing 3-zinc finger region as DNA binding domain can also serve as nuclear localization signal (NLS). However, the nuclear transport mechanism of Sp1 has not been well understood. In this study, we performed a gene expression study on mutant Sp1 genes causing a set of amino acid substitutions in zinc finger domains to elucidate nuclear import activity. Nuclear localization of the GFP-fused mutant Sp1 proteins bearing concomitant substitutions in the first and third zinc fingers was highly inhibited. These mutant Sp1 proteins had also lost the binding ability as to the GC box sequence. The results suggest that the overall tertiary structure formed by the three zinc fingers is essential for nuclear localization of Sp1 as well as dispersed basic amino acids within the zinc fingers region. (キーワード) Active Transport, Cell Nucleus / Aminoquinolines / Cell Nucleus / HeLa Cells / Humans / Nuclear Localization Signals / Sp1 Transcription Factor / Tosyl Compounds / Zinc / Zinc Fingers (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbrc.2008.12.165 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19138671 ● Search Scopus @ Elsevier (PMID): 19138671 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2008.12.165 (DOI: 10.1016/j.bbrc.2008.12.165, PubMed: 19138671)
64.	Kanako Sugawara, Youichi Tajima, Ikuo Kawashima, Takahiro Tsukimura, Seiji Saito, Kazuki Ohno, Kunihiko Iwamoto, Toshihide Kobayashi, Kouji Itou and Hitoshi Sakuraba : Molecular interaction of imino sugars with human a-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease, Molecular Genetics and Metabolism, Vol.96, No.4, 233-238, 2009. (要約) Enzyme enhancement therapy (EET) for Fabry disease involving imino sugars has been developed and attracted interest. It is thought that imino sugars act as pharmacological chaperones for wild-type and mutant alpha-galactosidases (GLAs) in cells, but the mechanisms underlying the molecular interactions between the imino sugars and the enzyme have not been clarified yet. We examined various kinds of imino sugars and found that galactostatin bisulfite (GBS) inhibited GLA in vitro and increased the enzyme activity in cultured Fabry fibroblasts as in the case of 1-deoxygalactonojirimycin (DGJ). Then, we analyzed the molecular interactions between the imino sugars and recombinant human GLA by means of isothermal titration calorimetry and surface plasmon resonance biosensor assays, and first determined the thermodynamic and binding-kinetics parameters of imino sugar and GLA complex formation. The results revealed that DGJ bound to the enzyme more strongly than GBS, the binding of DGJ to the enzyme protein being enthalpy-driven. In the case of GBS, the reaction was mainly enthalpy-driven, but there was a possibility that entropy-driven factors were involved in the binding. Structural analysis in silico revealed that both the chemicals fit into the active-site pocket and undergo hydrogen bonding with residues comprising the active-site pocket including the catalytic ones. The side chain of GBS was oriented towards the entrance of the active-site pocket, and thus it could be in contact with residues comprising the wall of the active-site pocket. Thermodynamic, kinetic and structural studies should provide us with a lot of information for improving EET for Fabry disease. (キーワード) 1-Deoxynojirimycin / Animals / CHO Cells / Catalytic Domain / Cells, Cultured / Cricetinae / Cricetulus / Fabry Disease / Fibroblasts / Galactosamine / Humans / Imino Sugars / Kinetics / Models, Molecular / Thermodynamics / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.ymgme.2008.12.017 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19181556 ● Search Scopus @ Elsevier (PMID): 19181556 ● Search Scopus @ Elsevier (DOI): 10.1016/j.ymgme.2008.12.017 (DOI: 10.1016/j.ymgme.2008.12.017, PubMed: 19181556)
65.	Yutaka Tatano, Reiko Fujinawa, Yasunori Kozutsumi, Tsutomu Takahashi, Daisuke Tsuji, Kohji Tsuta, Goro Takada, Hitoshi Sakuraba and Kouji Itou : Tropoelastin regulates chemokine expression in fibroblasts in Costello syndrome., Biochemical and Biophysical Research Communications, Vol.372, No.4, 681-687, 2008. (要約) Costello syndrome is a multiple congenital anomaly associated with growth and mental retardation, cardiac and skeletal anomalies, and a predisposition to develop neoplasia. Comprehensive expression analysis revealed remarkable up-regulation of several cytokines and chemokines including Gro family proteins, interleukin-1beta (IL-1beta), IL-8 and MCP-1 but down-regulation of extracellular matrix components including collagens and proteoglycans of skin fibroblasts derived from a Japanese Costello syndrome patient characterized by significantly reduced tropoelastin mRNA, impaired elastogenesis and enhanced cell proliferation. In contrast, decreases in these chemokines and IL-1beta expression were observed in Costello fibroblastic cell lines stably expressing the bovine tropoelastin (btEln) gene and in restored elastic fibers. These results strongly suggest that the human TE gene (ELN) transfer could be applicable for the gene therapy of a group of Costello syndrome patients with reduced ELN gene expression. (キーワード) Abnormalities, Multiple / Adolescent / Chemokines / Cytokines / Female / Fibroblasts / Gene Expression Profiling / Gene Therapy / Gene Transfer Techniques / Humans / Protein Biosynthesis / Reverse Transcriptase Polymerase Chain Reaction / Skin / Syndrome / Tropoelastin / Up-Regulation (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbrc.2008.05.131 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18533107 ● Search Scopus @ Elsevier (PMID): 18533107 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2008.05.131 (DOI: 10.1016/j.bbrc.2008.05.131, PubMed: 18533107)
66.	V Seyrantepe, J Peng, M Fedjaev, S Ernest, Y Kadota, M Canuel, Kouji Itou, CR Morales, J Lavoie, A Hinek, J Tremblay and AV Pshezhetsky : The Enzymatic Activity of Lysosomal Carboxypeptidase (Cathepsin) A is Required for Proper Elastic Fibre Formation and Inactivation of Endothelin-1, Circulation, Vol.117, No.15, 1973-1981, 2008. (要約) Lysosomal carboxypeptidase, cathepsin A (protective protein, CathA), is a component of the lysosomal multienzyme complex along with beta-galactosidase (GAL) and sialidase Neu1, where it activates Neu1 and protects GAL and Neu1 against the rapid proteolytic degradation. On the cell surface, CathA, Neu1, and the enzymatically inactive splice variant of GAL form the elastin-binding protein complex. In humans, genetic defects of CathA cause galactosialidosis, a metabolic disease characterized by combined deficiency of CathA, GAL, and Neu1 and a lysosomal storage of sialylated glycoconjugates. However, several phenotypic features of galactosialidosis patients, including hypertension and cardiomyopathies, cannot be explained by the lysosomal storage. These observations suggest that CathA may be involved in hemodynamic functions that go beyond its protective activity in the lysosome. We generated a gene-targeted mouse in which the active CathA was replaced with a mutant enzyme carrying a Ser190Ala substitution in the active site. These animals expressed physiological amounts of catalytically inactive CathA protein, capable of forming lysosomal multienzyme complex, and did not develop secondary deficiency of Neu1 and GAL. Conversely, the mice showed a reduced degradation rate of the vasoconstrictor peptide, endothelin-1, and significantly increased arterial blood pressure. CathA-deficient mice also displayed scarcity of elastic fibers in lungs, aortic adventitia, and skin. Our results provide the first evidence that CathA acts in vivo as an endothelin-1-inactivating enzyme and strongly confirm a crucial role of this enzyme in effective elastic fiber formation. (キーワード) Animals / Blood Pressure / Cathepsin A / Cells, Cultured / Elastic Tissue / Elastin / Endothelin-1 / Enzyme Activation / Fibroblasts / Genes, Synthetic / Hypertension / Lysosomes / Mice / Mice, Inbred C57BL / Mice, Knockout / Multienzyme Complexes / Neuraminidase / Neurons / Organ Specificity / RNA, Messenger / Sodium Chloride, Dietary / beta-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1161/CIRCULATIONAHA.107.733212 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18391110 ● Search Scopus @ Elsevier (PMID): 18391110 ● Search Scopus @ Elsevier (DOI): 10.1161/CIRCULATIONAHA.107.733212 (DOI: 10.1161/CIRCULATIONAHA.107.733212, PubMed: 18391110)
67.	M Yoshimizu, Y Tajima, F Matsuzawa, S Aikawa, I Iwamoto, T Kobayashi, T Edmunds, K Fujishima, Daisuke Tsuji, Kouji Itou, M Ikekita, I Kawashima, K Sugawara, N Ohyanagi, T Suzuki, T Togawa, K Ohno and H Sakuraba : Binding parameters and thermodynamics of the interection of imino sugars with a recombinant human acid -α-glucosidase (alglucosidase alfa): Insight into the complex formation mechanism., Clinica Chimica Acta, Vol.391, No.1-2, 68-73, 2008. (要約) Recently, enzyme enhancement therapy (EET) for Pompe disease involving imino sugars, which act as potential inhibitors of acid alpha-glucosidases in vitro, to improve the stability and/or transportation of mutant acid alpha-glucosidases in cells was studied and attracted interest. However, the mechanism underlying the molecular interaction between the imino sugars and the enzyme has not been clarified yet. We examined the inhibitory and binding effects of four imino sugars on a recombinant human acid alpha-glucosidase, alglucosidase alfa, by means of inhibition assaying and isothermal titration calorimetry (ITC). Furthermore, we built structural models of complexes of the catalytic domain of the enzyme with the imino sugars bound to its active site by homology modeling, and examined the molecular interaction between them. All of the imino sugars examined exhibited a competitive inhibitory action against the enzyme, 1-deoxynojirimycin (DNJ) exhibiting the strongest action among them. ITC revealed that one compound molecule binds to one enzyme molecule and that DNJ most strongly binds to the enzyme among them. Structural analysis revealed that the active site of the enzyme is almost completely occupied by DNJ. These biochemical and structural analyses increased our understanding of the molecular interaction between a human acid alpha-glucosidase and imino sugars. (キーワード) 1-Deoxynojirimycin / Binding Sites / Catalytic Domain / Drug Interactions / Glycogen Storage Disease Type II / Humans / Imino Sugars / Models, Molecular / Recombinant Proteins / Thermodynamics / alpha-Glucosidases (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.cca.2008.02.014 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18328816 ● Search Scopus @ Elsevier (PMID): 18328816 ● Search Scopus @ Elsevier (DOI): 10.1016/j.cca.2008.02.014 (DOI: 10.1016/j.cca.2008.02.014, PubMed: 18328816)
68.	Daisuke Tsuji, Yukari Higashine, Kazuhiko Matsuoka, Hitoshi Sakuraba and Kouji Itou : Therapeutic evaluation of GM2 gangliosidoses by ELISA using anti-GM2 ganglioside antibodies., Clinica Chimica Acta, Vol.378, No.1-2, 38-41, 2007. (要約) GM2 gangliosidoses, including Tay-Sachs disease, Sandhoff disease and the AB variant, comprise deficiencies of beta-hexosaminidase isozymes and GM2 ganglioside activator protein associated with accumulation of GM2 ganglioside (GM2) in lysosomes and neurosomatic clinical manifestations. A simple assay system for intracellular quantification of GM2 is required to evaluate the therapeutic effects on GM2-gangliosidoses. We newly established a cell-ELISA system involving anti-GM2 monoclonal antibodies for measuring GM2 storage in fibroblasts from Tay-Sachs and Sandhoff disease patients. We succeeded in detecting the corrective effect of enzyme replacement on elimination of GM2 in the cells with this ELISA system. This simple and sensitive system should be useful as additional diagnosis tool as well as therapeutic evaluation of GM2 gangliosidoses. (キーワード) Antibodies, Monoclonal / Cells, Cultured / Enzyme-Linked Immunosorbent Assay / Fibroblasts / G(M2) Ganglioside / Gangliosidoses, GM2 / Hexosaminidase B / Humans / Sandhoff Disease / Tay-Sachs Disease / beta-Hexosaminidase beta Chain / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.cca.2006.10.010 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17196574 ● Search Scopus @ Elsevier (PMID): 17196574 ● Search Scopus @ Elsevier (DOI): 10.1016/j.cca.2006.10.010 (DOI: 10.1016/j.cca.2006.10.010, PubMed: 17196574)
69.	Akira Shigenaga, Daisuke Tsuji, Naomi Nishioka, Shugo Tsuda, Kouji Itou and Akira Otaka : Synthesis of a stimulus-responsive processing device and its application to a nucleocytoplasmic shuttle peptide, ChemBioChem, Vol.8, No.16, 1929-1931, 2007. (キーワード) Active Transport, Cell Nucleus / Amino Acids / Animals / CHO Cells / Cell Nucleus / Cricetinae / Cricetulus / Fluorescent Dyes / Molecular Structure / Peptides / Receptors, Cytoplasmic and Nuclear / Ultraviolet Rays (徳島大学機関リポジトリ) ● Metadata: 111899 (出版サイトへのリンク) ● Publication site (DOI): 10.1002/cbic.200700442 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17899557 ● Search Scopus @ Elsevier (PMID): 17899557 ● Search Scopus @ Elsevier (DOI): 10.1002/cbic.200700442 (徳島大学機関リポジトリ: 111899, DOI: 10.1002/cbic.200700442, PubMed: 17899557)
70.	H Akeboshi, Y Chiba, Y Kasahara, M Takashiba, Y Takaoka, M Ohsawa, Y Tajima, I Kawashima, Daisuke Tsuji, Kouji Itou, H Sakuraba and Y Jigami : Production of Recombinant {beta}-Hexosaminidase A, a Potential Enzyme for Replacement Therapy for Tay-Sachs and Sandhoff Diseases, in the Methylotrophic Yeast Ogataea minuta., Applied and Environmental Microbiology, Vol.73, No.15, 4805-4812, 2007. (要約) Human beta-hexosaminidase A (HexA) is a heterodimeric glycoprotein composed of alpha- and beta-subunits that degrades GM2 gangliosides in lysosomes. GM2 gangliosidosis is a lysosomal storage disease in which an inherited deficiency of HexA causes the accumulation of GM2 gangliosides. In order to prepare a large amount of HexA for a treatment based on enzyme replacement therapy (ERT), recombinant HexA was produced in the methylotrophic yeast Ogataea minuta instead of in mammalian cells, which are commonly used to produce recombinant enzymes for ERT. The problem of antigenicity due to differences in N-glycan structures between mammalian and yeast glycoproteins was potentially resolved by using alpha-1,6-mannosyltransferase-deficient (och1Delta) yeast as the host. Genes encoding the alpha- and beta-subunits of HexA were integrated into the yeast cell, and the heterodimer was expressed together with its isozymes HexS (alphaalpha) and HexB (betabeta). A total of 57 mg of beta-hexosaminidase isozymes, of which 13 mg was HexA (alphabeta), was produced per liter of medium. HexA was purified with immobilized metal affinity column for the His tag attached to the beta-subunit. The purified HexA was treated with alpha-mannosidase to expose mannose-6-phosphate (M6P) residues on the N-glycans. The specific activities of HexA and M6P-exposed HexA (M6PHexA) for the artificial substrate 4MU-GlcNAc were 1.2 +/- 0.1 and 1.7 +/- 0.3 mmol/h/mg, respectively. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern suggested a C-terminal truncation in the beta-subunit of the recombinant protein. M6PHexA was incorporated dose dependently into GM2 gangliosidosis patient-derived fibroblasts via M6P receptors on the cell surface, and degradation of accumulated GM2 ganglioside was observed. (キーワード) Amino Acid Sequence / Biotechnology / Cells, Cultured / Fibroblasts / Hexosaminidase A / Hexosaminidase B / Humans / Molecular Sequence Data / Recombinant Proteins / Saccharomycetales / Sandhoff Disease / Tay-Sachs Disease / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1128/AEM.00463-07 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17557860 ● Search Scopus @ Elsevier (PMID): 17557860 ● Search Scopus @ Elsevier (DOI): 10.1128/AEM.00463-07 (DOI: 10.1128/AEM.00463-07, PubMed: 17557860)
71.	Kouji Itou : Recent advances in enzyme replacement therapy for lysosomal diseases, Glycoscience Lab Manual, 2007. (出版サイトへのリンク) ● Publication site (DOI): 10.1007/978-4-431-77922-3_53 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.1007/978-4-431-77922-3_53 (DOI: 10.1007/978-4-431-77922-3_53)
72.	T Yoshihara, Y Kadota, Yoshiyuki Yoshimura, Y Tatano, N Takeuchi, H Okitsu, Atsushi Umemoto, Takashi Yamauchi and Kouji Itou : Proteomic alteration in gastic adenocarcinomas from Japanese patients, Molecular Cancer, Vol.5, No.75, 75, 2006. (要約) Gastric adenocarcinomas comprise one of the common types of cancers in Asian countries including Japan. Comprehensive protein profiling of paired surgical specimens of primary gastric adenocarcinomas and nontumor mucosae derived from Japanese patients was carried out by means of two-dimensional gel electrophoresis (2D-EP) and liquid chromatography-electrospray ionic tandem mass spectrometry (LC-ESI-MS) to establish gastric cancer-specific proteins as putative clinical biomarkers and molecular targets for chemotherapy. Relatively common alterations in protein expression were revealed in the tumor tissues. Increases in manganese dismutase and nonhistone chromosomal protein HMG-1 (HMG-1) were observed, while decreases in carbonic anhydrases I and II, glutatione-S-transferase and foveolin precursor (gastrokine-1) (FOV), an 18-kDa stomach-specific protein with putative tumor suppressor activity, were detected. RT-PCR analysis also revealed significant down-regulation of FOV mRNA expression in tumor tissues. A possible pathological role for down-regulation of FOV in gastric carcinogenesis was demonstrated. Evaluation of the specific decreases in gene and protein expression of FOV in patients may be utilized as clinical biomarkers for effective diagnosis and assessment of gastric cancer. (キーワード) Adenocarcinoma / Aged / Asian Continental Ancestry Group / Chromatography, Liquid / Electrophoresis, Gel, Two-Dimensional / Female / Gene Expression Regulation, Neoplastic / Humans / Japan / Male / Middle Aged / Proteome / Proteomics / RNA, Messenger / Reverse Transcriptase Polymerase Chain Reaction / Stomach Neoplasms / Tandem Mass Spectrometry (出版サイトへのリンク) ● Publication site (DOI): 10.1186/1476-4598-5-75 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17187689 ● Search Scopus @ Elsevier (PMID): 17187689 ● Search Scopus @ Elsevier (DOI): 10.1186/1476-4598-5-75 (DOI: 10.1186/1476-4598-5-75, PubMed: 17187689)
73.	Yutaka Tatano, Naohiro Takeuchi, Jun Kuwahara, Hitoshi Sakuraba, Tsutomu Takahashi, Goro Takada and Kouji Itou : Elastogenesis in cultured dermal fibroblasts from patients with lysosomal β-galactosidase, protective protein/cathepsin A and neuraminidase-1 deficiencies, The Journal of Medical Investigation : JMI, Vol.53, No.1-2, 103-112, 2006. (要約) The human GLB1 gene encodes a lysosomal beta-galactosidase (beta-Gal) and an elastin-binding protein (EBP). Defect of the EBP as a chaperon for tropoelastin and a component of receptor complex among neuraminidase-1 (NEU1) and protective protein/cathepsin A (PPCA) is suggested responsible for impaired elastogenesis in autosomal recessive beta-Gal, PPCA and NEU1 deficiencies. The purpose of this study is to determine effects of GLB1, PPCA and NEU1 gene mutations on elastogenesis in skin fibroblasts. Elastic fiber formation and the EBP mRNA expression were examined by immunofluorescence with an anti-tropoelastin antibody and RT-PCR selective for EBP in skin fibroblasts with these lysosomal enzyme deficiencies. Apparently normal elastogenesis and EBP mRNA expression were observed for fibroblasts from Morquio B disease cases with the GLB1 gene alleles (W273L/W273L, W273L/R482H and W273L/W509C substitutions, respectively), a galactosialidosis case with the PPCA allele (IVS7+3A/IVS7+3A) and a sialidosis case with the NEU1 allele (V217M/G243R) as well as normal subject. In this study, the W273L substitution in the EBP could impossibly cause the proposed defect of elastogenesis, and the typical PPCA splicing mutation and the V217M/G243R substitutions in the NEU1 might hardly have effects on elastic fiber formation in the dermal fibroblasts. (キーワード) Base Sequence / Cathepsin A / Cells, Cultured / Elastin / Fibroblasts / Gangliosidoses / Humans / Mucopolysaccharidosis IV / Mutation / Neuraminidase / RNA, Messenger / Receptors, Cell Surface / Skin / beta-Galactosidase (徳島大学機関リポジトリ) ● Metadata: 110794 (出版サイトへのリンク) ● Publication site (DOI): 10.2152/jmi.53.103 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16538002 ● Search Scopus @ Elsevier (PMID): 16538002 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.53.103 (徳島大学機関リポジトリ: 110794, DOI: 10.2152/jmi.53.103, PubMed: 16538002)
74.	Seiichi Aikawa, Fumiko Matsuzawa, Yurie Satoh, Yoshito Kadota, Hirofumi Doi and Kouji Itou : Prediction of the mechanism of action of omuralide (clasto-lactacystin β-lactone) on human cathepsin A based on a structural model of the yeast proteasome β5/PRE2-subunit/omuralide complex., Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol.1764, No.8, 1372-1380, 2006. (要約) Cathepsin A (CathA) is a lysosomal serine carboxypeptidase that exhibits homology and structural similarity to the yeast and wheat serine carboxypeptidases (CPY and CPW) belonging to the alpha/beta-hydrolase fold family. Human CathA (hCathA) and CPW have been demonstrated to be inhibited by a proteasome (threonine protease) inhibitor, lactacystin, and its active derivative, omuralide (clasto-lactacystin beta-lactone), as well as chymostatin. A hCathA/omuralide complex model constructed on the basis of the X-ray crystal structures of the CPW/chymostatin complex and the yeast proteasome beta-subunit (beta5/PRE2)/omuralide one predicted that the conformation of omuralide in the active-site cleft of proteasome beta5/PRE2 should be very similar to that of chymostatin at the S1 catalytic subsites in the hCathA- and CPW-complexes. The relative positions of the glycine residues, i.e., Gly57 in hCathA, Gly53 in CPW, and Gly47 in beta5/PRE2, present in the oxyanion hole of each enzyme were also highly conserved. These results suggest that omuralide might inhibit hCathA and CPW at the S1 subsite in their active-site clefts through direct binding to the active serine residue. (キーワード) Catalytic Domain / Cathepsin A / Cysteine Endopeptidases / Humans / Lactones / Macromolecular Substances / Models, Molecular / Proteasome Endopeptidase Complex / Protein Conformation / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbapap.2006.05.008 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16870514 ● Search Scopus @ Elsevier (PMID): 16870514 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbapap.2006.05.008 (DOI: 10.1016/j.bbapap.2006.05.008, PubMed: 16870514)
75.	Tomohiro Itakura, Aya Kuroki, Yasuhiro Ishibashi, Daisuke Tsuji, Eri Kawashita, Yukari Higashine, Hitoshi Sakuraba, Shoji Yamanaka and Kouji Itou : Inefficiency in GM2 ganglioside elimination by human lysosomal beta-hexosaminidase beta-subunit gene transfer to fibroblastic cell line derived from Sandhoff disease model mice., Biological & Pharmaceutical Bulletin, Vol.29, No.8, 1564-1569, 2006. (要約) Sandhoff disease (SD) is an autosomal recessive GM2 gangliosidosis caused by the defect of lysosomal beta-hexosaminidase (Hex) beta-subunit gene associated with neurosomatic manifestations. Therapeutic effects of Hex subunit gene transduction have been examined on Sandhoff disease model mice (SD mice) produced by the allelic disruption of Hexb gene encoding the murine beta-subunit. We demonstrate here that elimination of GM2 ganglioside (GM2) accumulated in the fibroblastic cell line derived from SD mice (FSD) did not occur when the HEXB gene only was transfected. In contrast, a significant increase in the HexB (betabeta homodimer) activity toward neutral substrates, including GA2 (asialo-GM2) and oligosaccharides carrying the terminal N-acetylglucosamine residues at their non-reducing ends (GlcNAc-oligosaccharides) was observed. Immunoblotting with anti-human HexA (alphabeta heterodimer) serum after native polyacrylamide gel electrophoresis (Native-PAGE) revealed that the human HEXB gene product could hardly form the chimeric HexA through associating with the murine alpha-subunit. However, co-introduction of the HEXA encoding the human alpha-subunit and HEXB genes caused significant corrective effect on the GM2 degradation by producing the human HexA. These results indicate that the recombinant human HexA could interspeciesly associate with the murine GM2 activator protein to degrade GM2 accumulated in the FSD cells. Thus, therapeutic effects of the recombinant human HexA isozyme but not human HEXB gene product could be evaluated by using the SD mice. (キーワード) Animals / Blotting, Western / Cell Line / Fluorescent Antibody Technique / G(M2) Ganglioside / Genetic Vectors / Hexosaminidase A / Hexosaminidase B / Humans / Hydrolysis / Lysosomes / Mice / Sandhoff Disease / Transfection / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1248/bpb.29.1564 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16880605 ● Search Scopus @ Elsevier (PMID): 16880605 ● Search Scopus @ Elsevier (DOI): 10.1248/bpb.29.1564 (DOI: 10.1248/bpb.29.1564, PubMed: 16880605)
76.	H. Sakuraba, M. Sawada, F. Matsuzawa, S. Aikawa, Y. Chiba, Y. Jigami and Kouji Itou : Molecular pathologies of and enzyme replacement therapies for lysosomal diseases., Current Drug Targets. CNS and Neurological Disorders, Vol.5, No.4, 401-413, 2006. (要約) Lysosomal diseases comprise a group of inherited disorders resulting from defects of lysosomal enzymes and their cofactors, and in many of them the nervous system is affected. Recently, enzyme replacement therapy with recombinant lysosomal enzymes has been clinically available for several lysosomal diseases. Such enzyme replacement therapies can improve non-neurological disorders but is not effective for neurological ones. In this review, we discuss the molecular pathologies of lysosomal diseases from the protein structural aspect, current enzyme replacement therapies, and attempts to develop enzyme replacement therapies effective for lysosomal diseases associated with neurological disorders, i.e., production of enzymes, brain-specific delivery and incorporation of lysosomal enzymes into cells. (キーワード) Animals / Culture Media, Conditioned / Enzymes / G(M2) Ganglioside / Humans / Lysosomal Storage Diseases, Nervous System / Lysosomes / Recombinant Fusion Proteins / Sandhoff Disease / Tay-Sachs Disease / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.2174/187152706777950738 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16918392 ● Search Scopus @ Elsevier (PMID): 16918392 ● Search Scopus @ Elsevier (DOI): 10.2174/187152706777950738 (DOI: 10.2174/187152706777950738, PubMed: 16918392)
77.	Y Tatano, T Takahashi, Daisuke Tsuji, N Takeuchi, K Tsuta, G Takada, M Ohsawa, H Sakuraba and Kouji Itou : Significant decrease in tropoelastin gene expression in fibroblasts from a Japanese Costello syndrome patient with impaired elastogenesis and enhanced proliferation., The Journal of Biochemistry, Vol.140, No.2, 193-200, 2006. (要約) Costello syndrome is a connective tissue disorder associated with sparse, thin, and fragmented elastic fibers in tissues. In this study we demonstrated a significant decrease in the expression of tropoelastin mRNA in fibroblasts derived from a Japanese Costello syndrome patient with impaired elastogenesis and enhanced proliferation. In contrast, there were no changes in expression of the Harvey ras (HRAS), fibrillin-1, fibulin-5, microfibril-associated glycoprotein-1 (MAGP-1), lysyl oxidase (LOX), or 67-kDa non-integrin elastin-binding protein (EBP) gene. The proliferative activity of the Costello fibroblasts was about 4-fold higher than that of the normal and pathological control ones. However, no mutations were detected in the coding region of HRAS mRNA. Transduction of the bovine tropoelastin (bTE) gene with the lentiviral vector restored the elastic fiber formation and decreased the growth rate in the Costello fibroblasts. These results strongly suggest that the defect of human tropoelastin (hTE) gene expression should induce the impaired elastogenesis and enhanced proliferation of Costello fibroblasts, and that a primary cause other than the HRAS gene mutation should contribute to the pathogenesis in the present Costello case. (キーワード) Abnormalities, Multiple / Adolescent / Animals / Asian Continental Ancestry Group / Cattle / Cell Proliferation / Connective Tissue Diseases / DNA, Complementary / Elastin / Female / Fibroblasts / Gene Expression Regulation / Humans / RNA, Messenger / Skin / Transduction, Genetic / Tropoelastin (出版サイトへのリンク) ● Publication site (DOI): 10.1093/jb/mvj146 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16829682 ● Search Scopus @ Elsevier (PMID): 16829682 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvj146 (DOI: 10.1093/jb/mvj146, PubMed: 16829682)
78.	Y Oheda, M Kotani, M Murata, H Sakuraba, Y Kadota, Y Tatano, Jun Kuwahara and Kouji Itou : Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement, Glycobiology, Vol.16, No.4, 271-280, 2006. (要約) Sialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) can be specifically detected in cultured fibroblasts from sialidosis and galactosialidosis cases by blotting with a Maackia amurensis (MAM) lectin. We also examined the therapeutic effects of normal gene transfer and enzyme replacement by evaluating the decreases in sialylglycoconjugates accumulated in fibroblasts with these NEU1 deficiencies. The specific N-glycosylated proteins detected on MAM lectin blotting as well as the granular lysosomal fluorescence due to an avidin-FITC/biotinylated MAM lectin conjugate in sialidosis and galactosialidosis fibroblasts disappeared in parallel with the restoration of the intracellular NEU1 activity after transfection of the recombinant NEU1 fused to HA tag sequence and the wild-type PPCA cDNA as well as administration of the recombinant PPCA precursor protein. The detection method for the abnormal sialylglycoproteins in cultured cells involving MAM lectin was demonstrated to be useful not only for biochemical and diagnostic analyses of NEU1 deficiencies but also for therapeutic evaluation of these conditions. (キーワード) Cathepsin A / Cells, Cultured / Evaluation Studies as Topic / Fibroblasts / Gene Therapy / Humans / Mucolipidoses / Neuraminidase / Oligosaccharides / Protein Modification, Translational / Recombinant Fusion Proteins / Sialoglycoproteins / Transfection (出版サイトへのリンク) ● Publication site (DOI): 10.1093/glycob/cwj069 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16361247 ● Search Scopus @ Elsevier (PMID): 16361247 ● Search Scopus @ Elsevier (DOI): 10.1093/glycob/cwj069 (DOI: 10.1093/glycob/cwj069, PubMed: 16361247)
79.	Hitoshi Sakuraba, Mai Murata-Ohsawa, Ikuo Kawashima, Youichi Tajima, Masaharu Kotani, Toshio Ohshima, Yasunori Chiba, Minako Takashiba, Yoshifumi Jigami, Tomoko Fukushige, Tamotsu Kanzaki and Kouji Itou : Comparison of the effects of agalsidase alfa and agalsidase beta on cultured human Fabry fibroblasts and Fabry mice., Journal of Human Genetics, Vol.51, No.3, 180-188, 2006. (要約) We compared two recombinant alpha-galactosidases developed for enzyme replacement therapy for Fabry disease, agalsidase alfa and agalsidase beta, as to specific alpha-galactosidase activity, stability in plasma, mannose 6-phosphate (M6P) residue content, and effects on cultured human Fabry fibroblasts and Fabry mice. The specific enzyme activities of agalsidase alfa and agalsidase beta were 1.70 and 3.24 mmol h(-1) mg protein(-1), respectively, and there was no difference in stability in plasma between them. The M6P content of agalsidase beta (3.6 mol/mol protein) was higher than that of agalsidase alfa (1.3 mol/mol protein). The administration of both enzymes resulted in marked increases in alpha-galactosidase activity in cultured human Fabry fibroblasts, and Fabry mouse kidneys, heart, spleen and liver. However, the increase in enzyme activity in cultured fibroblasts, kidneys, heart and spleen was higher when agalsidase beta was used. An immunocytochemical analysis revealed that the incorporated recombinant enzyme degraded the globotriaosyl ceramide accumulated in cultured Fabry fibroblasts in a dose-dependent manner, with the effect being maintained for at least 7 days. Repeated administration of agalsidase beta apparently decreased the number of accumulated lamellar inclusion bodies in renal tubular cells of Fabry mice. (キーワード) Animals / Cells, Cultured / Disease Models, Animal / Fabry Disease / Fibroblasts / Humans / Isoenzymes / Mice / Mice, Inbred C57BL / Mice, Knockout / Microscopy, Electron / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s10038-005-0342-9 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16372133 ● Search Scopus @ Elsevier (PMID): 16372133 ● Search Scopus @ Elsevier (DOI): 10.1007/s10038-005-0342-9 (DOI: 10.1007/s10038-005-0342-9, PubMed: 16372133)
80.	Mai Murata-Ohsawa, Masaharu Kotani, Youichi Tajima, Daisuke Tsuji, Yasuhiro Ishibashi, Aya Kuroki, Kouji Itou, Kazuhiko Watabe, Kazunori Sango, Shoji Yamanaka and Hitoshi Sakuraba : Establishment of immortalized Schwann cells from Sandhoff mice and corrective effect of recombinant human β-hexosaminidase A on the accumulated GM2 ganglioside., Journal of Human Genetics, Vol.50, No.9, 460-467, 2005. (要約) We have established spontaneously immortalized Schwann cell lines from dorsal root ganglia and peripheral nerves of Sandhoff mice. One of the cell lines exhibited genetically and biochemically distinct features of Sandhoff Schwann cells. The enzyme activities toward 4-methylumbelliferyl N-acetyl-beta-D-glucosamine (beta-hexosaminidases A, B, and S) and 4-methylumbelliferyl N-acetyl-beta-D-glucosamine-6-sulfate (beta-hexosaminidases A and S) were decreased, and GM2 ganglioside accumulated in lysosomes of the cells. Incorporation of recombinant human beta-hexosaminidase isozymes expressed in Chinese hamster ovary cells into the cultured Sandhoff Schwann cells via cation-independent mannose 6-phosphate receptors was found, and the incorporated beta-hexosaminidase A degraded the accumulated GM2 ganglioside. The established Sandhoff Schwann cell line is useful for investigation and development of therapies for Sandhoff disease. (キーワード) Animals / CHO Cells / Cell Culture Techniques / Cricetinae / Cricetulus / Fibroblasts / Gangliosidoses, GM2 / Genotype / Humans / 免疫組織化学 (immunohistochemistry) / Lysosomes / Mice / Mice, Inbred C57BL / Microscopy, Fluorescence / Recombinant Proteins / Sandhoff Disease / Schwann Cells / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s10038-005-0278-0 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16180049 ● Search Scopus @ Elsevier (PMID): 16180049 ● Search Scopus @ Elsevier (DOI): 10.1007/s10038-005-0278-0 (DOI: 10.1007/s10038-005-0278-0, PubMed: 16180049)
81.	Daisuke Tsuji, Aya Kuroki, Yasuhiro Ishibashi, Tomohiro Itakura and Kouji Itou : Metabolic correction in microglia derived from Sandhoff disease model mice., Journal of Neurochemistry, Vol.94, No.6, 1631-1638, 2005. (要約) Sandhoff disease is an autosomal recessive lysosomal storage disease caused by a defect of the beta-subunit gene (HEXB) associated with simultaneous deficiencies of beta-hexosaminidase A (HexA; alphabeta) and B (HexB; betabeta), and excessive accumulation of GM2 ganglioside (GM2) and oligosaccharides with N-acetylglucosamine (GlcNAc) residues at their non-reducing termini. Recent studies have shown the involvement of microglial activation in neuroinflammation and neurodegeneration of this disease. We isolated primary microglial cells from the neonatal brains of Sandhoff disease model mice (SD mice) produced by disruption of the murine Hex beta-subunit gene allele (Hexb-/-). The cells expressed microglial cell-specific ionized calcium binding adaptor molecule 1 (Iba1)-immunoreactivity (IR) and antigen recognized by Ricinus communis agglutinin lectin-120 (RCA120), but not glial fibrillary acidic protein (GFAP)-IR specific for astrocytes. They also demonstrated significant intracellular accumulation of GM2 and GlcNAc-oligosaccharides. We produced a lentiviral vector encoding for the murine Hex beta-subunit and transduced it into the microglia from SD mice with the recombinant lentivirus, causing elimination of the intracellularly accumulated GM2 and GlcNAc-oligosaccharides and secretion of Hex isozyme activities from the transduced SD microglial cells. Recomibinant HexA isozyme isolated from the conditioned medium of a Chinese hamster ovary (CHO) cell line simultaneously expressing the human HEXA (alpha-subunit) and HEXB genes was also found to be incorporated into the SD microglia via cell surface cation-independent mannose 6-phosphate receptor and mannose receptor to degrade the intracellularly accumulated GM2 and GlcNAc-oligosaccharides. These results suggest the therapeutic potential of recombinant lentivirus encoding the murine Hex beta-subunit and the human HexA isozyme (alphabeta heterodimer) for metabolic cross-correction in microglial cells involved in progressive neurodegeneration in SD mice. (キーワード) Animals / Brain / Calcium-Binding Proteins / Dimerization / Disease Models, Animal / Encephalitis / Female / G(M2) Ganglioside / Gene Therapy / Genetic Vectors / Gliosis / Hexosaminidase A / Hexosaminidase B / Humans / Isoenzymes / Lentivirus / Male / Mice / Mice, Inbred C57BL / Mice, Knockout / Microfilament Proteins / Microglia / Protein Subunits / Receptor, IGF Type 2 / Sandhoff Disease / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1471-4159.2005.03317.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16092933 ● Search Scopus @ Elsevier (PMID): 16092933 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1471-4159.2005.03317.x (DOI: 10.1111/j.1471-4159.2005.03317.x, PubMed: 16092933)
82.	Daisuke Tsuji, Aya Kuroki, Yasuhiro Ishibashi, Tomohiro Itakura, Jun Kuwahara, Shoji Yamanaka and Kouji Itou : Specific induction of macrophage inflammatory protein 1-alpha in glial cells of Sandhoff disease model mice associated with accumulation of N-acetylhexosaminyl glycoconjugates., Journal of Neurochemistry, Vol.92, No.6, 1497-1507, 2005. (要約) Sandhoff disease is a lysosomal storage disease caused by simultaneous deficiencies of beta-hexosaminidase A (HexA; alphabeta) and B (HexB; betabeta), due to a primary defect of the beta-subunit gene (HEXB) associated with excessive accumulation of GM2 ganglioside (GM2) and oligosaccharides with N-acetylhexosamine residues at their non-reducing termini, and with neurosomatic manifestations. To elucidate the neuroinflammatory mechanisms involved in its pathogenesis, we analyzed the expression of chemokines in Sandhoff disease model mice (SD mice) produced by disruption of the murine Hex beta-subunit gene allele (Hexb-/-). We demonstrated that chemokine macrophage inflammatory protein-1 alpha (MIP-1alpha) was induced in brain regions, including the cerebral cortex, brain stem and cerebellum, of SD mice from an early stage of the pathogenesis but not in other systemic organs. On the other hand, little changes in other chemokine mRNAs, including those of RANTES (regulated upon activation, normal T expressed and secreted), MCP-1 (monocyte chemotactic protein-1), SLC (secondary lymphoid-tissue chemokine), fractalkine and SDF-1 (stromal derived factor-1), were detected. Significant up-regulation of MIP-1alpha mRNA and protein in the above-mentioned brain regions was observed in parallel with the accumulation of natural substrates of HexA and HexB. Immunohistochemical analysis revealed that MIP-1alpha-immunoreactivity (IR) in the above-mentioned brain regions of SD mice was co-localized in Iba1-IR-positive microglial cells and partly in glial fibrillary acidic protein (GFAP)-IR-positive astrocytes, in which marked accumulation of N-acetylglucosaminyl (GlcNAc)-oligosaccharides was observed from the presymptomatic stage of the disease. In contrast, little MIP-1alpha-IR was observed in neurons in which GM2 accumulated predominantly. These results suggest that specific induction of MIP-1alpha might coincide with the accumulation of GlcNAc-oligosaccharides due to a HexB deficiency in resident microglia and astrocytes in the brains of SD mice causing their activation and acceleration of the progressive neurodegeneration in SD mice. (キーワード) Acetylglucosamine / Animals / Astrocytes / Brain / Calcium-Binding Proteins / Chemokine CCL3 / Chemokine CCL4 / Chemokines / Disease Models, Animal / Disease Progression / G(M2) Ganglioside / Gene Expression Regulation / Glial Fibrillary Acidic Protein / Glycoconjugates / Hexosaminidase A / Hexosaminidase B / Macrophage Inflammatory Proteins / Mice / Mice, Inbred C57BL / Mice, Knockout / Microfilament Proteins / Microglia / Neuroglia / Protein Subunits / RNA, Messenger / Sandhoff Disease / Up-Regulation / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1111/j.1471-4159.2005.02986.x (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15748167 ● Search Scopus @ Elsevier (PMID): 15748167 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1471-4159.2005.02986.x (DOI: 10.1111/j.1471-4159.2005.02986.x, PubMed: 15748167)
83.	Kouhei Ishiwari, Masaharu Kotani, Minoru Suzuki, Elena Pumbo, Akemi Suzuki, Toshihide Kobayashi, Tamaki Ueno, Tomoko Fukushige, Tamotsu Kanzaki, Masato Imada, Kouji Itou, Shinji Akioka, Youichi Tajima and Hitoshi Sakuraba : Clinical, biochemical, and cytochemical studies on a Japanese Salla disease case associated with a renal disorder., Journal of Human Genetics, Vol.49, No.12, 656-663, 2004. (要約) We report the first Japanese case of Salla disease. A 5-year-old male patient developed unique proteinuria with other clinical manifestations, including coarse facies, dysostosis multiplex, mild mitral valve regurgitation, umbilical and inguinal herniation, and mild developmental delay. Pathological analysis of biopsied kidney tissues showed marked vacuolation of podocytes, mesangial cells, capillary endothelial cells, and tubular cells. Biochemical studies involving thin-layer chromatography and mass spectrometry revealed increased excretion of free sialic acid (N-acetylneuraminic acid) into the patient's urine. Immuno- and lectin staining of the patient's cells demonstrated the accumulation of sialyl and asialyl glycoconjugates in lysosomes and late endosomes. A defect in sialyl glycoconjugate metabolism is thought to have occurred in the patient's cells, besides impairment of the lysosomal transport of free sialic acid residues. A renal disorder should be considered as an important manifestation, not only in infantile free sialic acid storage disease but also in Salla disease. (キーワード) Biological Transport / Child, Preschool / Endothelial Cells / Humans / 日本 (Japan) / Kidney Diseases / Kidney Tubules / Lysosomes / Male / N-Acetylneuraminic Acid / Sialic Acid Storage Disease (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s10038-004-0203-y (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15635485 ● Search Scopus @ Elsevier (PMID): 15635485 ● Search Scopus @ Elsevier (DOI): 10.1007/s10038-004-0203-y (DOI: 10.1007/s10038-004-0203-y, PubMed: 15635485)
84.	Yurie Satoh, Yoshito Kadota, Yukako Oheda, Jun Kuwahara, Seiichi Aikawa, Fumiko Matsuzawa, Hirofumi Doi, Takaaki Aoyagi, Hitoshi Sakuraba and Kouji Itou : Microbial serine carboxypeptidase inhibitors - comparative analysis of actions on homologous enzymes derived from man, yeast and wheat ., The Journal of Antibiotics, Vol.57, No.5, 316-325, 2004. (要約) The actions of peptidase inhibitors derived from Streptomycete on human cathepsin A (hCath A), yeast carboxypeptidase Y (CPY), and wheat carboxypeptidase II (CPW) were analyzed comparatively. Lactacystin and omuralide (clasto-lactacystin beta-lactone), well-known cytoplasmic proteasome inhibitors, both had a potent and non-competitive inhibitory effect on these homologous serine carboxypeptidases, although they inhibited CPW and hCath A more effectively than CPY in vitro. Ebelactone B exhibited a mixed non-competitive inhibitory effect and selectivity for CPY. Piperastatin A showed competitive inhibition of CPY and hCath A but had little effect on CPW. In contrast, chymostatin inhibited CPW efficiently, while it had less effect on hCath A and CPY. In cell culture system, lactacystin was the most potent as to inactivation of the intralysosomal recombinant hCath A activity expressed in a genetically engineered fibroblastic cell line with galactosialidosis (hCath A deficiency). These results suggest that the specific inhibitory effects of lactacystin and its derivatives on hCath A might be applicable to elucidate the pathophysiological roles in the human deficinecy. (キーワード) Carboxypeptidases / Cathepsin A / Cell Line / Cysteine Endopeptidases / DNA, Complementary / Dose-Response Relationship, Drug / Fibroblasts / Humans / Immunoblotting / Multienzyme Complexes / Proteasome Endopeptidase Complex / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / Serine Proteinase Inhibitors / Species Specificity / Streptomyces / Triticum (出版サイトへのリンク) ● Publication site (DOI): 10.7164/antibiotics.57.316 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15303492 ● Search Scopus @ Elsevier (PMID): 15303492 ● Search Scopus @ Elsevier (DOI): 10.7164/antibiotics.57.316 (DOI: 10.7164/antibiotics.57.316, PubMed: 15303492)
85.	Kouji Itou, Yurie Satoh, Yoshito Kadota, Yukako Oheda, Jun Kuwahara, Michie Shimmoto and Sakuraba Hitoshi : Expression of lysosomal protective protein/cathepsin A in a stably transformed human neuroblastoma cell line during bi-directional differentiation into neuronal and Schwannian cells., Neurochemistry International, Vol.44, No.6, 447-457, 2004. (要約) Human neuroblastoma GOTO cell lines were established that stably express recombinant human lysosomal protective protein/cathepsin A (PPCA) cDNA by transfection. Intracellular cathepsin A (acid serine carboxypeptidase) activity increased four-fold compared with in those of the parent and mock-transfected cell lines. The immunoreactive 54 kDa precursor/zymogen and mature 32/20 kDa two-chain forms were produced in the cells. The amount of the latter form expressed in the GOTO cells was significantly larger than those in the PPCA-overexpressing CHO cell lines previously established. The intracellular proteins showed a typical lysosomal granular distribution and the glycosylated 54 kDa precursor was secreted into the culture medium without the addition of an alkalizing agent. The PPCA-overexpressing cell lines also retained the ability to differentiate bi-directionally as well as the parent cells; into neuronal cells on induction by dibutyryl cAMP in serum-free medium and into Schwannian cells on induction by bromodeoxyuridine. During the course of differentiation into neuronal and Schwannian cells, the intracellular cathepsin A activity further increased two and five times, respectively, which was associated with an increase in the expression of the 32/20 kDa two-chain form. The glycosylated precursor proteins were taken up via the mannose 6-phosphate receptors, and the cathepsin A, alpha-neuraminidase and beta-galactosidase (beta-Gal) activities deficient in the fibroblasts derived from a patient with PPCA deficiency (galactosialidosis) were restored. These results suggest that the bi-directional differentiation of GOTO cell lines stably expressing the recombinant human PPCA gene could be a model system for analyzing the functions of PPCA in peripheral neuronal cells and Schwannian cells as well as the recombinant PPCA could be a useful source for enzyme replacement therapy (ERT) for galactosialidosis patients. (キーワード) Cathepsin A / Cell Differentiation / Cell Transformation, Neoplastic / Electrophoresis, Polyacrylamide Gel / Fluorescent Antibody Technique, Indirect / Humans / Lysosomes / Neuroblastoma / Neurons / Recombinant Proteins / Schwann Cells (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.neuint.2003.07.001 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14687610 ● Search Scopus @ Elsevier (PMID): 14687610 ● Search Scopus @ Elsevier (DOI): 10.1016/j.neuint.2003.07.001 (DOI: 10.1016/j.neuint.2003.07.001, PubMed: 14687610)
86.	Midori Itoh, Jun Kuwahara, Kouji Itou, Yu-ichi Fukuda, Mikiko Kohya, Mitsuru Shindo and Kozo Shishido : Apoptosis-inducing activity of synthetic intermediates of halichlorine., Bioorganic & Medicinal Chemistry Letters, Vol.12, No.16, 2069-2072, 2002. (要約) Synthetic intermediates of alkaloid halichlorine with the azaspiro core structure have been found to induce apoptosis of cultured human cells including an acute monocytic leukemia cell line (THP-1) at micromolar concentrations. The novel biological activity of the intermediates was suggested to depend on the skeletal structure and silyloxymethyl functionality on the five-membered ring. (キーワード) PINNAIC ACID / SPIROCYCLIC CORE / VCAM-1 INDUCTION / CASPASE FAMILY / HALICHLORINE / INHIBITOR / STEREOCHEMISTRY / SPECIFICITIES / CONSTRUCTION / EXPRESSION (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0960-894X(02)00373-6 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12127506 ● Search Scopus @ Elsevier (PMID): 12127506 ● Search Scopus @ Elsevier (DOI): 10.1016/S0960-894X(02)00373-6 (DOI: 10.1016/S0960-894X(02)00373-6, PubMed: 12127506)
87.	Kouji Itou, Yasunori Naganawa, Fumiko Matuzawa, Seiichi Aikawa, Hirofumi Doi, Naokazu Sasagasako, Takeshi Yamada, Jun-ichi Kira, Takuro Kobayashi, Alexey V. Pshezhetsky and Hitoshi Sakuraba : Novel missense mutaitions in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes., Journal of Human Genetics, Vol.47, No.1, 29-37, 2002. (要約) Three novel missense mutations in the human lysosomal sialidase gene causing amino acid substitutions (P80L, W240R. and P316S) in the coding region were identified in two Japanese sialidosis patients. One patient with a severe, congenital form of type 2 sialidosis was a compound heterozygote for 239C-to-T (P80L) and 718T-to-C (W240R). The other patient with a mild juvenile-onset phenotype (type 1) was a homozygote for the base substitution of 946C-to-T (P316S). None of these mutant cDNA products showed enzymatic activity toward an artificial substrate when coexpressed in galactosialidosis fibroblastic cells together with protective protein/cathepsin A (PPCA). All mutants showed a reticular immunofluorescence distribution when coexpressed with the PPCA gene in COS-1 cells, suggesting that the gene products were retained in the endoplasmic reticulum/Golgi area or rapidly degraded in the lysosomes. Homology modeling of the structural changes introduced by the mutations predicted that the P80L and P316S transversions cause large conformational changes including the active site residues responsible for binding the sialic acid carboxylate group. The W240R substitution was deduced to influence the molecular surface structure of a limited region of the constructed models, which was also influenced by previously identified V217M and G243R transversions. (キーワード) Adult / Amino Acid Substitution / Animals / COS Cells / Cercopithecus aethiops / Crystallography, X-Ray / DNA / DNA Primers / Female / Humans / Immunoenzyme Techniques / Infant / Lysosomes / Male / Models, Molecular / Mucolipidoses / Mutation / Mutation, Missense / Neuraminidase / Phenotype / Pregnancy / Prenatal Diagnosis / Protein Conformation / Reverse Transcriptase Polymerase Chain Reaction (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s10038-002-8652-7 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11829139 ● Search Scopus @ Elsevier (PMID): 11829139 ● Search Scopus @ Elsevier (DOI): 10.1007/s10038-002-8652-7 (DOI: 10.1007/s10038-002-8652-7, PubMed: 11829139)
88.	Yasunori Naganawa, Kouji Itou, Michie Shimmoto, Kyoko Takiguchi, Hirofumi Doi, Yuzuru Nishizawa, Takayoshi Kobayashi, Sachiko Kamei, Alexey V. Pshezhetsky, M. Potier and Hitoshi Sakuraba : Molecular and structural studies of Japanese patients with sialidosis type 1., Journal of Human Genetics, Vol.45, No.4, 241-249, 2000. (要約) To gain insight into the pathogenesis of sialidosis type 1, we performed molecular investigations of two unrelated Japanese patients. Both of them are compound heterozygotes for base substitutions of 649G-to-A and 727G-to-A, which result in amino acid alterations V217M and G243R, respectively. Using homology modeling, the structure of human lysosomal neuraminidase was constructed and the structural changes caused by these missense mutations were deduced. The predicted change due to V217M was smaller than that caused by G243R, the latter resulting in a drastic, widespread alteration. The overexpressed gene products containing these mutations had the same molecular weight as that of the wild type, although the amounts of the products were moderately decreased. A biochemical study demonstrated that the expressed neuraminidase containing a V217M mutation was partly transported to lysosomes and showed residual enzyme activity, although a G243R mutant was retained in the endoplasmic reticulum/Golgi area and had completely lost the enzyme activity. Considering the data, we surmise that the V217M substitution may be closely associated with the phenotype of sialidosis type 1 with a late onset and moderate clinical course. (キーワード) Adult / Animals / COS Cells / X線結晶学 (X-ray crystallography) / Female / Humans / Immunoblotting / 免疫組織化学 (immunohistochemistry) / Male / Models, Molecular / Mucolipidoses / Mutation, Missense / Neuraminidase / Polymerase Chain Reaction / Protein Conformation / Sequence Analysis, DNA (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s100380070034 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10944856 ● Search Scopus @ Elsevier (PMID): 10944856 ● Search Scopus @ Elsevier (DOI): 10.1007/s100380070034 (DOI: 10.1007/s100380070034, PubMed: 10944856)
89.	Kyoko Takiguchi, Kouji Itou, Michie Shimmoto, Pinar T. Ozand, Hirofumi Doi and Hitoshi Sakuraba : Structural and functional study of K453E mutant protective protein/cathepsin A causing the late infantile form of galactosialidosis., Journal of Human Genetics, Vol.45, No.4, 200-206, 2000. (要約) To clarify the molecular basis of the late infantile form of galactosialidosis, we characterized a defective protective protein/cathepsin A (PPCA) gene product with the K453E mutation newly found in an Arabic patient with this disease. Immunocytochemical, expression, and metabolic studies revealed that the precursor PPCA was synthesized but not processed to the mature form, and it was degraded in the mutant. A structural model of the mutant PPCA was constructed by amino acid substitution of 453glutamic acid for lysine in the crystal structure of the wild type PPCA precursor reported. The results show that the K453E mutation is located at the dimer interface of the PPCA and reduces the hydrogen bond formation in the dimer. This structural change may cause instability of the PPCA dimer. (キーワード) Amino Acid Substitution / Blotting, Northern / Carboxypeptidases / Cathepsin A / 子ども (children) / X線結晶学 (X-ray crystallography) / European Continental Ancestry Group / Female / Glutamic Acid / Humans / 免疫組織化学 (immunohistochemistry) / Lysine / Metabolism, Inborn Errors / Models, Molecular / Mutation, Missense / Neuraminidase / Protein Structure, Quaternary / beta-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s100380070027 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10944848 ● Search Scopus @ Elsevier (PMID): 10944848 ● Search Scopus @ Elsevier (DOI): 10.1007/s100380070027 (DOI: 10.1007/s100380070027, PubMed: 10944848)
90.	Ryoichi Kase, Uwe Bierfreund, Andreas Klein, Thomas Kolter, Kouichi Utsumi, Kouji Itou, Konrad Sandhoff and Hitoshi Sakuraba : Characterization of two α-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease., Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Vol.1501, No.2-3, 227-235, 2000. (要約) The mutant products Q279E ((279)Gln to Glu) and R301Q ((301)Arg to Gln) of the X-chromosomal inherited alpha-galactosidase (EC 3.2.1. 22) gene, found in unrelated male patients with variant Fabry disease (late-onset cardiac form) were characterized. In contrast to patients with classic Fabry disease, who have no detectable alpha-galactosidase activity, atypical variants have residual enzyme activity. First, the properties of insect cell-derived recombinant enzymes were studied. The K(m) and V(max) values of Q279E, R301Q, and wild-type alpha-galactosidase toward an artificial substrate, 4-methylumbelliferyl-alpha-D-galactopyranoside, were almost the same. In order to mimic intralysosomal conditions, the degradation of the natural substrate, globotriaosylceramide, by the alpha-galactosidases was analyzed in a detergent-free-liposomal system, in the presence of sphingolipid activator protein B (SAP-B, saposin B). Kinetic analysis revealed that there was no difference in the degradative activity between the mutants and wild-type alpha-galactosidase activity toward the natural substrate. Then, immunotitration studies were carried out to determine the amounts of the mutant gene products naturally occurring in cells. Cultured lymphoblasts, L-57 (Q279E) and L-148 (R301Q), from patients with variant Fabry disease, and L-20 (wild-type) from a normal subject were used. The 50% precipitation doses were 7% (L-57) and 10% (L-148) of that for normal lymphoblast L-20, respectively. The residual alpha-galactosidase activity was 3 and 5% of the normal level in L-57 and L-148, respectively. The quantities of immuno cross-reacting materials roughly correlated with the residual alpha-galactosidase activities in lymphoblast cells from the patients. Compared to normal control cells, fibroblast cells from a patient with variant Fabry disease, Q279E mutation, secreted only small amounts of alpha-galactosidase activity even in the presence of 10 mM NH(4)Cl. It is concluded that Q279E and R301Q substitutions do not significantly affect the enzymatic activity, but the mutant protein levels are decreased presumably in the ER of the cells. (キーワード) Ammonium Chloride / Cells, Cultured / Enzyme Stability / Fabry Disease / Galactosides / Glycoproteins / Humans / Kinetics / Liposomes / Male / Mutation / Precipitin Tests / Recombinant Proteins / Saposins / Sphingolipid Activator Proteins / Trihexosylceramides / Umbelliferones / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0925-4439(00)00024-7 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10838196 ● Search Scopus @ Elsevier (PMID): 10838196 ● Search Scopus @ Elsevier (DOI): 10.1016/S0925-4439(00)00024-7 (DOI: 10.1016/S0925-4439(00)00024-7, PubMed: 10838196)
91.	Keiko Ohsugi, Keiko Kobayashi, Kouji Itou, Hitoshi Sakuraba and Noriko Sakuragawa : Enzymatic corrections for cells derived from Fabry disease patients by a recombinant adenovirus vector., Journal of Human Genetics, Vol.45, No.1, 1-5, 2000. (要約) Fabry disease is an X-linked inherited metabolic disorder caused by a deficiency of alpha-galactosidase (alpha-gal), resulting in the accumulation of ceramide trihexoside (CTH) in body fluids and in many organs and tissues. We constructed a recombinant adenovirus with a human alpha-gal cDNA (AxCAG alpha-gal), and transfected this vector to skin fibroblasts from Fabry patients. Transfected cells expressed high amounts of alpha-gal in their cytoplasm, and a high level of alpha-gal activity was detected in the medium. The accumulated CTH in the fibroblasts disappeared 3 days after infection. The secreted alpha-gal also eliminated the accumulated CTH from uninfected patient's cells. The enzyme may be taken up through mannose-6-phosphate receptors, as the addition of mannose-6-phosphate to the medium completely inhibited the uptake of the enzyme. The infected cells continued to express alpha-gal for more than 10 days. These results suggest that AxCAG alpha-gal could be used as enzyme replacement gene therapy for Fabry disease. (キーワード) Adenoviridae / DNA, Recombinant / Fabry Disease / Fibroblasts / 遺伝子治療 (gene therapy) / Genetic Vectors / Humans / Skin / Transfection / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1007/s100380050001 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10697955 ● Search Scopus @ Elsevier (PMID): 10697955 ● Search Scopus @ Elsevier (DOI): 10.1007/s100380050001 (DOI: 10.1007/s100380050001, PubMed: 10697955)
92.	Kouji Itou, K Oyanagi, H. Takahashi, T. Sato, Y. Hashizume, M. Shimmoto and H. Sakuraba : Abnormal distribution of endothelin-1 in the cerebellum affected by galactosialidosis., Annals of Neurology, Vol.47, No.1, 122-126, 2000. (要約) Endothelin-1 is a peptidic substrate in vitro of lysosomal protective protein/cathepsin A (PPCA) with serine carboxypeptidase activity. Endothelin-1-specific immunoreactivity has been demonstrated to be markedly increased and distributed abnormally in the neurons and glial cells within autopsied brain regions, including the cerebellum, hippocampal formation, and spinal cord, of patients affected with galactosialidosis, a human PPCA deficiency. The genetic defect of the endothelin-1 degrading activity of PPCA is suggested to cause some of the neurological abnormalities of this disease. (キーワード) Adenosine Diphosphate / Adolescent / Adult / Brain / Child / Child, Preschool / Endothelin-1 / Humans / Immunohistochemistry / Lysosomal Storage Diseases / Male / beta-Galactosidase (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10632112 ● Search Scopus @ Elsevier (PMID): 10632112 (PubMed: 10632112)
93.	Jun Kuwahara, Yasuo Watanabe, Takashi Kayasuga and Kouji Itou : Zn finger and nuclear localization of transcription factor Sp1, Nucleic Acids Symposium Series, No.44, 265-266, 2000. (要約) Transcription factor Sp1 is located in the nucleus of a mammalian cell and importantly related to expression of many cellular genes. In order to elucidate the nuclear localization mechanism of Sp1, various truncated fragments of Sp1 were fused to green fluorescent protein (GFP) and expressed in HeLa cell. The results show significance of the DNA binding region, especially, zinc finger (Zn finger) domain for nuclear localization of Sp1 in HeLa cell. (キーワード) Binding Sites / Cell Nucleus / Green Fluorescent Proteins / HeLa Cells / Humans / Luminescent Proteins / Molecular Structure / Nuclear Localization Signals / Peptide Fragments / Podophyllin / Podophyllotoxin / Protein Structure, Tertiary / Recombinant Fusion Proteins / Zinc Fingers (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12903370 ● Summary page in Scopus @ Elsevier: 2-s2.0-0141782147 (PubMed: 12903370, Elsevier: Scopus)
94.	Yasunori Naganawa, Kouji Itou, Michie Shimmoto, Sachiko Kamei, Kyoko Takiguchi, Hirofumi Doi and Hitoshi Sakuraba : Stable expression of protective protein/cathepsin A-green fluorescent protein fusion genes in a fibroblastic cell line from a galactosialidosis patient., The Biochemical Journal, Vol.340, 467-474, 1999. (要約) Fibroblastic cell lines derived from a galactosialidosis patient, stably expressing the chimaeric green fluorescent protein variant (EGFP) gene fused to the wild-type and mutant human lysosomal protective protein/cathepsin A (PPCA) cDNA, were first established as a model system for revealing the sorting and processing of lysosomal enzymes and for investigating the molecular bases of their deficiencies. In the cell line expressing the wild-type PPCA-EGFP chimaera gene (EGFP-PPwild), an 81 kDa form (27 kDa EGFP fused to the C-terminus of the 54 kDa PPCA precursor) was produced, then processed into the mature 32/20 kDa two-chain form free of the EGFP domain. The intracellular cathepsin A, alpha-N-acetylneuraminidase and beta-galactosidase activities, which are deficient in the parent fibroblastic cells, could also be significantly restored in the cells. In contrast with the uniform and strong fluorescence throughout the cytoplasm and nucleus in the mock-cell line expressing only EGFP cDNA, weak reticular and punctate fluorescence was distributed throughout the EGFP-PPwild cell line. Bafilomycin A1, a potent inhibitor of vacuolar ATPase and intracellular acidification, induced the distribution of Golgi-like perinuclear fluorescence throughout the living and fixed cells, in which only the 81 kDa product was detected. After removal of the agent, time-dependent transport of the chimaeric protein from the Golgi apparatus to the prelysosomal structure in living cells was monitored with a confocal laser scanning microscope system. Leupeptin caused the distribution of lysosome-like granular fluorescence throughout the cytoplasm in the fixed cells, although it was hardly observed in living cells. The latter agent also dose-dependently induced an increase in the intracellular amount of the 81 kDa product containing the EGFP domain and inhibited the restoration of cathepsin A activity in the EGFP-PPwild cells after the removal of bafilomycin A1. In parallel, both the mature two-chain form and PPCA function disappeared. These results suggested that the chimaera gene product was transported to acidic compartments (endosomes/lysosomes), where proteolytic processing of the PPCA precursor/zymogen, quenching of the fluorescence, and random degradation of the EGFP portion occurred. A cell line stably expressing a chimaeric gene with a mutant PPCA cDNA containing an A1184-->G (Y395C) mutation, commonly detected in Japanese severe early-infantile type of galactosialidosis patients, showed an endoplasmic reticulum (ER)-like reticular fluorescence pattern. The PPCA-immunoreactive gene product was hardly detected in this cell line. The mutant chimaeric product was suggested to be degraded rapidly in the ER before transport to post-ER compartments. A cell line expressing the chimaeric gene with a T746-->A (Y249N) PPCA mutation exhibited both ER-like reticular and granular fluorescence on the reticular structure that was stronger than that in the EGFP-PPwild cells. Some of them contained large fluorescent inclusion-body-like structures. The ineffectiveness of transport inhibitors in the distribution changes in the two mutant chimaeric proteins suggested that they were not delivered to acidic compartments. Therefore this expression system can possibly be applied to the direct analysis of the sorting defects of mutant gene products in living cells and will be useful for the molecular investigation of lysosomal diseases, including galactosialidosis. (キーワード) Amino Acid Sequence / Anti-Bacterial Agents / Base Sequence / Biological Transport / Carboxypeptidases / Cathepsin A / Cell Line / DNA, Complementary / Fibroblasts / Green Fluorescent Proteins / Humans / Leupeptins / Luminescent Proteins / Lysosomal Storage Diseases / Lysosomes / Macrolides / Microscopy, Fluorescence / Models, Biological / Molecular Sequence Data / Mutation / Protein Processing, Post-Translational / Recombinant Fusion Proteins (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10333491 ● Search Scopus @ Elsevier (PMID): 10333491 (PubMed: 10333491)
95.	Osamu Sohma, Masashi Mizuguchi, Sachio Takashima, Akira Satake, Kouji Itou, Hitoshi Sakuraba, Yoshiyuki Suzuki and Kiyomitsu Oyanagi : Expression of protective protein in human tissue., Pediatric Neurology, Vol.20, No.3, 210-214, 1999. (要約) The authors investigated by immunohistochemistry the distribution of protective protein in human tissues. Immunoreactivity was observed in the cytoplasm, revealing a granular pattern and cell type specificity. The most intense staining was observed in the large neurons of brain, distal and collecting tubular cells of kidney, epithelial cells of bronchus, and Leydig cells of testis. In a patient with galactosialidosis type IIa, all these stains were absent. The neurons that were most strongly stained in the control group, such as the Betz cells, neurons in the basal forebrain, motor neurons in the cranial nerve nuclei, and ventral horn cells of the spinal cord, were markedly ballooned in the patient with galactosialidosis. (キーワード) Adolescent / Brain Chemistry / Bronchi / Carboxypeptidases / Cathepsin A / Cell Nucleus / 子ども (children) / Glycoproteins / Humans / 免疫組織化学 (immunohistochemistry) / Kidney / Lysosomal Storage Diseases / Male / Neuraminidase / Neurons / 脊髄 (spinal cord) / Testis / beta-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0887-8994(98)00151-9 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10207930 ● Search Scopus @ Elsevier (PMID): 10207930 ● Search Scopus @ Elsevier (DOI): 10.1016/S0887-8994(98)00151-9 (DOI: 10.1016/S0887-8994(98)00151-9, PubMed: 10207930)
96.	H Sakuraba, Kouji Itou, M Shimmoto, K Utsumi, R Kase, Y Hashimoto, T Ozawa, Y Ohwada, G Imataka, M Eguchi, T Furukawa, U Schepers and K Sandhoff : GM2 gangliosidosis AB variant: Clinical and biochemical studies of a Japanese patient ., Neurology, Vol.52, No.2, 372-377, 1999. (要約) To determine the clinical features and biochemical basis of the first Japanese patient with the GM2 gangliosidosis AB variant. The clinical manifestations and laboratory findings in the patient were investigated. Cultured fibroblasts from the patient were analyzed by means of immunofluorescence staining with an anti-GM2 ganglioside monoclonal antibody and thin-layer chromatography and immunostaining. GM1 ganglioside catabolism in cultured cells was analyzed by pulse labeling, and the amount of GM2 activator in cells was determined by Western blot analysis. Gene analysis was performed according to standard protocols. The patient showed progressive neurologic manifestations of quite early onset. Muscular weakness and hypotonia became evident by 1 month of age, and the patient then developed a startle reaction, severe psychomotor retardation, and myoclonic seizures. Immunocytochemical analysis clearly revealed the accumulation of GM2 ganglioside in cultured fibroblasts from the patient, and thin-layer chromatography confirmed it. Western blot and metabolic studies showed a complete deficiency of GM2 activator. Gene analysis did not reveal any mutations in the protein coding region of the GM2 activator gene. The clinical features and biochemical basis of this Japanese patient with GM2 gangliosidosis AB variant were determined. Immunocytochemical analysis using cultured fibroblasts as samples is available for the diagnosis of this disease. (キーワード) Anticonvulsants / Blotting, Western / Cells, Cultured / Chromatography, Thin Layer / Electroencephalography / Epilepsies, Myoclonic / Fibroblasts / G(M2) Ganglioside / Gangliosidoses / Genetic Variation / Humans / 免疫組織化学 (immunohistochemistry) / 小児 (infant) / 日本 (Japan) / Male / Psychomotor Performance / Pyridoxine (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9932959 ● Search Scopus @ Elsevier (PMID): 9932959 (PubMed: 9932959)
97.	Kouichi Utsumi, Kouji Itou, Ryoichi Kase, Michie Shimmoto, Naomasa Yamamoto, Yasuhiro Katagiri, Kenjiro Tanoue, Masaharu Kotani, Takashi Ozawa, Tomomasa Oguchi and Hitoshi Sakuraba : Urinary excretion of the vitronectin receptor (integrin αvβ3) in patients with Fabry disease., Clinica Chimica Acta, Vol.279, No.1-2, 55-68, 1999. (要約) A renal disorder is one of the important manifestations of Fabry disease, but the details of the pathogenesis have not been clarified yet. We examined the possibility that the vitronectin receptor (VNR, integrin alpha V beta 3), one of the integrins, is involved in the progression of the renal injury in Fabry disease. We measured the urinary excretion of beta 3 originating from VNR in Fabry patients by immunoblotting analysis and enzyme-linked immunosorbent assay (ELISA). Immunofluorescent microscopic analyses for VNR and globotriaosylceramide were performed on urinary sediments from Fabry patients. Furthermore, beta 3 and vitronectin in kidney tissues were analyzed immunohistochemically. Immunoblotting analysis and ELISA showed that the urinary excretion of beta 3 originating from VNR was significantly increased in the Fabry group compared with both the pathological and healthy control groups. Immunofluorescent microscopy revealed the expression of VNR and accumulation of globotriaosylceramide in urinary sediments from the Fabry patients. Increased expression of beta 3 was observed in glomerular epithelial cells, and in Bowman's capsular epithelial layer and tubular cells, and the amount of vitronectin was moderately increased in the kidney tissues from the Fabry patients. The urinary excretion of VNR was increased, and the expression of VNR was observed in Fabry kidney tissues. The expression of VNR may be involved in the progression of the renal injury in this disease. (キーワード) Adolescent / Adult / Child / Disease Progression / Enzyme-Linked Immunosorbent Assay / Fabry Disease / Female / Fluorescent Antibody Technique, Direct / Humans / Immunoblotting / Kidney Diseases / Male / Middle Aged / Receptors, Vitronectin / Vitronectin (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0009-8981(98)00169-7 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10064118 ● Search Scopus @ Elsevier (PMID): 10064118 ● Search Scopus @ Elsevier (DOI): 10.1016/S0009-8981(98)00169-7 (DOI: 10.1016/S0009-8981(98)00169-7, PubMed: 10064118)
98.	Kouji Itou, Yasunori Naganawa, Sachiko Kamei, Michie Shimmoto and Hitoshi Sakuraba : Stabilizing effect of lysosomal β-galactosidase on the catalytic activity of protective protein/cathepsin A secreted by human platelets., Biochemical and Biophysical Research Communications, Vol.253, No.2, 228-234, 1998. (要約) The 32/20-kDa two-chain form of protective protein/cathepsin A (CathA) secreted by human platelets was thermostable in the aggregation supernatant at acidic pH, but was denatured at neutral pH. Leupeptin partly protected the CathA against denaturation, which was not observed in the supernatant after depletion of the cosecreted lysosomal acid beta-galactosidase (beta-Gal) by affinity separation with p-aminophenylthiogalactose (PATG)-agarose beads even at pH 4.8. The purified recombinant human beta-Gal proteins, the 84-kDa precursor and 64-kDa mature-like enzyme (the tryptic product of the 84-kDa precursor), also protected the CathA against denaturation at neutral pH in part. Biospecific interaction analysis revealed that the CathA secreted by platelets dose dependently bound to the immobilized recombinant beta-Gal proteins. The association rate constant of CathA with the 64-kDa mature-like beta-Gal was 4.0 x 10(6) (M-1 s-1) at acidic pH, which was three times larger than that with the 84-kDa beta-Gal precursor. The calculated affinity constants for the enzyme molecules at acidic pH were approximately 1 x 10(9) (M-1), and those at neutral pH were two orders lower. These results first demonstrated that beta-Gal stabilizes the catalytic activity of CathA through direct binding in vitro. The affinity was shown to increase with removal of the carboxy-terminal domain of the beta-Gal precursor. (キーワード) Blood Platelets / Carboxypeptidases / Catalysis / Cathepsin A / Cell-Free System / Enzyme Stability / Extracellular Space / Hot Temperature / Humans / Hydrogen-Ion Concentration / Lysosomes / Platelet Aggregation / Protein Denaturation / Recombinant Proteins / beta-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1006/bbrc.1998.9696 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9878520 ● Summary page in Scopus @ Elsevier: 2-s2.0-0032545333 (DOI: 10.1006/bbrc.1998.9696, PubMed: 9878520, Elsevier: Scopus)
99.	Kouji Itou, Michie Shimmoto, Kouichi Utsumi, Nobuyuki Mizoguchi, Norio Miharu, Koso Ohama and Hitoshi Sakuraba : Protective protein/cathepsin A loss in cultured cells derived from an early-infantile form of galactosialidosis patients homozygous for the A1184-G transition (Y395C mutation)., Biochemical and Biophysical Research Communications, Vol.247, No.1, 12-17, 1998. (要約) Galactosialidosis is a human autosomal recessive lysosomal storage disease caused by a genetic defect of protective protein/cathepsin A (PPCA). The patients in a Japanese family with the severe early-infantile form of galactosialidosis were revealed to be homozygous for the A1184-G transition in the PPCA gene in both alleles, which leads to the Y395C substitution. The acid carboxypeptidase (cathepsin A) and lysosomal neuraminidase activities were markedly decreased in cultured fibroblasts and chorionic villus cells derived from the patients, although the decrease in beta-galactosidase activity was less. Immunoblot and immunocytochemical analyses showed that neither the precursor nor the mature form of the PPCA gene product was present in the cultured cells. The Y395C mutation was revealed to cause the loss of the translated product, that determines the severity of the clinical phenotype. (キーワード) Amino Acid Substitution / Antibodies / Carboxypeptidases / Cathepsin A / Cells, Cultured / Cysteine / Female / Fluorescent Antibody Technique, Indirect / Genotype / Homozygote / Humans / Immunoblotting / Infant / Lysosomal Storage Diseases / Lysosomes / Male / Pedigree / Point Mutation / Tyrosine (出版サイトへのリンク) ● Publication site (DOI): 10.1006/bbrc.1998.8659 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9636645 ● Summary page in Scopus @ Elsevier: 2-s2.0-0032499617 (DOI: 10.1006/bbrc.1998.8659, PubMed: 9636645, Elsevier: Scopus)
100.	Ryoichi Kase, Michie Shimmoto, Kouji Itou, Kouichi Utsumi, Masaharu Kotani, Choji Taya, Hiromichi Yonekawa and Hitoshi Sakuraba : Immunohistochemical characterization of transgenic mice highly expressing human lysosomal α-galactosidase., Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Vol.1406, No.3, 260-266, 1998. (要約) Human lysosomal alpha-galactosidase predominantly hydrolyzes ceramide trihexoside. A transgenic mouse line, C57BL/6CrSIc-TgN(GLA) 1951 Rin, highly expressing human alpha-galactosidase, has been established and investigated biochemically and immunohistochemically in order to clarify the distribution of the expressed enzyme proteins and to evaluate it as a donor model of organ transplantation therapy for Fabry disease caused by a genetic defect of alpha-galactosidase. In these transgenic mice, about five copies of the transgene were integrated, and alpha-galactosidase activity was expressed in liver, kidney, heart, spleen, small intestine, submaxillary gland, skeletal muscle, cerebrum, cerebellum, bone marrow cells and serum. The enzyme activity was about 22 to 11,080-fold higher than that in non-transgenic mice. In liver, heart and kidney tissues, which are important organs for transplantation studies, sufficient amounts of alpha-galactosidase mRNAs were transcribed, and the expressed enzymes, with molecular weights of 54-60 kDa, are abundant in the liver (enzyme activity: 53,965 nmol h-1 mg-1 protein) and heart (39,906 nmol h-1 mg-1 protein), followed by in the kidney tissue (9177 nmol h-1 mg-1 protein), respectively. An immunohistochemical microscopic study clearly demonstrated the distribution of the expressed enzyme proteins in kidney and liver tissues. Highly expressed alpha-galactosidase was detected in glomerular cells, tubular cells and hepatocytes. These transgenic mice will be useful as a donor model for experimental organ transplantation, and also it will enable recurrent biopsies and long-term observation. The organ transplantation data on mice will provide us with important information. (キーワード) Animals / Blotting, Northern / Blotting, Southern / Blotting, Western / Female / Gene Expression / Humans / Immunohistochemistry / Kidney / Liver / Lysosomes / Mice / Mice, Inbred C57BL / Mice, Transgenic / Myocardium / Organ Specificity / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0925-4439(98)00012-X (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9630664 ● Search Scopus @ Elsevier (PMID): 9630664 ● Search Scopus @ Elsevier (DOI): 10.1016/S0925-4439(98)00012-X (DOI: 10.1016/S0925-4439(98)00012-X, PubMed: 9630664)
101.	A. Hara, Eiichiro Uyama, M. Uchino, Michie Shimmoto, K. Utsumi, Kouji Itou, Ryoichi Kase, M. Naito, E. Sugiyama, T. Taketomi, K. Sukegawa and H. Sakuraba : Adult Sandhoff disease: R505Q and I207V substitutions in the HEXB gene of the first Japanese case., Journal of the Neurological Sciences, Vol.155, No.1, 86-91, 1998.
102.	Toshika Okumiya, O. Kawamura, Kouji Itou, R. Kase, S. Ishi, S. Kamei and H. Sakuraba : Novel missence mutation (M72V) of α-galactosidase gene and its expression product in an atypical Fabry hemizygote., Human Mutation, Vol.Suppl 1, S213-S216, 1998. (キーワード) Adult / Amino Acid Substitution / Animals / COS Cells / DNA (DNA) / DNA Mutational Analysis / Fabry Disease / Gene Expression Regulation, Enzymologic / Heterozygote / Humans / Male / Methionine / Mutation, Missense / Point Mutation / Valine / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1002/humu.1380110169 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9452090 ● Summary page in Scopus @ Elsevier: 2-s2.0-0031975248 (DOI: 10.1002/humu.1380110169, PubMed: 9452090, Elsevier: Scopus)
103.	Michie Shimmoto, Ryoichi Kase, Kouji Itou, Kouichi Utsumi, Satoshi Ishii, Choji Taya, Hiromichi Yonekawa and Hitoshi Sakuraba : Generation and characterization of transgenic mouse expressing a human mutant α-galactosidase with an R301Q substitution causing a variant form of Fabry disease., FEBS Letters, Vol.417, No.1, 89-91, 1997.
104.	Kouji Itou, Norio Miharu, Koso Ohama, Nobuyuki Mizoguchi, Nobuo Sakura and Hitoshi Sakuraba : Fetal diagnosis of galactosialidosis (protective protein/cathepsin A deficiency)., Clinica Chimica Acta, Vol.266, No.2, 75-82, 1997. (要約) The fetal diagnosis of galactosialidosis is performed by measuring carboxypeptidase (cathepsin A) activity in cultured villous cells and by immunofluorescence analysis with an antibody against an oligopeptide corresponding to the N-terminal domain of the human mature protective protein. Neither carboxypeptidase activity nor immunofluorescence was detected in cultured villous cells derived from an at-risk fetus or in cultured fibroblasts derived from the sister with galactosialidosis. Neuraminidase and beta-galactosidase activities were also confirmed to be deficient or low. A direct assay system for protective protein/cathepsin A is useful for the accurate prenatal diagnosis of galactosialidosis. (キーワード) Antibodies / Carboxypeptidases / Cathepsin A / Cells, Cultured / Chorionic Villi / Chorionic Villi Sampling / Female / Fluorescent Antibody Technique / Galactosides / Gangliosidoses / Humans / Lysosomal Storage Diseases / Pregnancy / Prenatal Diagnosis (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0009-8981(97)00141-1 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9437536 ● Search Scopus @ Elsevier (PMID): 9437536 ● Search Scopus @ Elsevier (DOI): 10.1016/S0009-8981(97)00141-1 (DOI: 10.1016/S0009-8981(97)00141-1, PubMed: 9437536)
105.	Hitoshi Sakuraba, Kouji Itou, Yoko Kuroki, Ryoichi Kase, Michie Shimmoto, Kouichi Utsumi, Hideki Ozawa, Tadashi Tai, Akio Hara and Eiichiro Uyama : Immunocytochemical detection of accumulated substrates in cultured fibroblasts from patients with the infantile and adult forms of Sandhoff disease., Clinica Chimica Acta, Vol.265, No.2, 263-266, 1997. (キーワード) Adult / Aging / Antibodies, Monoclonal / Cells, Cultured / Fibroblasts / G(M2) Ganglioside / Glycoproteins / Humans / Immunohistochemistry / Infant / Oligosaccharides / Sandhoff Disease / beta-N-Acetylhexosaminidases (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0009-8981(97)00143-5 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9385467 ● Search Scopus @ Elsevier (PMID): 9385467 ● Search Scopus @ Elsevier (DOI): 10.1016/S0009-8981(97)00143-5 (DOI: 10.1016/S0009-8981(97)00143-5, PubMed: 9385467)
106.	Hideki Ozawa, Katsuko Yamashita, Hitoshi Sakuraba, Kouji Itou, Ryoichi Kase and Tadashi Tai : Generation and characterization of mouse monoclonal antibodies specific for N-linked neutral oligosaccharides of glycoproteins., Archives of Biochemistry and Biophysics, Vol.342, No.1, 48-57, 1997.
107.	Tomoyo Takata, Toshika Okumiya, Hidemasa Hayashibe, Michie Shimmoto, Ryoichi Kase, Kouji Itou, Koichi Utsumi, Sachiko Karnei and Hitoshi Sakuraba : Screening and detection of gene mutations in Japanese patients with Fabry disease by single-stranded conformation polymorphism analysis., Brain & Development, Vol.19, No.2, 111-116, 1997. (要約) We have applied non-radioactive polymerase chain reaction (PCR)-single-stranded conformation polymorphism (SSCP) to the detection of gene mutations causing Fabry disease. Nineteen of 22 known mutations were detected as electrophoretic mobility shifts on PCR-SSCP analysis. Then, DNA from newly diagnosed Japanese patients with the classical form of Fabry disease was subjected to PCR-SSCP analysis, and 4 novel mutations (1 small deletion, 1 nonsense mutation and 2 missense mutations) and 1 neutral polymorphism were identified. Furthermore, identification of an asymptomatic heterozygote and a hemizygote with moderate clinical manifestations was successfully achieved by application of this method to a family with the variant form of Fabry disease. PCR-SSCP is useful for the gene diagnosis of etiologically heterogeneous Fabry disease. (キーワード) Adolescent / Adult / Fabry Disease / Female / Genetic Testing / Heterozygote / Humans / Japan / Male / Middle Aged / Mutation / Pedigree / Polymerase Chain Reaction / Polymorphism, Single-Stranded Conformational / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0387-7604(96)00486-X (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9105656 ● Search Scopus @ Elsevier (PMID): 9105656 ● Search Scopus @ Elsevier (DOI): 10.1016/S0387-7604(96)00486-X (DOI: 10.1016/S0387-7604(96)00486-X, PubMed: 9105656)
108.	Nobuaki Takiyama, Kouji Itou, Michie Shimmoto, Junji Nishimoto, Koji Inui, Hitoshi Sakuraba and Yoshiyuki Suzuki : Molecular form and subcellular distribution of acid β-galactosidase in fibroblasts from patients with Morquio B disease and galactosialidosis., Brain & Development, Vol.19, No.2, 126-130, 1997. (要約) The molecular form and subcellular distribution of acid beta-galactosidase in cultured fibroblasts from patients with beta-galactosidase deficiency (GM1-gangliosidosis, Morquio B disease and galactosialidosis) were studied, using antibodies against three different forms of the human enzyme: a high-molecular-weight multienzymic complex, a recombinant 84-kDa precursor, and a 64-kDa tryptic product of the precursor. The mature enzyme from normal fibroblasts was immunoprecipitated by the anti-complex and anti-64-kDa protein antibodies, but not by the anti-84-kDa precursor one. immunofluorescence staining of normal fibroblasts revealed the granular (lysosomal) distribution with anti-64-kDa protein antibody and the perinuclear reticular distribution with anti-84-kDa precursor antibody, probably representing the Golgi apparatus. Both patterns were demonstrated in Morquio B disease, but the residual enzyme activity was exclusively due to the mature enzyme. In Type 1 galactosialidosis, most of the expressed enzyme was detected as the precursor form with a perinuclear reticular distribution. In type 2 galactosialidosis, more than half of the enzyme activity was due to the mature form with a lysosomal distribution. Fibroblasts from a patient with GM1 gangliosidosis, expressing no beta-galactosidase mRNA, did not react against either anti-64-kDa protein antibody or anti-84-kDa precursor antibody. The combined use of immunoprecipitation and immunostaining was useful for analysing the pathophysiology of the intracellular processing and transport of the mutant beta-galactosidase. (キーワード) Antibody Specificity / Cells, Cultured / Fibroblasts / Fluorescent Antibody Technique, Direct / Galactosides / Gangliosidosis, GM1 / Humans / Infant / Metabolism, Inborn Errors / Mucopolysaccharidosis IV / Multienzyme Complexes / Phenotype / RNA, Messenger / Recombinant Proteins / Subcellular Fractions / beta-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/S0387-7604(96)00494-9 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9105659 ● Search Scopus @ Elsevier (PMID): 9105659 ● Search Scopus @ Elsevier (DOI): 10.1016/S0387-7604(96)00494-9 (DOI: 10.1016/S0387-7604(96)00494-9, PubMed: 9105659)
109.	O. Kawamura, H. Sakuraba, Kouji Itou, Y. Suzuki, M. Doi, H. Kuwabara, S. Oshima, S. Abe, H. Warabi and N. Yoshizawa : Subclinical Fabry's disease occuring in the context of IgA nephropathy., Clinical Nephrology, Vol.47, No.2, 71-75, 1997. (要約) A 28-year-old male patient with both IgA nephropathy and an unusual case of Fabry's disease has been followed for 10 years. Diagnosis of both these diseases was made by histological examination of renal biopsy tissues and the enzyme activities of alpha-galactosidase A. Serial biopsies revealed the hithertofore unrecognized process of glomerular glycolipid accumulation peculiar to Fabry's disease at the initial stages of the disease. Physical examinations and routine laboratory analyses failed to show significant signs of Fabry's disease throughout the 10-year period. While alpha-galactosidase A activity is markedly decreased in the plasma of this patient as in classical Fabry hemizygotes, the activity in leukocytes and culture fibroblasts showed a considerable residual activity. Fabry's disease associated with IgA nephropathy apparently is extremely rare, and the present subclinical case is unique in that the early stages of substrate accumulation are demonstrable. (キーワード) Adult / Antigens, CD / Biopsy / Fabry Disease / Glomerulonephritis, IGA / Humans / Kidney Glomerulus / Male / Microscopy, Electron / Trihexosylceramides / alpha-Galactosidase (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9049452 ● Search Scopus @ Elsevier (PMID): 9049452 (PubMed: 9049452)
110.	Ryoichi Kase, Uwe Bierfreund, Andreas Klein, Thomas Kolter, Kouji Itou, Suzuki Minoru, Yasuhiro Hashimoto, Konrad Sandhoff and Hitoshi Sakuraba : Only sphingolipid activator protein B (SAP-B or saposin B) stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α-galactosidase in a detergent-free liposomal system., FEBS Letters, Vol.393, No.1, 74-76, 1996.
111.	Reiko Minamikawa-Tachino, Yuji Maeda, Issei Fujishiro, Kouji Itou, Akira Satake, Shigeki Aoki, Hideo Yamada, Yoshiyuki Suzuki and Hitoshi Sakuraba : Three-dimensional brain visualization for metachromatic leukodystrophy., Brain & Development, Vol.18, No.5, 394-399, 1996. (要約) The basic understanding of many neurogenetic diseases requires study of the clinical, biochemical, and pathological aspects. To study the pathological aspects, the organs affected by the disease must be observed. We have used volume visualization techniques to create three-dimensional (3D) brain images of a patient with late infantile metachromatic leukodystrophy (MLD). The 3D brain images showed clearly, stereographically, and non-invasively the intracerebral lesion. This lesion, which indicated hyperintensity in magnetic resonance (MR) images, extended throughout the periventricular white matter. The 3D brain images are provided to integrate information. Volumetric ray-casting was useful in obtaining directly images of the entire brain and in allowing an intuitive understanding of the extension of the lesion in three dimensions and of the extent of the defects in the MLD brain. Isosurfacing facilitated a clear extraction of the lesion located by volumetric ray-casting. Each technique used in this study played a role in visualization and their use was complementary. 3D brain images will promote morphological investigation of neurogenetic diseases. (キーワード) Brain / Child, Preschool / Humans / Image Processing, Computer-Assisted / Leukodystrophy, Metachromatic / Magnetic Resonance Imaging / Male (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0387-7604(96)00040-X (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8891235 ● Search Scopus @ Elsevier (PMID): 8891235 ● Search Scopus @ Elsevier (DOI): 10.1016/0387-7604(96)00040-X (DOI: 10.1016/0387-7604(96)00040-X, PubMed: 8891235)
112.	Kouji Itou, T. Takenaka, S. Nakao, M. Setoguchi, H. Tanaka, T. Suzuki and H. Sakuraba : Immunofluorescence analysis of globotriaosylceramide accumulated in the hearts of variant hemizygotes and heterozygotes with Fabry disease., The American Journal of Cardiology, Vol.78, No.1, 116-117, 1996.
113.	Michie Shimmoto, Yutaka Nakahori, Ikumi Matsushita, Toshikatsu Shinka, Yoko Kuroki, Kouji Itou and Hitoshi Sakuraba : A human protective protein gene partially overlaps the gene encoding phopholipid transfer protein on the complementary strand of DNA, Biochemical and Biophysical Research Communications, Vol.220, No.3, 802-806, 1996.
114.	M Fukushima, Y Tsuchiyama, T Nakato, T Yokoi, H Ikeda, S Yoshida, T Kusumoto, Kouji Itou and H Sakuraba : A female heterozygous patient of Fabry's disease with renal accumulation of trihexosylceramide detected with a monoclonal antibody., American Journal of Kidney Diseases, Vol.26, No.6, 952-955, 1995. (要約) We describe a female patient with heterozygous Fabry's disease. The patient had persistent proteinuria and microhematuria but lacked any other diagnostic signs such as corneal and cutaneous involvement. Kidney tissue obtained at biopsy showed the segmentally distributed enlarged glomerular epithelia. These cells were filled with vacuolated foamy cytoplasm, which had lamellar and myelinoid structures under electronmicroscopic observation. Accumulation of trihexosylceramide (CTH) in these foamy epithelial cells was confirmed with immunohistochemical staining with the use of anti-CTH monoclonal antibody. Alpha-galactosidase activity of leukocytes was 67 nmol/mg protein/hr, which was approximately half that of the normal population (mean +/- SD, 147 +/- 65 nmol/mg protein/hr, n = 20). All of these findings were compatible with the diagnosis of heterozygous Fabry's disease. We recommend that kidney tissue biopsy specimens suggesting Fabry's disease be immunostained with anti-CTH antibody. (キーワード) Antibodies, Monoclonal / Biopsy / Fabry Disease / 女性 (female) / Heterozygote / Humans / 免疫組織化学 (immunohistochemistry) / Kidney / Leukocytes / Middle Aged / Trihexosylceramides / alpha-Galactosidase (出版サイトへのリンク) ● Publication site (DOI): 10.1016/0272-6386(95)90061-6 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 7503071 ● Summary page in Scopus @ Elsevier: 2-s2.0-0028866658 (DOI: 10.1016/0272-6386(95)90061-6, PubMed: 7503071, Elsevier: Scopus)
115.	Yoko Kuroki, Kouji Itou, Yoko Nadaoka, Tsukasa Tanaka and Hitoshi Sakuraba : A novel missense mutation (C522Y) is present in the β-hexosaminidase β-subunit gene of a Japanese patient with infantile Sandhoff disease., Biochemical and Biophysical Research Communications, Vol.212, No.2, 564-571, 1995.
116.	Kouji Itou, Ryoichi Kase, Michie Shimmoto, Akira Satake, Hitoshi Sakuraba and Yoshiyuki Suzuki : Protective protein as an endogenous endothelin degradation enzyme in human tissues., The Journal of Biological Chemistry, Vol.270, No.2, 515-518, 1995.
117.	A. Satake, Kouji Itou, M. Shimmoto, C. T. Saido, H. Sakuraba and Y. Suzuki : Distribution of lysosomal protective protein in human tissues., Biochemical and Biophysical Research Communications, Vol.205, No.1, 38-43, 1994.
118.	Akihiko Tsuji, Ryoichi Oda, Kohji Sakiyama, Hideaki Nagamune, Kouji Itou, Ryoichi Kase, Hitoshi Sakuraba, Yoshiyuki Suzuki and Yoshiko Matsuda : Lysosomal enzyme replacement using α2-macroglobulin as a transport vehicle, The Journal of Biochemistry, Vol.115, No.5, 937-944, 1994. (要約) α2-マクログロブリン(α2M)を運搬担体に用いたリソソーム酵素欠損性遺伝病の酵素補充療法システムを開発した． α2Mはレセプターを介してリソソームに取り込まれることから，豚肝臓から精製した α-グルコシダーゼ或いはα-ガラクトシダーゼにα2Mを運搬担体として二価架橋試薬で連結し，リソソーム指向性の酵素補充療法剤を構築した．これを用いてin vitro実験を行い，ポンペ病及びファブリー病細胞の細胞病態が改善されることを証明した．
119.	Masaharu Kotani, Hiroshi Hosoya, Kouji Itou, Hitoshi Sakuraba, Masashi Kusubata, Masaki Inagaki, Kazumori Yazaki, Yoshiyuki Suzuki and Tadashi Tai : Evidence for direct binding of intracellularly distributed ganglioside GM2 to isolated vimentin intermediate filaments in normal and Tay-Sachs disease human fibroblasts., Cell Structure and Function, Vol.19, No.2, 81-87, 1994.
120.	Akihiro Oshima, Kunihiro Yoshida, Kouji Itou, Ryoichi Kase, Hitoshi Sakuraba and Yoshiyuki Suzuki : Intracellular processing and maturation of mutant gene products in hereditary β-galactosidase deficiency (β-galactosidosis)., Human Genetics, Vol.93, No.2, 109-114, 1994.
121.	Kouji Itou, M. Kotani, T. Tai, H. Suzuki, T. Utsunomiya, M. Inoue, H. Yamada, H. Sakuraba and Y. Suzuki : Immunofluorescence imaging diagnosis of Fabry heterozygotes using a confocal laser scanning microscopy., Clinical genetics, Vol.36, 171-177, 1993.
122.	H. Sakuraba, Kouji Itou, M. Kotani, T. Tai, H. Yamada, K. Kurosawa, Y. Kuroki, H. Suzuki, T. Utsunomiya, H. Inoue and Y. Suzuki : Prenatal diagnosis of GM2-gangliosidosis: immunofluorescence analysis of ganglioside GM2 in cultured amniocytes by confocal laser scanning microscopy., Brain & development., Vol.15, No.4, 278-282, 1993.
123.	N. Takiyama, Kouji Itou, A. Oshima, H. Sakuraba and Y. Suzuki : Characterization of an anti-β-galactosidase antibody recognizing a precursor but not a mature enzyme in solution., Biochemical and Biophysical Research Communications, Vol.193, No.2, 1993.
124.	Michie Shimmoto, Yukiko Fukuhara, Kouji Itou, Akihiro Oshima, Hitoshi Sakuraba and Yoshiyuki Suzuki : Protective protein gene mutations in galactosialidosis., The Journal of Clinical Investigation, Vol.91, 2393-2398, 1993.
125.	Kouji Itou, Nobuaki Takiyama, Ryoichi Kase, Keiji Kondoh, Akira Sano, Akihiro Oshima, Hitoshi Sakuraba and Yoshiyuki Suzuki : Purification and characterization of human lysosomal protective protein expressed in stably transformed Chinese hamster ovary cells., The Journal of Biological Chemistry, Vol.268, 1180-1186, 1993.

学術論文(紀要・その他):

1.	Chiaki Komiya, Jun Tsukimoto, Masahiro Ueda, Takuya Morisaki, Tsubasa Inokuma, Akira Shigenaga, Kouji Itou and Akira Otaka : Preparation of protein thioesters enabled by carboxypeptidase-mediated C-terminal specific hydrazinolysis, Peptide Science 2018, 8, 2019.
2.	Takuya Morisaki, Masaya Denda, Jun Yamamoto, Daisuke Tsuji, Tsubasa Inokuma, Kouji Itou, Akira Shigenaga and Akira Otaka : Development of N-sulfanyltehylanilide (SEAlide)-based traceable linker for enrichment and selective labeling of target proteins, Peptide Science 2016, 179-181, 2017.
3.	Takahiro Nakamura, Akira Shigenaga, Naoto Naruse, Tsubasa Inokuma, Kouji Itou and Akira Otaka : Second-generation synthetic strategy of GM2-activator protein (GM2AP) analogues applicable to the preparation of a protein library, EPS Proceedings 2016, 63, 2016.
4.	Ken Sakamoto, Kohei Sato, Akira Shigenaga, Daisuke Tsuji, Kouji Itou and Akira Otaka : N-Sulfanylethyl anilide linkers as peptide thioester equivalent, Peptides Across The Pacific, Proceedings of the Twenty-Third American and Sixth International Peptide Symposium, 242-243, 2013.
5.	Kohei Sato, Keisuke Kitakaze, Ken Sakamoto, Akira Shigenaga, Daisuke Tsuji, Kouji Itou and Akira Otaka : Convergent chemical synthesis of human GM2 activator protein analog using SEAlide chemistry, Peptide Science 2012, Vol.2012, 13-14, 2013. (キーワード) GM2 activator protein / protein chemical synthesis / SEAlide peptide (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1571135651156844416 (CiNii: 1571135651156844416)
6.	Akira Shigenaga, Daisuke Tsuji, Naomi Nishioka, Shugo Tsuda, Kouji Itou and Akira Otaka : Development of stimulus-responsive amino acid with peptide bond-cleavage ability and its application to a nucleocytoplasmic shuttle peptide, Peptide Science 2007, Vol.2007, 97-98, 2008. (キーワード) nuclear export signal (NES) / nuclear localization signal (NLS) / stimulus responsive / trimethyl lock / UV irradiation (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1573950400368902528 (CiNii: 1573950400368902528)

総説・解説:

1.	月本準, 伊藤孝司 : 細胞内結晶化能を持つノイラミニダーゼ1と欠損症の治療法開発, 生化学, Vol.95, No.6, 784-791, 2023年12月.
2.	Jun Tsukimoto and Kouji Itou : Human neuraminidase 1 and related diseases, Trends in Glycoscience and Glycotechnology, Vol.35, No.206, E53-E55, Jul. 2023.
3.	伊藤孝司, 西岡宗一郎, 篠田知果, 竹内美絵, 佐々井優弥, 水野輝, 桐山慧, 月本準 : 遺伝子組換えカイコによるグライコバイオロジクスの開発, Applied Cell Biology Japan, Vol.35, 1-18, 2022年12月. (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1520576282617359488 (CiNii: 1520576282617359488)
4.	月本準, 伊藤孝司 : ライソゾーム病と創薬, 生体の科学, Vol.73, No.3, 241-245, 2022年6月. (キーワード) ライソゾーム病 / 酵素補充療法 / 小胞輸送 / マンノース-6-リン酸 / 遺伝子治療 / 血液脳関門 / ライソゾームビョウ / コウソホジュウリョウホウ / ショウホウユソウ / マンノース-6-リンサン / イデンシチリョウ / ケツエキノウカンモン (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1520855533695843584 (CiNii: 1520855533695843584)
5.	伊藤孝司, 西岡宗一郎, 日高朋, 月本準, 桐山慧, 篠田知果, 竹内美絵, 麻植真結子, 辻大輔 : 遺伝子組換えカイコによるヒトバイオ医薬品開発の現状と課題, 蚕糸・昆虫バイオテック, Vol.88, No.3, 167-174, 2019年12月. (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1391131406306660608 (CiNii: 1391131406306660608)
6.	石井明子, 多田稔, 立松謙一郎, 冨田正浩, 市原隆光, 山口秀人, 田中貴, 田中剛, 原園景, 木吉真人, 柴田寛子, 遊佐敬介, 佐藤陽治, 武田茂樹, 伊藤孝司, 川崎ナナ, 瀬筒秀樹 : トランスジェニックカイコを用いて製造されるバイオ医薬品の品質管理戦略構築に関する考え方, 医薬品医療機器レギュラトリーサイエンス, Vol.50, No.10, 615-627, 2019年10月. (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1523106605635958912 (CiNii: 1523106605635958912)
7.	伊藤孝司 : GM2ガングリオシドーシスの遺伝子治療, 医学と薬学, Vol.76, No.8, 1133-1144, 2019年7月.
8.	伊藤孝司, 西岡宗一郎, 日高朋, 辻大輔, 真板宣夫 : 組換えカイコ繭由来ライソゾーム病治療薬の開発, 薬学雑誌, Vol.138, No.7, 855-893, 2018年7月. (要約) Lysosomal storage diseases (LSDs) are inborn errors caused by genetic defects of lysosomal enzymes associated with the excessive accumulation of natural substrates and neurovisceral manifestations. Until now, enzyme replacement therapy (ERT) with human lysosomal enzymes produced by genetically engineered mammalian cell lines has been applied clinically to treat several LSDs. ERT is based on the incorporation of <i>N</i>-glycosylated lysosomal enzymes through binding to glycan receptors on the surface of target cells and delivery to lysosomes. However, ERT has several disadvantages, including difficulty in mass producing human enzymes, dangers of pathogen contamination, and high cost. Recently, we have succeeded in producing transgenic silkworms which overexpress human lysosomal enzymes in silk glands, and have purified active and functional enzymes from middle silk glands and cocoons. Silk gland- and cocoon-derived human enzymes carrying high-mannose and pauci-mannose <i>N</i>-glycans are endocytosed by monocytes <i>via</i> the mannose receptor pathway; these were then delivered to lysosomes. Human cathepsin A (Ctsa) precursor proteins purified from the cocoons have been found to suppress microglial activation in the brains of <i>Ctsa</i>-deficient mice; this deficiency is caused by a splicing defect, and serves as a galactosialidosis model associated with the combination of a deficiency of lysosomal neuraminidase 1 (NEU1) and the accumulation of sialyloligosaccharides. Transgenic silkworms overexpressing human lysosomal enzymes in silk glands could serve as a future bioresource to provide safe therapeutic enzymes for the treatment of LSDs. The combination of recent developments in transglycosylation technology with microbial endoglycosidases will aid in the development of therapeutic glycoproteins as bio-medicines.<br> (キーワード) lysosomal disease / transgenic silkworm / enzyme replacement therapy / transglycosylation (出版サイトへのリンク) ● Publication site (DOI): 10.1248/yakushi.17-00202-3 (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1390282763041729280 ● Search Scopus @ Elsevier (DOI): 10.1248/yakushi.17-00202-3 (DOI: 10.1248/yakushi.17-00202-3, CiNii: 1390282763041729280)
9.	関水和久, 伊藤孝司 : カイコ創薬プラットフォーム構築から新蚕業革命へ, 薬学雑誌, Vol.138, No.7, 861-862, 2018年7月. (出版サイトへのリンク) ● Publication site (DOI): 10.1248/yakushi.17-00202-F (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1390564238018440192 ● Search Scopus @ Elsevier (DOI): 10.1248/yakushi.17-00202-F (DOI: 10.1248/yakushi.17-00202-F, CiNii: 1390564238018440192)
10.	伊藤孝司 : 先天性糖鎖異常リソソーム病, 未来を創るグライコサイエンスー我が国のロードマップー, 119-120, 2018年5月.
11.	辻大輔, 伊藤孝司 : リソソームの生理機能制御とリソソーム病における異常, 生化学, Vol.90, No.1, 60-68, 2018年2月. (出版サイトへのリンク) ● Publication site (DOI): 10.14952/SEIKAGAKU.2018.900060 (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1520290883053254784 ● Summary page in Scopus @ Elsevier: 2-s2.0-85051702210 (DOI: 10.14952/SEIKAGAKU.2018.900060, CiNii: 1520290883053254784, Elsevier: Scopus)
12.	伊藤孝司 : 遺組換えカイコによるバイオ医薬品開発, アグリバイオ, Vol.1, No.6, 13-17, 2017年6月.
13.	津田雄介, 重永章, 佐藤浩平, 中村太寛, 北風圭介, 猪熊翼, 伊藤孝司, 大髙章 : 天然アミノ酸配列に適用可能な新規タンパク質チオエステル合成法の開発, ケミカルバイオロジー, Vol.9, 7-10, 2016年6月.
14.	Kouji Itou, Kobayashi Isao, Nishioka So-ichiro, Sezutsu Hideki, Machii Hiroaki and Tamura Toshiki : Recent progress in development of transgenic silkworms overexpressing recombinant human proteins with therapeutic potential in silk glands, Drug Discoveries & Therapeutics, Vol.10, No.1, 34-39, Feb. 2016. (出版サイトへのリンク) ● Publication site (DOI): 10.5582/ddt.2016.01024 (文献検索サイトへのリンク) ● Search Scopus @ Elsevier (DOI): 10.5582/ddt.2016.01024 (DOI: 10.5582/ddt.2016.01024)
15.	重永章, 辻大輔, 西岡直美, 津田修吾, 伊藤孝司, 大髙章 : 刺激応答型アミノ酸を利用した核-細胞質シャトルペプチドの開発, ケミカルバイオロジー, Vol.1, No.1, 7-10, 2008年5月.
16.	辻大輔, 伊藤孝司 : リソソーム病の分子病理と治療ターゲット, 生化学, Vol.79, No.7, 678-682, 2007年7月. (キーワード) 1-Deoxynojirimycin / Animals / Anti-Inflammatory Agents, Non-Steroidal / Aspirin / Bone Marrow Transplantation / Disease Models, Animal / G(M2) Activator Protein / Genetic Therapy / Humans / Lysosomal Storage Diseases, Nervous System / Mutation / beta-N-Acetylhexosaminidases (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17763701 ● CiNii @ 国立情報学研究所 (CRID): 1520009409042629632 ● Search Scopus @ Elsevier (PMID): 17763701 (PubMed: 17763701, CiNii: 1520009409042629632)
17.	Kouji Itou : Neurochemical aspects of Sandhoff disease, Neurochemistry of Metabolic Diseases-Lysosomal storage diseases, phenylketonuria and Canavan disease, 55-82, 2007.
18.	伊藤孝司 : 細胞の構造とオルガネラ「リソソーム蓄積症」, 生物薬科学実験講座, 2007年.
19.	伊藤孝司, 辻大輔, 櫻庭均 : Sandhoff病モデルマウスから樹立されたオリゴデンドロサイトおよびシュワン細胞株における蓄積複合糖質の解析, 生体の科学, Vol.57, No.3, 224-228, 2006年6月.
20.	伊藤孝司 : リソソーム病の酵素補充療法に関する最近の進歩, 未来を拓く糖鎖科学, 271-272, 2005年11月.
21.	桜庭均, 伊藤孝司 : リソソーム性ノイラミニダーゼ(ノイラミニダーゼ-1), 日本臨床増刊号「生化学的検査 I」, Vol.62, 517-520, 2004年.
22.	伊藤孝司 : 保護タンパク質/カテプシンAおよびリソソーム性シアリダーゼと遺伝性代謝異常症, 生化学, Vol.72, 1160-1164, 2000年.
23.	伊藤孝司, 新本美智枝, 桜庭均 : ガラクトシアリドーシス, 別冊日本臨床「先天代謝異常症候群」ー遺伝子解析の進歩と成果ー, Vol.19, 407-410, 1996年.
24.	伊藤孝司, 新本美智枝, 桜庭均 : ガラクトシアリドーシスの遺伝子解析と分子病理, 病理と臨床「病理診断と分子生物学・遺伝学」, Vol.14, 34-37, 1996年.
25.	桜場均, 石井達, 加瀬良一, 伊藤孝司, 奥宮敏可, 辻明彦, 佐藤能雅 : 遺伝性代謝病:病因解明と治療法開発への分子遺伝学的アプローチ, 小児科診療, Vol.59, No.5, 821-828, 1996年. (要約) Fabry病を例にとり，遺伝子上の変異の多様性と発現蛋白の性状について，さらに昆虫細胞におけるα-ガラクトシダーゼの大量発現，構造解析，酵素補充療法への応用について最新の知見について解説した．
26.	伊藤孝司 : レーザースキャン共焦点画像解析システムによる糖脂質の分析, 日本臨牀, Vol.53, No.12, 3095-3101, 1995年.
27.	伊藤孝司, 桜庭均 : 保護タンパク質-ライソゾーム酵素の保護作用を示す多機能性糖タンパク質, 生体の科学, Vol.46, No.3, 230-234, 1995年.
28.	桜庭均, 石井達, 加瀬良一, 伊藤孝司, 奥宮敏可, 竹中俊宏 : ファブリー病の分子遺伝学, 神経内科, Vol.41, No.55, 437-445, 1994年.
29.	桜庭均, 伊藤孝司 : ガラクトシアリドーシスと保護蛋白質, Molecular Medicine, Vol.30, 643-644, 1993年.
30.	桜庭均, 伊藤孝司, 新本美智枝 : 多機能性保護タンパク質とその遺伝性欠損症'ガラクトシアリドーシス', 生化学, Vol.65, 561-566, 1993年.
31.	伊藤孝司, 桜庭均 : リソソームにおける複合糖質の分解と疾患, 蛋白質核酸酵素, Vol.37, 1951-1956, 1992年.

国際会議:

1.	Jun Tsukimoto, Miyoshi Mizuki, Fukuike Rin, Takeuchi Yoshie, Horii Yuto, Iniwa Toshiki, Nishioka So-ichiro and Kouji Itou : Inhibition of in cellulo crystallization of human neuraminidase 1 and application for gene therapy of lysosomal storage disease, Sialoglyco 2022, Sep. 2022.
2.	Kouji Itou : Molecular pathogenesis and therapy for galactosialidosis by utilizing the novel disease model mice, Wakayama Medical University International Symposium on Japan-France Glycopathophysiology 2022, Feb. 2022.
3.	Yuki Yoshino, Naonobu Tanaka, Kanji Niwa, Daisuke Tsuji, Kouji Itou and Yoshiki Kashiwada : Phytochemical study on the roots of Ferula communis (5), The 11th JSP CSP KSP Joint Symposium on Pharmacognosy, 65, Tokyo, Sep. 2021.
4.	SHIMOMOTO Yusei, Naonobu Tanaka, Kanji Niwa, Daisuke Tsuji, Kouji Itou and Yoshiki Kashiwada : Studies on the constituents of Hypericum plants (53): Structures and biological activities on dibenzo-1,4-dioxane derivatives isolated from the roots of Hypericum ascyron, The 11th JSP CSP KSP Joint Symposium on Pharmacognosy, 64, Tokyo, Sep. 2021.
5.	Sakura Takahashi, Naonobu Tanaka, Seita Kajihara, Kanji Niwa, Daisuke Tsuji, Kouji Itou and Yoshiki Kashiwada : Studies on Uzbek medicinal plants (39): New norditerpenes from Perovskia scrophulariifolia, The 11th JSP CSP KSP Joint Symposium on Pharmacognosy, 63, Tokyo, Sep. 2021.
6.	Kouji Itou, Jun Tsukimoto, Daisuke Tsuji, Yuto Horii, Toshiki Iniwa, Yuri Fukushi and Haruna Andoh : Innovative gene therapy for lysosomal neuraminidase 1 (NEU1) deficiencies, WorldSymposium2020, Orlando, Feb. 2020.
7.	Kouji Itou, Yukiya Ohnishi, Daisuke Tsuji, Watanabe Ryosuke, Kamori Nijiho, Asai Katsuhito and Muramatsu Shinichi : In vivo gene therapy for GM2 gangliosidoses with novel AAV9/3-CMV-modHEXBvector ., CHU St.Justine Conference, Montreal, Feb. 2020.
8.	Kouji Itou, Yukiya Ohnishi, Daisuke Tsuji, Watanabe Ryosuke, Asai Katsuhito and Muramatsu Shinichi : Novel gene therapy for GM2 gangliosidoses with novel AAV9/3-CMV-modHEXB vector, 23rd ESN Biennial Meeting 7th Conference on Molecular Mechanisms of Regulation in the Nervous System, Milano, Sep. 2019.
9.	Kouji Itou, Jun Tsukimoto, Daisuke Tsuji, Yuto Horii, Toshiki Iniwa, Yuri Fukushi, Haruna Andoh, P Simona, L Cabitta, S Grassi, A Prinetti and S Sonnino : Molecular pathogenesis and innovative therapy for lysosomal neuraminidase 1 (neu1)deficiencies(sialidosis and galactosialidoisis), Glyco25, Milano, Aug. 2019.
10.	Jun Tsukimoto, Toshiki Iniwa, Yuto Horii, So-ichirou Nishioka and Kouji Itou : Study on in cellulo crystallization of human neuraminidase 1 and association with cathepsin A., Glyco25, Milano, Aug. 2019.
11.	Hiroki Tanaka, Daisuke Tsuji, Yukiya Ohnishi, Tsuyoshi Matsugu, Hiromi Teramoto, Ryuto Nakae and Kouji Itou : Aberrant autophagy in lysosomal storage disorders is caused by decrease of snare proteind in lysosomes., Glyco25, Milano, Aug. 2019.
12.	Yukiya Ohnishi, Daisuke Tsuji, Nijiho Kamori, Shinichi Muramatsu and Kouji Itou : In vivo gene therapy by ttilizing modified LL-Hexosaminidase B for GM2 gangliosidoses, Glyco25, Milano, Aug. 2019.
13.	Chiaki Komiya, Jun Tsukimoto, Masahiro Ueda, Takuya Morisaki, Tsubasa Inokuma, Akira Shigenaga, Kouji Itou and Akira Otaka : Preparation of protein thioesters enabled by carboxypeptidase-mediated C-terminal specific hydrazinolysis, 10th International Peptide Symposium, Kyoto, Dec. 2018.
14.	Naoshi Yamazaki, Makiko Shinomiya, Hironobu Ike, Yasuo Shinohara, Noriaki Minakawa, Kouji Itou and Yoshiharu Takiguchi : Use of modified U1 small nuclear RNA for improved formation of properly spliced mRNA encoding human cathepsin A from the gene having an IVS7 +3a>g mutation, The 43rd FEBS Congress, Praha, Jul. 2018.
15.	Kouji Itou, Nishioka So-ichiro, Kobayashi Isao, Matsuzaki Yuji, Iino Kenta, Nadanaka Satomi, Kasashima-Sumitani Megumi, Hidaka Tomo, Daisuke Tsuji, Sezutsu Hideki, Kitagawa Hiroshi and Yamamoto Kenji : A novel glycotechnology to produce human lysosomal enzymes carrying synthetic N-glycans with terminal mannose 6-phosphate residues and application to enzyme placement therapy for lysosomal storage diseases, World Symposium 2018, San diego(USA), Feb. 2018.
16.	Tsukimoto Jun and Kouji Itou : Expression and cheracterization of human neuraminidase 4 (NEU4) in culture systems, 1st International Conference on the Glycobiology of Nervous System., Korea Seoul(Korea Univ.), Sep. 2017.
17.	Uno MIchel Shintaro, Daisuke Tsuji, Watanabe Ryosuke, Tanaka Hiroki, Ballabio Andrea and Kouji Itou : Tfeb-mediated neuro-protection in Sandhoff disease model mouse brain, 1st International Conference on the Glycobiology of Nervous System., Korea Seoul(Korea Univ.), Sep. 2017.
18.	Tanaka Hiroki, Daisuke Tsuji, Watanabe Ryosuke, Shintaroh Michael Uno and Kouji Itou : Impairment of autophagosome-lysosome fusion in lysosomal storage didorders, 1st International Conference on the Glycobiology of Nervous System., Korea Seoul(Korea Univ.), Sep. 2017.
19.	Daisuke Tsuji, Watanabe Ryosuke, Tanaka Hiroki, Shintaroh Michael Uno and Kouji Itou : Mecheanism of neuronal cell death in Tay-Sachs disease iPS model, 1st International Conference on the Glycobiology of Nervous System., Korea Seoul(Korea Univ.), Sep. 2017.
20.	Kouji Itou, Yuhki Tanaka, Tomo Hidaka, Yuhto Horii, So-ichiro Nishioka, Daisuke Tsuji, Simona Prioni, Livia Cabitta, Alessandro Prinetti, Sandro Sonnino, Isao Kobayashi, Megumi Sumitani and Hideki Sezutsu : Neuropathogenesis of murine disease model with cmnined defiencies of lysosomal cathepsinA (Ctsa) and neuraminidase-1 (Neu1) and therapeutic approach., 1st International Conference on the Glycobiology of Nervous System., Korea Seoul(Korea Univ.), Sep. 2017.
21.	渡邊綾佑 and Kouji Itou : Lysoglycosphingolipids Induce Neuronal Cell Death via Pl3K/Akt Signaling., 24th International Symposium On Glycoconjugates, ICC Jeju(Jeju Island,Korea), Aug. 2017.
22.	Kouji Itou : "Neo-glycoenzymes" produced by utilizing transglycosylation activity of endoglycosidases and synthetic N-lysosomal storage diseases., 24th International Symposium On Glycoconjugates, ICC Jeju(Jeju Island,Korea), Aug. 2017.
23.	Takuya Morisaki, Masaya Denda, Jun Yamamoto, Daisuke Tsuji, Tsubasa Inokuma, Kouji Itou, Akira Shigenaga and Akira Otaka : Development of N-Sulfanylethylanilide-based Traceable Linker for Purification and Selective Labeling of Target Proteins, American Peptide Symposium 2017, Whistler, BC, Canada, Jun. 2017.
24.	Kouji Itou, Isao Kobayashi, So-ichiro Nishioka, Tomo Hidaka, Daisuke Tsuji and Hideki Sezutsu : A transgenic silkworm overexpressing human lysosomal enzyme as a novel resource for producing recombinant glycobiologicsand its application to development of enzyme replacement therapy for lysosomal storage diseases., 13th Annual WORLD Symposium 2017, San Diego, CA, USA(Manchester Grand Hyatt), Feb. 2017.
25.	Naoshi Yamazaki, Yasuo Shinohara, Kouji Itou, Noriaki Minakawa and Yoshiharu Takiguchi : Rescue of mutation-induced exon 7 skipping in human Cathepsin A by using modified U1 small nuclear RNA, 2016 ASCB Annual Meeting, San Francisco, Dec. 2016.
26.	Takahiro Nakamura, Akira Shigenaga, Naoto Naruse, Tsubasa Inokuma, Kouji Itou and Akira Otaka : Second-Generation Synthetic Strategy of GM2-Activator Protein (GM2AP) Analogues Applicable to the Preparation of a Protein Library, 34th European Peptide Symposium 2016 & 8th International Peptide Symposium, Leipzig, Germany, Sep. 2016.
27.	Yusuke Tsuda, Akira Shigenaga, Kohei Tsuji, Masaya Denda, Kohei Sato, Keisuke Kitakaze, Takahiro Nakamura, Tsubasa Inokuma, Kouji Itou and Akira Otaka : Development of Chemistry-based Protocol for Sequence-dependent Thioesterification, American Peptide Symposium 2015, Florida, Jun. 2015.
28.	Daisuke Tsuji, Spampanato Carmine, Sambri Irene, Fraldi Alessandro, Kouji Itou and Ballabio Andrea : Analysis of endogenous TFEB expression and distribution in LSD model mice, Gordon Research Conference, USA,Texas,Galveston(Hotel Galvez), Mar. 2015.
29.	Keiko Miyoshi, Taigo Horiguchi, Ayako Tanimura, Hiroko Hagita, Yoshihiro Touda, Shoji Kagami, Kenji Mori, Daisuke Tsuji, Kouji Itou and Takafumi Noma : Gaucher disease caused by possible atypical mechanism, Gordon Research Conference, USA,Texas,Galveston(Hotel Galvez), Mar. 2015.
30.	Kitakaze Keisuke, Tasaki Chikako, Mizutani Yasumichi, Sugiyama Eiji, Mariko Ikuo, kamiya Mako, Setou Mitsutoshi, Urano Yasuteru and Kouji Itou : Development of protease-resisitant modified human beta-hexosaminidase B and evaluation of intracerebroventricular replacement effects on GM2 gangliosidosis model mice., The 11th Annual World Symposium 2015, Orland,Florida,USA, Feb. 2015.
31.	Kohei Sato, Keisuke Kitakaze, Ken Sakamoto, Akira Shigenaga, Daisuke Tsuji, Kouji Itou and Akira Otaka : Synthetic study of GM2 activator protein using N-sulfanylethylanilide peptide, The 33rd European Peptide Symposium, Sofia, Aug. 2014.
32.	Kouji Itou, Daisuke Tsuji, Mariko Ikuo, Kitakaze Keisuke, Asanuma Daisuke, Kamiya Mako, Urano Yasuteru, Sugiyama Eiji, Setou Mitsutoshi, Yuzaki Michisuke and Sakuraba Hitoshi : Molecular therapy and evaluation for neurodegenerative GM2 gangliosidoses, New Frontier of Molecular Neuropathology 2014, Tokyo, Mar. 2014.
33.	Kitakaze Keisuke, Asanuma Daisuke, Asanuma Daisuke, Kamiya Mako, Daisuke Tsuji, Mariko Ikuo, Urano Yasuteru, Sakuraba Hitoshi and Kouji Itou : Replacement Effects of Human Modified Lysosomal β-Hexosaminidase B on Tay-Sachs and Sandhoff Disease Models and Imaging with Novel pH-activatable Fluorescent Probes imaging of endocytosed lysosomal enzymes with pH-activatable fluorescent probe and evaluation of enzyme replacement effects on lysosomal storage diseases., The 10th Annual World Symposium 2014, SanDiego, CA, USA, Feb. 2014.
34.	Kouji Itou, Daisuke Tsuji, Mariko Ikuo, Keisuke Kitakaze, So-ichirou Nishioka, Izumi Imataki, Saeka Yamaguchi, Yasunori Chiba, Hitoshi Sakuraba, Isao Kobayashi, Hideki Sezutsu and Hiroaki Machii : Establishment of patient-derived iPS cells with neurodegenerative lysosomal storage diseases and application for evaluating lysosomal enzyme replacement effects on differentiated neural cells., The IUBMB 10th International Symposium on Cell Surface Macromolecules, India,Kolkata, Jan. 2014.
35.	Kitakaze Keisuke, Mariko Ikuo, Sugiyama Eiji, Asanuma Daisuke, Kamiya Mako, Setou Mitsutoshi, Urano Yasuteru, Sakuraba Hitoshi and Kouji Itou : Imaging of lysosomal enzyme replacement effects with a novel fluorescent probe and imaging mass spectrometry., International Symposium on Glyco-Neuroscience, Hyogo Prefecture, Jan. 2014.
36.	Yusuke Tsuda, Akira Shigenaga, Kohei Sato, Takahiro Nakamura, Keisuke Kitakaze, Kouji Itou and Akira Otaka : Development of chemical protocol for preparation of peptide/protein thioesters applicable to naturally occurring sequences, 17th KPPS Annual Symposium, Seoul, Nov. 2013.
37.	Kouji Itou, Daisuke Tsuji, Kentarou Namba, Saeka Yamaguchi, Keisuke Kitakaze, Izumi Imataki, Naozumi Ishimaru and Hitoshi Sakuraba : Establishment of Human Cell Culture Systems Induced from iPS Cells Derived from Tay-Sachs Disease Patient for Drug Discovery., The 55th Annual Meeting of The Japanese Society for Inherited Metabolic Diseases(JSIMD), Chiba, Nov. 2013.
38.	Ken Sakamoto, Kohei Sato, Akira Shigenaga, Daisuke Tsuji, Kouji Itou and Akira Otaka : Development of efficient synthetic method for N-amino acyl N-sulfanylethyl anilide linkers as peptide thioester equivalent, 23rd American Peptide Symposium, Hawai'i, Jun. 2013.
39.	Kitakaze Keisuke, Daisuke Tsuji, Asanuma Daisuke, Kamiya Mako, Urano Yasuteru, Sakuraba Hitoshi and Kouji Itou : Evaluation of enzyme replacement effect and development of purified system to obtain recombinant lysosomal enzyme with M6P-type glycan., Gordon Research Conference 2013 Lysosomal Diseases, Italy,Lucca(Barga), Apr. 2013.
40.	Kouji Itou, Daisuke Tsuji, So-ichirou Nishioka, Syunsuke Ikedo, Tetuya Higashi, I Kobayashi, H Sezutsu, A Ishii, K. Harazono, M. Tada, Nana Kawasaki and Hiroaki Machii : Molecular properties of recombinant human lysosomal enzyme produced by transgenic silkworm and therapeutic potential for lysosomal storage disease., Gordon Research Conference 2013 Lysosomal Diseases, Italy,Lucca (Barga), Apr. 2013.
41.	T Harada, Shuji Ozaki, A Oda, M Iwasa, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Masahiro Abe, Hirofumi Shibata, Akishige Ikegame, Daisuke Tsuji, Kouji Itou, M Ri, S Iida, Y Shiotsu, S Kawai, H Yamada-Okabe and Toshio Matsumoto : Combination Therapy of a Defucosylated Anti-HM1.24 Monoclonal Antibody Plus Lenalidomide Induces Marked Antibody-Dependent Cellular Cytotoxicity and Inhibits the Clonogenic Potential of Myeloma Cancer Stem-Like Cells., 54th ASH Annual Meeting and Exposition, USA, Atlanta, Dec. 2012.
42.	Kohei Sato, Keisuke Kitakaze, Ken Sakamoto, Akira Shigenaga, Daisuke Tsuji, Kouji Itou and Akira Otaka : Chemical synthesis of human GM2 activator protein analog using SEAlide peptide-mediated one-pot multi-fragment condensation, The 6th Takeda Science Foundation Symposium on PharmaSciences, Suita, Sep. 2012.
43.	Kouji Itou, Nishioka So-ichiro, Daisuke Tsuji, Nobuo Maita, Kobayashi Isao, Sezutsu Hideki, Harazono Kei, Ishii Akiko, Kawasaki Nana and Machii Hiroaki : Transgenic silkworm as a novel therapeutic glycoenzyme resource for lysosomal storage diseases, 21st International Symposium on Glycoconjugates, Madrid, Spain, Jul. 2012.
44.	Kouji Itou, Nishioka So-ichiro, Daisuke Tsuji, Nobuo Maita, Kobayashi Isao, Sezutsu Hideki, Harazono Kei, Ishii Akiko, Kawasaki Nana and Machii Hiroaki : Vital imaging of endocytosed lysosomal enzymes with pH-activatable fluorescent probe and evaluation of enzyme replacement effects on lysosomal storage diseases., Gordon Research Conference 2012, NH, USA, Jun. 2012.
45.	Seiji Hitaoka, Hiroshi Matoba, Masataka Harada, Akihiro Kawano, Syuhei Sakamoto, Kohei Okada, Tatsusada Yoshida, Daisuke Tsuji, Tkatsugu Hirokawa, Kouji Itou and Hiroshi Chuman : Linear Expression by Representative Energy Terms Analysis on Binding Affinity of Sialic Acid Analogues with Human Neuraminidase -LERE-QSAR (2), The 4th French-Japanese Workshop on Computational Methods in Chemistry, Fukuoka, Feb. 2012.
46.	Kouji Itou, Daisuke Tsuji, Kazuhiko Matsuoka, Soichiro Nishioka, Ikuo Kawashima, Yasunori Chiba, Yoshifumi Jigami, Takao Taki, Hitoshi Sakuraba, Isao Kobayashi, Hideki Sezutsu, Toshiki Tamura and Hiroaki Machii : Novel therapeutic glycoenzyme resources for lysosomal storage diseases, 21st International Symposium on Glycoconjugates, Vienna, Austria, Aug. 2011.
47.	Daisuke Tsuji, Masahiro Toyoshima and Kouji Itou : Protein kinaseC regulate morphology of microglia derived from Sandhoff disease model mice, 21st International Symposium on Glycoconjugates, Vienna, Austria, Aug. 2011.
48.	Kouji Itou, Daisuke Tsuji, Akeboshi Hiromi, Matsuoka Kazuhiko, Kawashima kuo, Chiba Yasunori, Jigami Yoshifumi, Taki Takao and Sakuraba Hitoshi : Brain-directed enzyme replacement therapy for lysosomal storage diseases., Kerala,India, Jan. 2011.
49.	Kouji Itou, Daisuke Tsuji, Kazuhiko Matsuoka, Ikuo Kawashima, Yasunori Chiba, Yoshifumi Jigami, Hitoshi Sakuraba, Isao Kobayashi, Hideki Sezutsu and Hiroaki Machii : Brain-directed enzyme replacement therapy for lysosomal storage diseases, IXth International Symposium on Biochemical Roles of Eukaryotic Cell Surface Macromolecules, Kerala, India, Jan. 2011.
50.	Kouji Itou, Daisuke Tsuji, Hiromi Akeboshi, Kazuhiko Matsuoka, Ikuo Kawashima, Yasunori Chiba, Yoshifumi Jigami, Takao Taki and Hitoshi Sakuraba : Intracerebroventricular enzyme replacement therapy for GM2 gangliosidosis, Gordon Research Conference on Lysosomal Diseases 2011, TX, USA, Jan. 2011.
51.	Seiji Hitaoka, Masataka Harada, Eri Kori, Hiroshi Matoba, Satoshi Kitao, Rahman Md. Motiur, Tatsusada Yoshida, Daisuke Tsuji, Takatsugu Hirokawa, Kouji Itou and Hiroshi Chuman : Molecular Modeling of Human Neuraminidase-1 -Structure-Activity Relation of Sialic Acid Analogs against Neuraminidases as Validation of Modeling-, Asia Hub for e-Drug Discovery Symposium (AHeDD)2010, Seoul, Dec. 2010.
52.	Kouji Itou, Takatsugu Hirokawa, Satoshi Kitao, Daisuke Tsuji, Isao Kobayashi, Hideki Sezutsu, Hiroaki Mchii, Toshiki Tamura, Shin-ichi Nakakita and Jun Hirabayashi : Production and Characterization of Recombinant Human Cathepsin A Purified from Silk Gland of Genetically Engineered Silkworm, ICS2010, Chiba, Aug. 2010.
53.	Daisuke Tsuji, T Koyama, Yoshiki Kashiwada, Yoshihisa Takaishi and Kouji Itou : Lycorine induces differentiation from embryonic stem cells into PSA-NCAM-positive cells, ICS2010, Chiba, Aug. 2010.
54.	Kazuhiko Matsuoka, Tomomi Tamura, Daisuke Tsuji, Hitoshi Sakuraba and Kouji Itou : Functional alteration of human beta-hexosaminidase B for enzyme replacement therapy for GM2 gangliosidoses, Glyco-20, Puerto Rico, USA, Dec. 2009.
55.	Kouji Itou, Kazuhiko Matsuoka, Daisuke Tsuji, Ikuo Kawashima, Hiromi Akeboshi, Yasunori Chiba, Yoshifumi Jigami and Hitoshi Sakuraba : Therapeutic approaches for Tay-Sachs and Sandhoff disease models with recombinant human lysosomal beta-hexosaminidase, Glyco-20, Puerto Rico, USA, Dec. 2009.
56.	Akishige Ikegame, Shuji Ozaki, Daisuke Tsuji, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Ayako Nakano, Kumiko Kagawa, Kyoko Takeuchi, Ken-ichiro Yata, Masahiro Abe, Kouji Itou and Toshio Matsumoto : A recombinant HLA class I-specifi single-chain Fv diabody can target cancer stem cell-like side population cells in multiple myeloma, 51th Annual Meeting of the American Society of Hematolog, New Orleans, Louisiana, USA, Dec. 2009.
57.	Seiji Hitaoka, Eri Kori, Masataka Harada, Yoshito Kadota, Yasushi Horikawa, Tatsusada Yoshida, Kouji Itou and Hiroshi Chuman : Expression and Molecular Dynamics Studies on Effect of Amino Acid Substitutions at Arg344 in Human Cathepsin A, The Second French-Japanese Workshop on Computational Methods in Chemistry 2009, Nishinomiya, Nov. 2009.
58.	Akira Otaka, Akira Shigenaga, Naomi Nishioka, Daisuke Tsuji and Kouji Itou : Cleavage of peptide bonds for the preparation of functional peptides, The 12th Japan-Korea Joint Symposium on Drug Design and Development, Sendai, May 2008.
59.	Nunuk Puwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi : Activation of IL-6/STAT3/Sca-1 system induces proliferation of duct cells in the duct-ligated mouse submandibular gland, The 2nd International Symposium on The Future Direction of Oral Sciences in The 21st Century-Oral Sciences for Our Healthy Life-, organized by Toshihiko Nagata, Tokushima, Dec. 2007.
60.	Nunuk Puwanti, Daisuke Tsuji, Ahmad Azlina, Mileva Ratko Karabasil, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : Alterations of AQP5, cellular markers of duct, and Sca-1 expression in the duct-ligated mouse submandibular gland, The 5th International Conference of Aquaporin, Nara, Jul. 2007.
61.	Kouji Itou, K Matsuoka, Daisuke Tsuji, S Aikawa, F Matsuzawa, H Akeboshi, Y Chiba, Y Jigami and H Sakuraba : Molecular design of superfunctional human b-hexosaminidase A forenzyme replacement therapy of Tay-Sachs disease and Sandhoff disease, Glyco-19, Cairns, Jul. 2007.
62.	Daisuke Tsuji, Eri Kawashita, Yukari Higashine, Hiroko Yasuoka, Yukiko Hirose and Kouji Itou : Establishment of glial cell lines derived from Sandhoff disease model mice, Glyco-19, Cairns, Jul. 2007.
63.	Nunuk Purwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : Changes of cellular markers of duct/acinni and side populations in the duct-ligated mouse submandibular gland, The 1st International Symposium and Workshop on The Future Direction of Oral Sciences in The 21st Century, organized by Bando, E., Awaji, Mar. 2007.
64.	Kouji Itou, Daisuke Tsuji, Hiroko Yasuoka and Kazuhiko Matsuoka : Induction of neurons from mesenchymal stem cells of Sandhoff disease model mice, Glycobiology and Sphingobiology 2007, Tokushima, Feb. 2007.
65.	Daisuke Tsuji, Eri Kawashita, Yukari Higashine and Kouji Itou : Characterization of glial cell lines established from Sandhoff disease model mice, Glycobiology and Sphingobiology 2007, Tokushima, Feb. 2007.
66.	H Akeboshi, Y Chiba, Y Kasahara, M Takashiba, Y Takaoka, M Ohsawa, I Kawashima, Daisuke Tsuji, Kouji Itou, H Sakuraba and Y Jigami : Production of recombinant β-hexosaminidase A that is applicable to enzyme replacement therapy for GM2 gangliosidosis, in methylotrophic yeast, Society for Glycobiology 2006, Los Angels, Nov. 2006.
67.	Nunuk Purwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : The expression of cellular markers of duct/acini and side population dynamics in the duct-ligated mouse submandibular gland., 3rd International Symposium on Salivary Glands in Honor of Niels Stensen, Okazaki, Oct. 2006.
68.	Yoshito Kadota, Seiichi Aikawa, Fumiko Matsuzawa, Kohji Tsuta, Hitoshi Sakuraba and Kouji Itou : Effects of R344-Residue substitutions on intracellular Processing and Protective Function of Human Lysosomal Protective Protein/Cathepsin A, Sialoglycoscience 2006(Fifth International Conference, Mishima, Japan), Shizuoka, Aug. 2006.
69.	Kouji Itou, Yoshito Kadota, Seiichi Aikawa, Fumiko Matsuzawa, Kohji Tsuta, Hitoshi Sakuraba, Tadashi Satoh and Souichi Wakatsuki : Predicted Molecular Interaction between Human Lysosomal Sialidase (Neuraminidase 1) and Protective Protein/Cathepsin A, Sialoglycoscience 2006(Fifth International Conference, Mishima, Japan), Shizuoka, Aug. 2006.
70.	Yoshito Kadota, Seiichi Aikawa, Fumiko Matsuzawa, Kohji Tsuta, Hitoshi Sakuraba and Kouji Itou : Effects of Amino Acid Substitutions on Intracellular Processing and Protective Function of Human Cathepsin A Revealed on Structural Modeling, IUBMB, Kyoto, Jun. 2006.
71.	H Akeboshi, Y Chiba, Y Kasahara, Y Takaoka, M Takashiba, Kouji Itou and Y Jigami : Purification and characterization of recombinant human β-hexosaminidaseA produced in methylotrophic yeast., IUBMB, Kyoto, Jun. 2006.
72.	Yutaka Tatano, Kohji Tsuta, Reiko Fujinawa, Harumi Yamamoto, Yasunori Kozutsumi, Naohiro Takeuchi, Mai Murata, Hitoshi Sakuraba, Tsutomu Takahashi, Goro Takada and Kouji Itou : Up-regulation of chemokine and cytokine expression in skin fibroblasts derived from a Costello syndrome case with impaired elastogenesis., IUBMB, Kyoto, Jun. 2006.
73.	Shunsuke Izaki, Masashi Takano, Yoshito Kadota, Takashi Yamauchi, Atsushi Umemoto, Toshinori Oka and Kouji Itou : Glycoproteomic alteration in gastric and colorectal adenocarcinomas detected on lectin blotting., IUBMB, Kyoto, Jun. 2006.
74.	Yasuhiro Ishibashi, Kazuhiko Matsuoka, Daisuke Tsuji and Kouji Itou : Development of a novel selection method for cell lines highly expressing a glycosidase composed of two subunits., IUBMB, Kyoto, Jun. 2006.
75.	Eri Kawashita, Aya Kuroki, Fumiko Matsuzawa, Seiichi Aikawa, Daisuke Tsuji, Kazuhiko Matsuoka, Hitoshi Sakuraba and Kouji Itou : Functional Alteration of Human-Murine Chimeric Lysosomal beta-Hexosaminidase A through Homology Modeling, IUBMB, Kyoto, Jun. 2006.
76.	Daisuke Tsuji, Naohiro Kuga, Mai Murata, Hitoshi Sakuraba and Kouji Itou : Analysis of glycoconjugates accumulated in oligodendrocyte precursor cells and Schwann cells derived from Sandhoff disease model mice, IUBMB, Kyoto, Jun. 2006.
77.	Kouji Itou, Daisuke Tsuji, A Kuroki and Y Ishibashi : Metabolic correction in the CNS cell lines derived from Sandhoff disease model mice, GLYCO XVIII, Florence, Italy, Sep. 2005.
78.	Daisuke Tsuji, Aya Kuroki, Yasuhiro Ishibashi and Kouji Itou : Specific Induction of Macrophage Inflammatory Proteinn 1-Alpha in the Brain Regions of Sandhoff Disease Model Mice, US/JAPAN GLYCO 2004, Honolulu, Nov. 2004.
79.	Kouji Itou, Aya Kuroki, Fumiko Matsuzawa, Sei-ichi Aikawa, Yasuhiro Ishibashi, Daisuke Tsuji, Hitoshi Sakuraba and Hirofumi Doi : Species-specific Interaction between Human and Murine Lysosomal Beta-Hexosaminidase A Subunits for GM2 Ganglioside Degradation, US/JAPAN GLYCO 2004, Honolulu, Nov. 2004.

国内講演発表:

1.	月本準, 福池凛, 三好瑞希, 堀井雄登, 五百磐俊樹, 加守虹穂, 竹内美絵, 西岡宗一郎, 田良島典子, 南川典昭, 伊藤孝司 : NEU1欠損症モデルマウスの作製と新規遺伝子治療法開発, 日本薬学会第144年会, 2024年3月.
2.	山﨑尚志, 大川亜衣梨, 山本汐里, 枇杷谷有佐, 月本準, 伊藤孝司, 小暮健太朗 : 塩基改変U1 snRNAを用いたカテプシンAスプライス異常の修復, 第62回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2023年10月.
3.	月本準, 三好瑞希, 福池凛, 堀井雄登, 加守虹穂, 竹内美絵, 田良島典子, 南川典昭, 伊藤孝司 : ノイラミニダーゼ1細胞内結晶化の抑制とリソソーム病遺伝子治療への応用, 日本核酸医薬学会第8回年会, 2023年7月.
4.	大川亜衣梨, 山本汐里, 枇杷谷有佐, 月本準, 伊藤孝司, 小暮健太朗, 山﨑尚志 : 改変 U1 snRNA を用いたカテプシン A スプライス異常の修復, 第64回日本生化学会中国四国支部例会, 2023年5月.
5.	瀧澤伶奈, 下元悠聖, 今林潔, 辻大輔, 伊藤孝司, 柏田良樹, 田中直伸 : オトギリソウ科植物の成分に関する研究(56)-Hypericum sp.花部由来のプレニル化アシルフロログルシノールの構造と生物活性-, 日本薬学会第143年会, 2023年3月.
6.	山本璃子, 長野秀嗣, 米良茜, カランジットサンギータ, 中山淳, 辻大輔, 赤木玲子, 伊藤孝司, 難波康祐 : 1,3a,6a-トリアザペンタレン類の合成と光応答型細胞毒性の評価, 日本薬学会第143年会, 2023年3月.
7.	伊藤孝司, 月本準, 三好瑞希, 福池凜 : リソソーム性ノイラミニダーゼ1⽋損症に対する新規in vivo遺伝⼦治療法開発, 第45回日本分子生物学会年会, 2022年12月.
8.	福池凜, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 三好瑞希, 木野倫子, 石丸直澄, 伊藤孝司 : AAVPHP.eBベクターの脳室内単回投与によるNEU1⽋損症に対する遺伝⼦治療, 第45回日本分子生物学会年会, 2022年12月.
9.	三好瑞希, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 福池凜, 木野倫子, 石丸直澄, 伊藤孝司 : 効率的治療を⽬的としたリソソーム性ノイラミニダーゼ1⽋損症に対するAAV5遺伝⼦治療, 第45回日本分子生物学会年会, 2022年12月.
10.	川合開斗, 桐山慧, 吉岡由真, 鬼塚正義, 水野輝, 藤岡佳祐, 広川貴次, 佐藤あやの, 伊藤孝司 : N型糖鎖改変に基づく昆⾍由来リソソーム酵素の細胞内取り込み制御機構の解析, 第45回日本分子生物学会年会, 2022年12月.
11.	大西恭弥, 村松慎⼀, 伊藤孝司 : エンドサイトーシス阻害がアデノ随伴ウイルスベクターの細胞内取り込みを促進するメカニズムの解明, 第45回日本分子生物学会年会, 2022年11月.
12.	月本準, 三好瑞希, 福池凛, 堀井雄登, 五百磐俊樹, 加守虹穂, 竹内美絵, 西岡宗一郎, 伊藤孝司 : ノイラミニダーゼ1(NEU1)細胞内結晶化阻止とNEU1欠損症の治療, 第63回日本先天代謝異常学会学術集会, 2022年11月.
13.	川合開斗, 桐山慧, 吉岡由真, 鬼塚正義, 水野輝, 藤岡佳祐, 広川貴次, 佐藤あやの, 伊藤孝司 : 哺乳類細胞を用いた昆虫細胞由来リソソーム酵素β-ヘキソサミニダーゼの発現と糖鎖改変による影響, 第95回日本生化学会大会, 2022年11月.
14.	大西恭弥, 村松慎一, 伊藤孝司 : 小胞輸送系の制御によるAAVベクター細胞内取り込み促進と治療戦略への応用, 第95回日本生化学会大会, 2022年11月.
15.	三好瑞希, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 福池凜, 木野倫子, 石丸直澄, 伊藤孝司 : 先天代謝異常症ガラクトシアリドーシスに対するより効果的な遺伝子治療薬開発, 第95回日本生化学会大会, 2022年11月.
16.	福池凜, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 三好瑞希, 伊藤孝司 : 改変型NEU1/CTSA遺伝子二重搭載AAVPHP.eBベクターを用いたNEU1欠損症に対する遺伝子治療, 第95回日本生化学会大会, 2022年11月.
17.	月本準, 三好瑞希, 福池凛, 堀井雄登, 五百磐俊樹, 加守虹穂, 竹内美絵, 西岡宗一郎, 伊藤孝司 : ノイラミニダーゼ1細胞内結晶化抑制とリソソーム病治療応用, 第95回日本生化学会大会, 2022年11月.
18.	柴田一光, 永田千明, 田崎友亮, 辻大輔, 伊藤孝司, Xue-Rong Yang, Feng-Lai Lu, Xiao-Jie Yan, Dian-Peng Li, 柏田良樹, 田中直伸 : 中国広西壮族自治区の薬用植物に関する研究(5), 第61回日本薬学会中国四国支部学術大会, 202, 2022年11月.
19.	山本璃子, 長野秀嗣, 米良茜, カランジットサンギータ, 中山淳, 辻大輔, 伊藤孝司, 難波康祐 : 1,3a,6a-トリアザペンタレン類の合成と光応答型細胞毒性の評価, 第61回日本薬学会・日本薬剤師会・日本病院薬剤師会中四国支部学術大会, 2022年11月.
20.	高橋朔良, 瀧澤伶奈, 辻大輔, 伊藤孝司, 冨永辰也, 柏田良樹, 田中直伸 : 神田茶「茶汁」に含まれるカテキン代謝物の構造と生物活性, 第9回食品薬学シンポジウム, 118-120, 2022年10月.
21.	伊藤孝司 : 神経難病GM2ガングリオシドーシスに対する日本アカデミア発のin vivo遺伝子治療法開発, ACTjapan フォーラムアカデミア臨床開発Update∼遺伝子治療のフロンティア∼, 2022年10月.
22.	川合開斗, 桐山慧, 吉岡由真, 鬼塚正義, 水野輝, 藤岡佳祐, 広川貴次, 佐藤あやの, 伊藤孝司 : 昆虫由来リソソーム酵素の N 型糖鎖改変と細胞内取り込みへの影響, 第41回日本糖質学会年会, 2022年9月.
23.	吉野悠希, 辻大輔, 伊藤孝司, 柏田良樹, 田中直伸 : セリ科Ferula communis根の成分研究(7), 日本生薬学会第68回年会, 308, 2022年9月.
24.	大西恭弥, 村松慎一, 伊藤孝司 : Dynamin依存性エンドサイトーシス阻害はマクロピノサイトーシス活性化を介してAAVベクターの細胞内取り込みを促進する, 第21回次世代を担う若手のためのファーマ・バイオフォーラム2022, 2022年9月.
25.	三好瑞希, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 福池凜, 伊藤孝司 : リソソーム性ノイラミニダーゼ1欠損症に対する効率的な遺伝子治療, 第21回次世代を担う若手のためのファーマ・バイオフォーラム2022, 2022年9月.
26.	福池凜, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 三好瑞希, 伊藤孝司 : 細胞内非結晶性 NEU1 及び CTSA 遺伝子同時搭載 AAVPHP.eB を用いたガラクトシアリドーシスモデルマウスに対する遺伝子治療, 第28回日本遺伝子細胞治療学会学術集会(JSGCT2022), 2022年7月.
27.	三好瑞希, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 福池凜, 伊藤孝司 : 細胞内結晶化抑制型NEU1とCTSAの二重搭載AAV5ベクターを用いたミオクローヌスモデルマウスの遺伝子治療, 第28回日本遺伝子細胞治療学会学術集会(JSGCT2022), 2022年7月.
28.	伊藤孝司 : 中枢神経症状を伴うライソゾーム病に対する日本発革新的遺伝子治療法の開発, 第6回神経代謝病研究会, 2022年6月.
29.	伊藤孝司 : 中枢神経症状を伴うライソゾーム病に対する新規遺伝子治療法, 第64回日本小児神経学会学術集会, 2022年6月.
30.	福池凛, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 三好瑞希, 伊藤孝司 : 改変型NEU1/CTSA遺伝子二重搭載AAVPHP.eBベクターによるミオクローヌス発症マウスの遺伝子治療, 第63回日本生化学会中国・四国支部例会, 2022年5月.
31.	水野輝, 月本準, 堀井雄登, 竹内美絵, 伊藤孝司 : TGカイコ繭由来ヒトCTSA及び人口糖鎖改変体のCTSA欠損症モデルマウス脳室内及び静脈内への補充効果解析, 第63回日本生化学会中国・四国支部例会, 2022年5月.
32.	福池凜, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 三好瑞希, 伊藤孝司 : 改変型NEU1/CTSA遺伝子二重搭載AAVPHP.eBベクターよるミオクローヌス発症マウスの遺伝子治療, 第63回日本生化学会中国・四国支部例会, 2022年5月.
33.	水野輝, 月本準, 堀井雄登, 竹内美絵, 伊藤孝司 : TGカイコ繭由来ヒトCTSA及び人工糖鎖改変体の，CTSA欠損症モデルマウス脳室内及び静脈内への補充効果解析, 第63回日本生化学会中国・四国支部例会, 2022年5月.
34.	三好瑞希, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 福池凜, 伊藤孝司 : 細胞内結晶化抑制型NEU1及びCTSA遺伝子同時搭載AAV5を用いたガラクトシアリドーシスモデルマウスに対する遺伝子治療法開発, 第63回日本生化学会中国・四国支部例会, 2022年5月.
35.	川合開斗, 桐山慧, 吉岡由真, 鬼塚正義, 藤岡佳祐, 水野輝, 広川貴次, 伊藤孝司 : 昆虫細胞由来リソソーム酵素β-ヘキソサミニダーゼの立体構造予測と糖鎖改変, 第63回日本生化学会中国・四国支部例会, 2022年5月.
36.	大西恭弥, 村松慎一, 伊藤孝司 : 神経難病GM2ガングリオシドーシスに対する新規治療薬開発, 第63回日本生化学会中国・四国支部例会, 2022年5月.
37.	月本準, 竹内美絵, 五百磐俊樹, 堀井雄登, 西岡宗一郎, 伊藤孝司 : ヒトノイラミニダーゼ1細胞内結晶化に対する付加N型糖鎖の影響, 第63回日本生化学会中国・四国支部例会, 2022年5月.
38.	川合開斗, 桐山慧, 吉岡由真, 鬼塚正義, 藤岡佳祐, 水野輝, 伊藤孝司 : 昆虫由来リソソーム性β-ヘキソサミダーゼの糖鎖改変と発現解析, 日本薬学会第142年会(名古屋), 2022年3月.
39.	大西恭弥, 辻大輔, 伊藤孝司 : 酸化ストレスに起因するエンドサイトーシス障害がSNAREタンパク質局在へ与える影響の解析, 日本薬学会第142年会(名古屋), 2022年3月.
40.	伊藤孝司, 西岡宗一郎, 篠田知果, 竹内美絵, 月本準, 佐々井優弥, 大石高生, 灘中里実, 北川裕之, 原園景, 石井明子, 小林功, 笠嶋めぐみ, 立松謙一郎, 瀬筒秀樹 : 組換えカイコと天然糖鎖資源を活用するネオグライコバイオロジクスの創製と機能評価, 日本薬学会第142年会(名古屋), 2022年3月.
41.	三好瑞希, 月本準, 堀井雄登, 竹内美絵, 加守虹穂, 福池凜, 伊藤孝司 : 細胞内非結晶性NEU1及びCTSA遺伝子同時搭載AAV5を用いたガラクトシアリドーシスモデルマウスに対する遺伝子治療, 日本薬学会第142年会(名古屋), 2022年3月.
42.	伊藤孝司 : 中枢神経症状を伴う遺伝性ライソゾーム病の遺伝子治療法開発, 名城大学総合研究所難治性疾患発症メカニズム研究センター第3回セミナー, 2022年2月.
43.	桐山慧, 藤岡佳祐, 川合開斗, 水野輝, 伊藤孝司 : 昆虫細胞におけるヒトリソソーム酵素とN型糖鎖修飾酵素の生合成及び局在解析, 第44回日本分子生物学会年会, 2021年12月.
44.	船曵早希, 佐々木彩花, 向山はるか, 辻大輔, Yoshiko Murata, 山本武範, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : イネ科植物の鉄取り込み機構解明を志向したトランスポーター標識プローブの開発, 第60回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2021年11月.
45.	田中裕大, 辻大輔, 大西恭弥, 寺本日路美, 中江隆豊, 伊藤孝司 : リソソーム蓄積症におけるオートファジーの異常及びそのメカニズムに関する研究, 第94回日本生化学会大会, 2021年11月.
46.	大西恭弥, 辻大輔, 伊藤孝司 : 老化に伴う酸化ストレスはVAMP8の輸送減少を介してオートファジーを抑制する, 第94回日本生化学会大会, 2021年11月.
47.	中江隆豊, 辻大輔, 渡邊綾佑, 大西恭弥, 寺本日路美, 伊藤孝司 : GM2ガングリオシドーシスにおける蓄積基質が引き起こす病態発現メカニズムの解析, 第94回日本生化学会大会, 2021年11月.
48.	堀井雄登, 伊藤孝司 : ガラクトシアリドーシスモデルマウス脳室内・静脈内へのCHO由来組換えヒトCTSA前駆体補充による治療効果, 第94回日本生化学会大会, 2021年11月.
49.	桐山慧, 藤岡佳祐, 川合開斗, 水野輝, 伊藤孝司 : 哺乳類と昆虫細胞におけるヒトリソソーム酵素の生合成と糖鎖修飾機構の比較解析, 第94回日本生化学会大会, 2021年11月.
50.	篠田知果, 西岡宗一郎, 小林功, 炭谷-笠嶋めぐみ, 木下崇司, 三谷藍, 大石高生, 兼子明久, 今村公紀, 北川裕之, 灘中里美, 瀬筒秀樹, 伊藤孝司 : ムコ多糖症I型ニホンザルへの遺伝子組換えカイコ由来ヒトリソソーム酵素の補充効果, 第94回日本生化学会大会, 2021年11月.
51.	月本準, 堀井雄登, 五百磐俊樹, 三好瑞希, 西岡宗一郎, 伊藤孝司 : 細胞内結晶を生じない改変型NEU1の作製とライソゾーム病治療への応用, 第94回日本生化学会大会, 2021年11月.
52.	篠田知果, 西岡宗一郎, 小林功, 炭谷-笠嶋めぐみ, 立松謙一郎, 飯塚哲也, 木下崇司, 三谷藍, 大石高生, 兼子明久, 今村公紀, 宮部-西脇貴子, 北側裕之, 灘中里美, 瀬筒秀樹, 伊藤孝司 : エンドグリコシダーゼを用いた遺伝子組換えカイコ由来ヒトリソソーム酵素のN型糖鎖改変, 第40回日本糖質学会年会, 2021年10月.
53.	竹内美絵, 堀井雄登, 瀬筒秀樹, 小林功, 笠嶋めぐみ, 立松謙一郎, 飯塚哲也, 原園景, 石井明子, 伊藤孝司 : Tgカイコ繭由来ヒトCTSAの欠損症モデルマウス末梢臓器への補充効果, 第40回日本糖質学会年会, 2021年10月.
54.	月本準, 竹内美絵, 五百磐俊樹, 堀井雄登, 西岡宗一郎, 伊藤孝司 : N型糖鎖付加のヒトノイラミニダーゼ1細胞内結晶化への影響, 第40回日本糖質学会年会, 2021年10月.
55.	中江隆豊, 辻大輔, 渡邊綾佑, 大西恭弥, 山本圭, 沖野望, 伊東信, 伊藤孝司 : GM2ガングリオシドーシスにおけるLysoスフィンゴ糖脂質の病態生理学的役割, 第40回日本糖質学会年会, 2021年10月.
56.	高橋朔良, 田中直伸, 辻大輔, 伊藤孝司, 柏田良樹 : 神田茶「茶汁」に関する科学的研究(4), 第60回日本薬学会中国四国支部学術大会, 118, 2021年10月.
57.	高橋朔良, 田中直伸, 辻大輔, 伊藤孝司, 柏田良樹 : 神田茶「茶汁」に関する科学的研究(3), 日本生薬学会第67回年会, 246, 2021年9月.
58.	田中直伸, 高橋朔良, 梶原聖太, 丹羽莞慈, 辻大輔, 伊藤孝司, 柏田良樹 : ウズベキスタン産薬用植物Perovskia scrophulariifoliaより単離した新規ノルジテルペンperovsfolin A-Dの構造と生物活性, 第63回天然有機化合物討論会, 475-480, 2021年9月.
59.	仲村和佳, 伊藤孝司 : マンノース6-リン酸受容体システム制御によるリソソーム酵素発現システムの開発, 第62回日本生化学会中国・四国支部例会, 2021年9月.
60.	月本準, 竹内美絵, 五百磐俊樹, 堀井雄登, 西岡宗一郎, 伊藤孝司 : ヒトノイラミニダーゼ1細胞内結晶化に対する付加N型糖鎖の影響, 第62回日本生化学会中国・四国支部例会, 2021年9月.
61.	竹内美絵, 堀井雄登, 瀬筒秀樹, 小林功, 笠嶋めぐみ, 立松謙一郎, 飯塚哲也, 原園景, 石井明子, 伊藤孝司 : Tgカイコ繭由来ヒトCTSAの欠損症モデルマウスへの脳室内投与効果, 第62回日本生化学会中国・四国支部例会, 2021年9月.
62.	大西恭弥, 辻大輔, 伊藤孝司 : 酸化ストレスは細胞内小胞輸送系を阻害することでオートファジーを抑制する, 第62回日本生化学会中国・四国支部例会, 2021年9月.
63.	Saki Funabiki, 佐々木彩花, Haruka Mukaiyama, 辻大輔, Yoshiko Murata, 山本武範, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : イネ科植物の鉄取り込み機構解明を志向したトランスポーター標識プローブの開発, 創薬懇話会2021, 2021年6月.
64.	傳田将也, 小宮千明, 上田将弘, 月本準, 伊藤孝司, 重永章, 大髙章 : 既存モダリティの高度化を指向したペプチド・タンパク質新規修飾法の開発, 日本薬剤学会第36年会, 2021年5月.
65.	篠田知果, 西岡宗一郎, 小林功, 炭谷-笠嶋めぐみ, 松崎祐二, 飯野健太, 木下崇司, 三谷藍, 大石高生, 兼子明久, 今村公紀, 北川裕之, 灘中里美, 瀬筒秀樹, 伊藤孝司 : エンドグリコシダーゼを用いたトランスジェニックカイコ由来ヒトα-L-iduronidaseのN型糖鎖改変, 日本薬学会第141年会, 2021年3月.
66.	竹内美絵, 瀬筒秀樹, 小林功, 炭谷-笠島めぐみ, 立松謙一郎, 飯塚哲也, 木下崇司, 三谷藍, 伊藤孝司 : TGカイコ繭由来ヒトCTSAのガラクトシアリドーシスモデルマウス末梢臓器への酵素補充と有効性評価, 日本薬学会第141年会, 2021年3月.
67.	中江隆豊, 辻大輔, 大西恭弥, 寺本日路美, 伊藤孝司 : GM2ガングリオシドーシスの病態における蓄積生体内基質が与える影響の解析, 日本薬学会第141年会, 2021年3月.
68.	福士友理, 堀井雄登, 仲村和佳, 広川貴次, 鬼塚正義, 伊藤孝司 : ガラクトシアリドーシスの治療を目指したN型糖鎖追加型カテプシンAの分子機能解析, 日本薬学会第141年会, 2021年3月.
69.	堀井雄登, 伊藤孝司 : 酵素補充療法によるガラクトシアリドーシス治療に向けたCHO由来ヒトCTSA前駆体の補充効果検討, 日本薬学会第141年会, 2021年3月.
70.	月本準, 堀井雄登, 五百磐俊樹, 三好瑞希, 西岡宗一郎, 伊藤孝司 : ノイラミニダーゼ1(NEU1)の細胞内結晶化阻止とNEU1欠損症遺伝子治療シーズへの応用, 日本薬学会第141年会, 2021年3月.
71.	篠田知果, 西岡宗一郎, 月本準, 小林功, 笠嶋めぐみ, 松崎裕二, 飯野健太, 木下崇司, 三谷藍, 竹内美絵, 佐々井優弥, 辻大輔, 瀬筒秀樹, 伊藤孝司 : 遺伝子組み換えカイコを用いたムコ多糖症I型酵素補充療法の確立, 第93回日本生化学会大会, 2020年9月.
72.	田中裕大, 辻大輔, 大西恭弥, 北口眞大, 眞継毅, 寺本日路美, 中江隆豊, 伊藤孝司 : リソソーム性加水分解酵素の欠損がオートファジーに与える影響に関する検討, 第93回日本生化学会大会, 2020年9月.
73.	月本準, 堀井雄登, 五百磐俊樹, 三好瑞希, 西岡宗一郎, 伊藤孝司 : ヒトノイラミニダーゼ1細胞内結晶化の阻止とリソソーム病治療, 第93回日本生化学会大会, 2020年9月.
74.	北口眞大, 辻大輔, 大西恭弥, 寺本日路美, 伊藤孝司 : 中枢神経症状を呈するリソソーム病におけるミクログリア極性転換を標的とした新規治療法開発, 第93回日本生化学会大会, 2020年9月.
75.	眞継毅, 辻大輔, 中江隆豊, 寺本日路美, 山本圭, 伊藤孝司 : ヒトTay-Sachs病神経細胞モデルにおける蓄積GM2ガングリオシドの異常な細胞内局在, 第93回日本生化学会大会, 2020年9月.
76.	中江隆豊, 辻大輔, 大西恭弥, 眞継毅, 伊藤孝司 : GM2ガングリオシドーシスモデルマウスにおける中枢神経症状の病態発現メカニズムの解析, 第93回日本生化学会大会, 2020年9月.
77.	福士友理, 堀井雄登, 仲村和佳, 広川貴次, 鬼塚正義, 伊藤孝司 : ガラクトシアリドーシスの治療を目指したN型糖鎖追加型カテプシンAの創製と分子機能解析, 第93回日本生化学会大会, 2020年9月.
78.	大西恭弥, 辻大輔, 伊藤孝司 : 老化による加齢性色素Lipofuscinの蓄積はオートファジー機能を低下させる, 第93回日本生化学会大会, 2020年9月.
79.	篠田知果, 西岡宗一郎, 月本準, 小林功, 笠嶋めぐみ, 松崎祐二, 飯野健太, 木下崇司, 三谷藍, 竹内美絵, 佐々井優弥, 辻大輔, 瀬筒秀樹, 伊藤孝司 : トランスジェニックカイコ繭を用いたムコ多糖症Ⅰ型治療薬の開発, 第61回日本生化学会中国・四国支部例会, 2020年7月.
80.	竹内美絵, 五百磐俊樹, 大西恭弥, 堀井雄登, 月本準, 仲村和佳, 瀬筒秀樹, 小林功, 笠嶋めぐみ, 立松謙一郎, 飯塚哲也, 原園景, 石井明子, 松崎裕二, 飯野健太, 木下崇司, 三谷藍, 伊藤孝司 : トランスジェニックカイコ繭由来ヒトCTSAの有効性評価, 第61回日本生化学会中国・四国支部例会, 2020年7月.
81.	北口眞大, 辻大輔, 大西恭弥, 伊藤孝司 : リソソーム病におけるミクログリア極性転換を利用した治療法開発, 第61回日本生化学会中国・四国支部例会, 2020年7月.
82.	月本準, 堀井雄登, 五百磐俊樹, 三好瑞希, 西岡宗一郎, 伊藤孝司 : NEU1細胞内結晶化の抑制とNEU1欠損症遺伝子治療への応用, 第61回日本生化学会中国・四国支部例会, 2020年7月.
83.	寺本日路美, 辻大輔, 大西恭弥, 眞継毅, 中江隆豊, 伊藤孝司 : GM2ガングリオシドーシス神経細胞死モデルの構築と化合物による治療効果の検討, 第61回日本生化学会中国・四国支部例会, 2020年7月.
84.	福士友理, 堀井雄登, 仲村和佳, 広川貴次, 鬼塚正義, 伊藤孝司 : GS治療薬の開発を目指した糖鎖追加型カテプシンAの機能解析, 第61回日本生化学会中国・四国支部例会, 2020年7月.
85.	大西恭弥, 辻大輔, 伊藤孝司 : 加齢性色素Lipofuscinの蓄積によるオートファジー異常の解析, 第61回日本生化学会中国・四国支部例会, 2020年7月.
86.	堀井雄登, 伊藤孝司 : ガラクトシアリドーシス治療に向けたCHO由来組換えヒトCTSA前駆体の補充効果解析, 第61回日本生化学会中国・四国支部例会, 2020年7月.
87.	中江隆豊, 辻大輔, 大西恭弥, 眞継毅, 伊藤孝司 : GM2ガングリオシドーシスにおける病態発現メカニズムの解析, 第61回日本生化学会中国・四国支部例会, 2020年7月.
88.	月本準, 堀井雄登, 五百磐俊樹, 西岡宗一郎, 伊藤孝司 : NEU1の細胞内結晶化阻止と遺伝子治療への応用, 日本薬学会第140年会, 2020年3月.
89.	大西恭弥, 辻大輔, 伊藤孝司 : 老化によるオートファジー異常とそのメカニズムの解明, 日本薬学会第140年会, 2020年3月.
90.	北口眞大, 辻大輔, 大西恭弥, 伊藤孝司 : 中枢神経症状を呈するリソソーム病におけるミクログリア極性解析とJNK inhibitor を用いた治療効果検討, 日本薬学会第140年会, 2020年3月.
91.	眞継毅, 辻大輔, 中江隆豊, 寺本日路美, 山本圭, 伊藤孝司 : Tay-Sachs病神経細胞モデルの構築と蓄積糖脂質の細胞内局在解析, 日本薬学会第140年会, 2020年3月.
92.	寺本日路美, 辻大輔, 大西恭弥, 眞継毅, 中江隆豊, 田中裕大, 伊藤孝司 : GM2ガングリオシドーシス神経細胞モデルの構築とFTY720による治療効果の検討, 日本薬学会第140年会, 2020年3月.
93.	中江隆豊, 辻大輔, 大西恭弥, 眞継毅, 伊藤孝司 : GM2ガングリオシドーシスにおける神経細胞死誘導メカニズムの解析, 日本薬学会第140年会, 2020年3月.
94.	五百磐俊樹, 麻植真結子, 堀井雄登, 安藤春菜, 竹内美絵, 仲村和佳, 伊藤孝司 : カテプシンA欠損症モデルマウスの病理解析と蓄積基質の動態解析, 日本薬学会第140年会, 2020年3月.
95.	船曵早希, 佐々木彩花, 向山はるか, 辻大輔, 村田佳子, 山本武範, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : イネ科植物の鉄イオン取り込みトランスポーター標識プローブの合成と評価, 日本薬学会第140年会, 2020年3月.
96.	小祝孝太郎, 月本準, 東哲也, 加藤龍一, M.G.Chavas Leonard, 千田俊哉, 伊藤孝司, 湯本史明 : ヒトタンパク質の哺乳類細胞を用いた細胞内結晶化, 第42回日本分子生物学会, 2019年12月.
97.	五百磐俊樹, 麻植真結子, 堀井雄登, 安藤春菜, 竹内美絵, 仲村和佳, 伊藤孝司 : カテプシンA欠損症モデルマウスの表現型と病理解析, 第42回日本分子生物学会, 2019年12月.
98.	月本準, 堀井雄登, 西岡宗一郎, 五百磐俊樹, 伊藤孝司 : ヒトノイラミニダーゼ1 の細胞内結晶化制御と治療への応用, 第42回日本分子生物学会, 2019年12月.
99.	船曵早希, 佐々木彩花, 辻大輔, 村田佳子, カランジットサンギータ, 中山淳, 伊藤孝司, 山本武範, 難波康祐 : イネ科植物の鉄イオン取り込み機構解明に向けた標識プローブの合成と評価, 第58回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2019年11月.
100.	高橋里奈, 植田百花, 小出華永, 川合真央, 山﨑尚志, 月本準, 伊藤孝司, 滝口祥令 : イントロンやエクソン内の配列と結合する改変U1 snRNAによるCTSAエクソン7スプライス異常の修復, 第58回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2019年11月.
101.	浜田麻衣, 中山淳, 中山慎一朗, 寺町順平, 辻大輔, 重永章, 安部正博, 伊藤孝司, 大髙章, 難波康祐 : 天然マクロライドの網羅的全合成が拓く新規多発性骨髄腫治療薬の開発研究, 2019年度第2回(第30回)日本プロセス化学会東四国フォーラムセミナー, 2019年10月.
102.	福士友理, 堀井雄登, 仲村和佳, 広川貴次, 木下崇司, 三谷藍, 堂崎雅仁, 伊藤孝司 : 哺乳類細胞由来CTSAの糖鎖改変に基づく分子機能解析, 第92回日本生化学会大会, 2019年9月.
103.	堀井雄登, 伊藤孝司 : ガラクトシアリドーシスモデルに対するCHO由来組換えヒトカテプシンA(CTSA)前駆体の補充効果, 第92回日本生化学会大会, 2019年9月.
104.	月本準, 堀井雄登, 西岡宗一郎, 五百磐俊樹, 伊藤孝司 : ヒトノイラミニダーゼ1の細胞内結晶化の抑制とリソソーム蓄積症治療への応用, 第92回日本生化学会大会, 2019年9月.
105.	大西恭弥, 辻大輔, 加守虹穂, 村松慎一, 伊藤孝司 : GM2ガングリオシドーシスに対する，改変型β-Hexosaminidase B発現AAVベクターによる遺伝子治療法開発, 第92回日本生化学会大会, 2019年9月.
106.	楠本嵩志, 堂前純子, 田中直伸, 柏田良樹, 辻大輔, 伊藤孝司, 石田竜弘, 奥平桂一郎 : 天然物による膜トランスポーターABCA7の発現増強機構の解析, 第92回日本生化学会大会, 2019年9月.
107.	田中裕大, 辻大輔, 大西恭弥, 眞継毅, 寺本日路美, 中江隆豊, 伊藤孝司 : リソソーム酵素欠損に基づくリソソーム局在性SNAREタンパク質の減少とオートファジー異常に関する解析, 第92回日本生化学会大会, 2019年9月.
108.	伊藤孝司, 西岡宗一郎, 篠田知果, 竹内美絵, 福士友理, 月本準, 辻大輔, 小林功, 炭谷めぐみ, 飯塚哲也, 木下嵩司, 三谷藍, 堂崎雅仁, 須田稔, 松崎祐二, 飯野健太, 瀬筒秀樹 : 組換えカイコ絹糸腺で高発現するヒトリソソーム酵素のN型糖鎖改変と医薬応用, 第38回日本糖質学会年会, 2019年8月.
109.	眞継毅, 辻大輔, 中江隆豊, 寺本日路美, 井澤大貴, 山本圭, 伊藤孝司 : ヒトTay-Sachs病神経細胞モデルの構築とGM2ガングリオシドの細胞内局在解析, 第38回日本糖質学会年会, 2019年8月.
110.	Jun Tsukimoto, Yuto Horii, 西岡宗一郎 and Kouji Itou : Suppression of in cellulo crystallization of NEU1 and application for gene therapy for NEU1 deficiency, 第25回日本遺伝子細胞治療学会(JSGCT2019), Jul. 2019.
111.	船曵早希, 佐々木彩花, 向山はるか, 村田佳子, カランジットサンギータ, 中山淳, 難波康祐, 占部敦美, 辻大輔, 伊藤孝司 : イネ科植物の鉄イオン取り込み機構の解明に向けた化学プローブの開発, 第14回トランスポーター研究会年会, 2019年7月.
112.	Yukiya Ohnishi, Daisuke Tsuji, Nijiho Kamori, 村松慎一 and Kouji Itou : Development of the gene therapy by utilizing modified β-Hexosaminidase B for GM2 gangliosidoses, 第25回日本遺伝子細胞治療学会(JSGCT2019), Jul. 2019.
113.	浜田麻衣, 森崎巧也, 中山淳, 寺町順平, 辻大輔, 重永章, 山本武範, 篠原康雄, 大髙章, 伊藤孝司, 安部正博, 難波康祐 : 天然マクロライドの全合成が拓く新規多発性骨髄腫治療薬, 創薬懇話会2019 in 秋保(仙台), 2019年6月.
114.	伊藤孝司, 大西恭弥, 辻大輔, 村松慎一 : Tay-Sachs病に対する遺伝子治療法開発, 第61回日本小児神経学会学術集会, 2019年5月.
115.	堀井雄登, 伊藤孝司 : ガラクトシアリドーシスモデルに対するCHO由来組換えヒトCTSA前駆体の治療効果, 第60回日本生化学会中国・四国支部例会, 2019年5月.
116.	月本準, 堀井雄登, 西岡宗一郎, 伊藤孝司 : ヒトノイラミニダーゼ1の細胞内結晶化抑制とNEU1欠損症治療への応用, 第60回日本生化学会中国・四国支部例会, 2019年5月.
117.	北口眞大, 辻大輔, 伊藤孝司 : リソソーム病におけるミクログリア極性及び極性転換機構の解析, 第60回日本生化学会中国・四国支部例会, 2019年5月.
118.	田中裕大, 辻大輔, 大西恭弥, 眞継毅, 寺本日路美, 中江隆豊, 伊藤孝司 : リソソーム性分解酵素の遺伝的欠損に起因するオートファジーの異常とそのメカニズム解析, 第60回日本生化学会中国・四国支部例会, 2019年5月.
119.	五百磐俊樹, 伊藤孝司 : カテプシンA欠損症モデルマウスの基質の変動と行動解析, 第60回日本生化学会中国・四国支部例会, 2019年5月.
120.	大西恭弥, 辻大輔, 渡邊綾佑, 加守虹穂, 村松慎一, 伊藤孝司 : GM2ガングリオシドーシスに対する，AAVベクターを用いた遺伝子治療法開発, 日本薬学会第139年会, 2019年3月.
121.	北口眞大, 辻大輔, 伊藤孝司, 伊藤孝司 : リソソーム病におけるミクログリア極性転換の解析, 日本薬学会第139年会, 2019年3月.
122.	浜田麻衣, 中山淳, 重永章, 辻大輔, 寺町順平, 安部正博, 伊藤孝司, 大髙章, 難波康祐 : 新規Ynone化合物の創生・評価, 日本薬学会第139年会, 2019年3月.
123.	楠本嵩志, 堂前純子, 田中直伸, 柏田良樹, 辻大輔, 伊藤孝司, 石田竜弘, 奥平桂一郎 : 膜タンパク質ABCA7を増加させる新規天然物, 日本薬学会第139年会, 2019年3月.
124.	月本準, 西岡宗一郎, 堀井雄人, 東哲也, 伊藤孝司 : アミノ酸置換によるヒトノイラミニダーゼ1(NEU1)の細胞内結晶化の抑制と医療応用, 第42回日本分子生物学会年会, 2018年11月.
125.	五百磐俊樹, 伊藤孝司 : スプライシング異常に基づくカテプシンA欠損症モデルマウスにおけるEndothelin-1の動態, 第42回日本分子生物学会年会, 2018年11月.
126.	佐々木彩花, 向山はるか, 辻大輔, 村田佳子, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : 鉄取り込み機構解明を志向したトランスポーター標識プローブの開発, 第57回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2018年11月.
127.	四宮槙子, 小出華永, 高橋里奈, 山﨑尚志, 月本準, 伊藤孝司, 滝口祥令 : Exon specific U1 snRNAによる CTSAエクソン7スプライス異常の修復, 第57回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2018年11月.
128.	大西恭弥, 辻大輔, 渡邊綾佑, 浅井克仁, 村松慎一, 伊藤孝司 : AAV によるGM2 ガングリオシドーシスモデルマウスに対する遺伝子治療, 第60回日本先天代謝異常学会総会, 2018年11月.
129.	伊藤孝司, 大西恭弥, 辻大輔, 渡邊綾佑, 浅井克仁, 村松慎一 : AAV ベクターによるGM2 ガングリオシドーシスの遺伝子治療法開発, 第60回日本先天代謝異常学会総会, 2018年11月.
130.	伊藤孝司, 西岡宗一郎, 炭谷めぐみ, 飯塚哲也, 瀬筒秀樹, 松崎祐二, 飯野健太, 木下崇司, 堂崎雅仁, 須田稔 : Endo-M N175Q 及びEndo-CC N180H を用いる高分子量N 型ネオグライコプロテインの開発, 第9回グライコバイオロジクス研究会, 2018年10月.
131.	四宮槙子, 小出華永, 高橋里奈, 山﨑尚志, 月本準, 伊藤孝司, 滝口祥令 : Exon specific U1 snRNAを用いたCTSAエクソン7スキッピングの修復, 第91回日本生化学会大会, 2018年9月.
132.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル, 眞継毅, 大西恭弥, 伊藤孝司 : リソソーム病で共通するオートファジー異常とそのメカニズム解析, 第91回日本生化学会大会, 2018年9月.
133.	月本準, 伊藤孝司 : ヒトノイラミニダーゼ4(NEU4)の細胞内局在変化, 第91回日本生化学会大会, 2018年9月.
134.	大西恭弥, 辻大輔, 村松慎一, 伊藤孝司 : AAVベクターを用いたGM2ガングリオシドーシスモデルマウスの遺伝子治療, 第91回日本生化学会大会, 2018年9月.
135.	宇野マイケル新太郎, 辻大輔, 渡邊綾佑, 田中裕大, 伊藤孝司 : リソソーム病における神経細胞死に対するリソソーム制御因子TFEBの役割, 第91回日本製化学会大会, 2018年9月.
136.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 大西恭弥, 山本圭, 広川貴次, 沖野望, 伊東信, 伊藤孝司 : Lysoスフィンゴ糖脂質はPI2K/Aktシグナリングの阻害により神経細胞死を引き起こす, 第91回日本生化学会, 2018年9月.
137.	幾尾真理子, 杉崎圭, 寺町順平, 田原栄俊, 安倍正博, 伊藤孝司 : 骨芽前駆細胞の骨分化経路BMP/Smadは，核内DNA結合Smadを標的とする多発性骨髄腫由来分泌小胞exosomeによって抑制される, 第91回日本生化学会大会, 2018年9月.
138.	伊藤孝司, 西岡宗一郎, 小林功, 笠嶋めぐみ, 立松謙一郎, 瀬筒秀樹, 松崎祐二, 飯野健太, 木下崇司, 堂崎雅仁, 灘中里美, 北川裕之 : エンドグリコシダーゼと機能性合成N型糖鎖を利用するネオ糖タンパク質医薬品の開発を目指して, 第70回日本生物工学大会プログラム, 2018年9月.
139.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル, 眞継毅, 大西恭弥, 伊藤孝司 : リソソーム病におけるオートファジー異常の原因解明と病態に及ぼす影響, 第17回次世代を担う若手ファーマ・バイオフォーラム2018, 2018年9月.
140.	西岡宗一郎, 小林功, 炭谷めぐみ, 飯塚哲也, 日高朋, 木下嵩司, 住吉渉, 三谷藍, 堂崎雅仁, 須田稔, 辻大輔, 瀬筒秀樹, 伊藤孝司 : ENGase(Endo-CC)を用いたTGカイコ由来ヒトリソソーム酵素のN型糖鎖修飾, 第37回日本糖質学会年会, 2018年8月.
141.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 大西恭弥, 山本圭, 広川貴次, 沖野望, 伊東信, 伊藤孝司 : Lysoスフィンゴ糖脂質が神経細胞死を起こす分子メカニズムの解明, 第37回日本糖質学会年会, 2018年8月.
142.	小宮千明, 月本準, 上田将弘, 森崎巧也, 猪熊翼, 重永章, 伊藤孝司, 大髙章 : 加水分解酵素を利用したC末端特異的チオエステル化反応の開発, 第50回若手ペプチド夏の勉強会, 2018年8月.
143.	Kouji Itou : Gene therapy for GM2 ganglisosidosis with CNS involvement., 第24回日本遺伝子細胞治療学会学術集会, Jul. 2018.
144.	小宮千明, 月本準, 上田将弘, 森崎巧也, 猪熊翼, 重永章, 伊藤孝司, 大髙章 : 発現タンパク質に適用可能な新規チオエステル合成法の開発, 創薬懇話会 2018 in 志賀島, 2018年6月.
145.	四宮槙子, 小出華永, 高橋里奈, 月本準, 山﨑尚志, 伊藤孝司, 滝口祥令 : 改変U1 snRNAによるカテプシンAスプライス異常修復効果の検討, 第59回日本生化学会中国四国支部例会, 2018年5月.
146.	西岡宗一郎, 小林功, 松崎祐二, 飯野健太, 灘中里美, 笠島めぐみ, 日高朋, 辻大輔, 瀬筒秀樹, 北川裕之, 山本憲二, 伊藤孝司 : 化学酵素法によるTGカイコ繭由来ヒトリソソーム酵素の糖鎖修飾と酵素補充効果, 第59回日本生化学会中国・四国支部例会, 2018年5月.
147.	大西恭弥, 辻大輔, 村松慎一, 伊藤孝司 : AAVベクターによるGM2ガングリオシドーシスに対する遺伝子治療, 第59回日本生化学会中国・四国支部例会, 2018年5月.
148.	宇野マイケル新太郎, 辻大輔, 渡邊綾佑, 田中裕大, 伊藤孝司 : TNF-α及びIL-1βによるリソソーム制御因子TFEBの発現上昇メカニズムの解析, 第59回日本生化学会中国・四国支部例会, 2018年5月.
149.	月本準, 伊藤孝司 : ヒトノイラミニダーゼ4(NEU4)の細胞内局在性解析, 第59回日本生化学会中国・四国支部例会, 2018年5月.
150.	伊藤孝司 : in vivo Gene Therapy for GM2 Gangliosidoses, 第59回日本神経学会学術大会, 2018年5月.
151.	伊藤孝司 : GM2ガングリオシドーシスの遺伝子治療, 第59回日本神経学会学術大会, 2018年5月.
152.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 沖野望, 伊東信, 伊藤孝司 : lysoスフィンゴ糖脂質によって引き起こされる細胞死メカニズムの解明, 第59回日本生化学会中国・四国支部例会, 2018年5月.
153.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル, 眞継毅, 大西恭弥, 伊藤孝司 : SNAREタンパク質の局在変化に起因するリソソーム病におけるオートファジー異常, 第59回日本生化学会中国・四国支部例会, 2018年5月.
154.	堀井雄登, 池啓伸, 田中優希, 辻大輔, 伊藤孝司 : カテプシンA欠損モデルマウス由来小脳組織および初代培養神経系を用いた病態生理学的解析, 第59回日本生化学会中国・四国支部例会, 2018年5月.
155.	小宮千明, 月本準, 森崎巧也, 津田雄介, 宮島凜, 猪熊翼, 重永章, 伊藤孝司, 大髙章 : 均一修飾タンパク質の合成を指向したタンパク質C末端特異的活性化反応の開発, 日本薬学会第138年会, 2018年3月.
156.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 沖野望, 伊東信, 伊藤孝司 : リソソーム病で蓄積するlysoスフィンゴ糖脂質が神経系細胞に与える影響, 日本薬学会第138年会, 2018年3月.
157.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル新太郎, 眞継毅, 伊藤孝司 : リソソーム病でのオートファジー異常に関わる共通因子の解析, 日本薬学会第138年会, 2018年3月.
158.	辻大輔, 宇野マイケル新太郎, SPAMPANATE Carmine, 田中裕大, 渡邊綾佑, BALLABIO Andrea, 伊藤孝司 : リソソーム病における神経細胞死に対するリソソーム制御因子TFEBの役割, 日本薬学会第138年会, 2018年3月.
159.	佐々木彩花, 向山はるか, 辻大輔, 村田佳子, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : ムギネ酸・鉄錯体取り込みトランスポーター標識プローブの開発, 第56回日本薬学会第138年会, 2018年3月.
160.	宇野マイケル新太郎, 辻大輔, 渡邊綾佑, 田中裕大, Spampanato Carmine, Ballabio Andrea, 伊藤孝司 : 神経炎症におけるTNFーalphaの転写因子TFEB発現に与える影響の解析, 生命科学系学会合同年次大会 ConBio2017, 2017年12月.
161.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 沖野望, 伊東信, 伊藤孝司 : スフィンゴリピドーシスにおける神経細胞死に及ぼすlysoスフィンゴ糖脂質の役割, 生命科学系学会合同年次大会 ConBio2017, 2017年12月.
162.	堀井雄登, 池啓伸, 田中優希, 辻大輔, 伊藤孝司 : カテプシンA欠損症モデルマウス小脳の病理学的解析と初代培養神経系の構築, 生命科学系学会合同年次大会 ConBio2017, 2017年12月.
163.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル新太郎, 伊藤孝司 : リソソーム病におけるオートファジー異常とSNAREタンパク質の関与, 生命科学系学会合同年次大会 ConBio2017, 2017年12月.
164.	月本準, 伊藤孝司 : ヒトノイラミニダーゼ4(NEU4)に関する新知見, 生命科学系学会合同年次大会 ConBio2017, 2017年12月.
165.	伊藤孝司 : 哺乳類リソソーム酵素特異的なマンノース6ーリン酸含有N型糖鎖付加修飾機構と人工付加技術, 生命科学系学会合同年次大会 ConBio2017, 2017年12月.
166.	成瀬公人, 大川内健人, 猪熊翼, 重永章, 伊藤孝司, 大髙章 : N-S-acyl-transfer-mediated On-resin Formation of Thioester with Practical Application to Peptide Synthesis, 第54回ペプチド討論会, 2017年11月.
167.	小宮千明, 月本準, 森崎巧也, 津田雄介, 宮島凜, 猪熊翼, 重永章, 伊藤孝司, 大髙章 : Development of methodology for producing thioesters from naturally occurring peptide sequence, 第54回ペプチド討論会, 2017年11月.
168.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 沖野望, 伊東信, 伊藤孝司 : スフィンゴリピドーシス患者iPS細胞由来神経細胞を用いた病態解析と治療法検討, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
169.	月本準, 伊藤孝司 : 組換えヒトノイラミニダーゼ4の分子特性解析, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
170.	占部敦美, 津川稜, 西尾賢, 佐々木彩花, 鈴木基史, カランジットサンギータ, 中山淳, 伊藤孝司 : アルカリ性不良土壌での農耕を志向したムギネ酸類の実用化研究, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
171.	佐々木彩花, 向山はるか, 占部敦美, 辻大輔, 村田佳子, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : 鉄イオン取り込みトランスポーターの標識プローブの開発, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
172.	宇野マイケル新太郎, 辻大輔, 渡邊綾祐, 田中裕大, Spampanato Carmine, Ballabio Andrea, 伊藤孝司 : 神経炎症にTNF-αが転写因子TFEB発現に与える影響の解析, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
173.	日高朋, 西岡宗一郎, 原囿景, 月本準, 田中優希, 笠嶋めぐみ, 小林功, 辻大輔, 石井明子, 瀬筒秀樹, 伊藤孝司 : トランスジェニックカイコ繭由来カテプシンAの有効性評価, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
174.	堀井雄登, 池啓伸, 田中優希, 辻大輔, 伊藤孝司 : カテプシンA欠損症モデルマウス小脳組織および初代培養神経系の病理学的解析, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
175.	田中優希, 堀井雄登, 池啓伸, 辻大輔, 伊藤孝司 : スプライシング異常誘導型カテプシンA欠損症マウスの性状解析と疾患モデルとしての有効性, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
176.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル新太郎, 伊藤孝司 : リソソーム病でのオートファジー低下に対するSNAREタンパク質局在の影響, 第56回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2017年10月.
177.	伊藤孝司 : 中枢神経症状を伴うリソソーム病に対する治療法開発, 第19回応用薬理シンポジウム, 2017年9月.
178.	月本準, 伊藤孝司 : ヒトノイラミニダーゼ1(NEU1)及びNEU4の発現と分子特性解析, 第16回次世代を担う若手ファーマ・バイオフォーラム2017, 2017年9月.
179.	日高朋, 西岡宗一郎, 原囿景, 月本準, 田中優希, 堀井雄登, 小林功, 笠嶋めぐみ, 辻大輔, 石井明子, 瀬筒秀樹, 伊藤孝司 : トランスジェニックカイコ繭由来カテプシンAの有効性評価とエンドグリコシダーゼによる踏査改変, 第36回日本糖質学会年会, 2017年7月.
180.	辻大輔, 渡邊綾佑, 田中裕大, 宇野マイケル新太郎, 伊藤孝司 : GM2ガングリオシドーシスにおける神経細胞死メカニズムの解明, 第36回日本糖質学会年会, 2017年7月.
181.	伊藤孝司, 西岡宗一郎, 小林功, 笠嶋めぐみ, 原囿景, 松崎祐二, 飯野健太, 山本賢二, 灘中里美, 北川裕之, 日高朋, 辻大輔, 石井明子, 瀬筒秀樹 : エンドグリコシダーゼの糖鎖転移活性を利用するネオグライコ酵素の創製とリソソーム病治療薬開発, 第36回日本糖質学会年会, 2017年7月.
182.	佐々木彩花, 向山はるか, 占部敦美, 辻大輔, 村田佳子, カランジットサンギータ, 中山淳, 伊藤孝司, 難波康祐 : イネ科植物の鉄イオン取り込みトランスポーターの機構解明に向けた化学プローブの開発, 第12回トランスポーター研究会年会, 2017年7月.
183.	田中裕大, 辻大輔, 渡邊綾佑, 宇野マイケル新太郎, 伊藤孝司 : リソソーム蓄積症におけるオートファジーフラックス異常の解析, 第58回日本生化学会中四国支部例会, 2017年5月.
184.	月本準, 伊藤孝司 : ヒトノイラミニダーゼ4(NEU4)の分子特性解析, 第58回日本生化学会中四国支部例会, 2017年5月.
185.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 沖野望, 伊東信, 伊藤孝司 : スフィンゴリピドーシスにおけるLysoスフィンゴ糖脂質の細胞に与える影響の解析, 第58回日本生化学会中四国支部例会, 2017年5月.
186.	宇野マイケル新太郎, 辻大輔, 渡邊綾祐, 田中裕大, Spampanato Carmine, Ballabio Andrea, 伊藤孝司 : Sandhoff病モデルマウス脳内での神経細胞死に対するリソソーム制御因子Tfebにより誘導されるオートファジーの関与, 第58回日本生化学会中四国支部例会, 2017年5月.
187.	田中優希, 池啓伸, 堀井雄登, 辻大輔, 伊藤孝司 : スプライシング異常に起因するカテプシンA欠損症モデルマウスの性状解析, 第58回日本生化学会中四国支部例会, 2017年5月.
188.	伊藤孝司 : 組換えカイコ繭由来ライソゾーム病治療薬の開発, 日本薬学会第137年会一般シンポジウム, 2017年3月.
189.	宇野マイケル新太郎, 辻大輔, 田中裕大, 渡邊綾佑, Spampamato CARMINE, Ballabio ANDREA, 伊藤孝司 : Sandhoff病モデルマウス脳内の神経細胞死に対するリソソーム制御因子Tfebの役割, 日本薬学会第137年回(仙台), 2017年3月.
190.	渡邊綾佑, 辻大輔, 田中裕大, 宇野マイケル新太郎, 伊藤孝司 : Tay-Sachs病患者iPS細胞由来神経細胞を用いた分子病態解析と治療薬の開発, 日本薬学会第137年回(仙台), 2017年3月.
191.	月本準, 辻大輔, 伊藤孝司 : ヒトノイラミニダーゼ4の発現と分子特性解析, 日本薬学会第137年回(仙台), 2017年3月.
192.	田中裕大, 辻大輔, 本窪田絢加, 山口沙恵香, 渡邊綾佑, 宇野マイケル新太郎, 杉崎圭, 辻大輔, 伊藤孝司 : リソソーム病におけるオートリソソーム形成異常メカニズムの解明, 日本薬学会第137年回(仙台), 2017年3月.
193.	日高朋, 西岡宗一郎, 月本準, 田中優希, 近藤まり, 小林功, 笠嶋めぐみ, 辻大輔, 瀬筒秀樹, 伊藤孝司 : トランスジェニックカイコ繭由来CTSAの有効性の検討, 日本薬学会第137年回(仙台), 2017年3月.
194.	藤見紀明, 杉原涼, 西辻和親, 坂下直実, 辻大輔, 伊藤孝司, 辻田麻紀, 奥平桂一郎 : ヒトアポA-I結合タンパク質AIBPのLPS誘導性マクロファージ炎症反応抑制効果, 日本薬学会第137年回(仙台), 2017年3月.
195.	津田雄介, 重永章, 辻耕平, 傳田将也, 佐藤浩平, 北風圭介, 中村太寛, 猪熊翼, 伊藤孝司, 大髙章 : タンパク質位置選択的修飾を指向したチオエステル調製法の開発, 第34回メディシナルケミストリーシンポジウム, 2016年12月.
196.	森崎巧也, 傳田将也, 辻大輔, 山本純, 猪熊翼, 伊藤孝司, 重永章, 大髙章 : SEAlideを基盤とした標的タンパク質精製ツールの開発研究, 第34回メディシナルケミストリーシンポジウム, 2016年12月.
197.	木村麻里安, 四宮槙子, 池啓伸, 齋藤朱里, 山﨑尚志, 伊藤孝司, 南川典昭, 滝口祥令 : カテプシンAスプライシング異常の修復を目指した改変U1 snRNA発現系の構築, 第55回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2016年11月.
198.	森崎巧也, 傳田将也, 山本純, 辻大輔, 猪熊翼, 伊藤孝司, 重永章, 大髙章 : Development of N-sulfanylethylanilide (SEAlide)-based traceable linker for enrichment and selective labeling of target proteins, 第53回ペプチド討論会, 2016年10月.
199.	伊藤孝司, 月本準, 東哲也, 辻大輔, 真板宣夫 : ヒトリソソーム性シアリダーゼ(NEU1)のin vivo結晶化と細胞応答及び応用, 第89日本生化学会大会フォーラム, 2016年9月.
200.	西岡宗一郎, 小林功, 原園景, 久保勇樹, 松崎祐二, 真板宣夫, 日高朋, 辻大輔, 瀬筒秀樹, 町井博明, 石井明子, 川崎ナナ, 伊藤孝司 : TGカイコ由来ヒトリソソーム酵素の糖鎖リモデリングと治療への応用, 第35回日本糖質学会年会, 2016年9月.
201.	伊藤孝司 : エンドグリコシダーゼを用いるネオグライコ酵素の創製とリソソーム病治療薬開発への応用, 第35回日本糖質学会年会, 2016年9月.
202.	山本憲二, 伊藤孝司 : エンドグリコシダーゼを用いるグライコエンジニアリングの進展と課題, 第35回日本糖質学会年会, 2016年9月.
203.	伊藤孝司 : 中枢神経症状を伴うライソゾーム病の治療法開発を目指して, 日本ムコ多糖症研究会・日本ムコ多糖症患者家族の会設立30周年記念合同シンポジウム, 2016年9月.
204.	幾尾真理子, 杉崎圭, 伊藤孝司 : 多発性骨髄腫によるExosome を介した骨分化抑制機構の発見と解析, 第8回日本RNAi研究会/3回日本細胞外小胞学会JSEV, 2016年9月. (キーワード) Exosomes / 多発性骨髄腫 / 骨分化
205.	古曳泰規, 傳田将也, 森崎巧也, 辻大輔, 猪熊翼, 伊藤孝司, 重永章, 大髙章 : ''SEAL-tag''を基盤とした細胞内での標的タンパク質ラベル化法の開発, 日本ケミカルバイオロジー学会第11回年会, 2016年6月.
206.	森崎巧也, 傳田将也, 辻大輔, 山本純, 猪熊翼, 伊藤孝司, 重永章, 大髙章 : 標的タンパク質精製ツール"SEAlide-based traceable linker"の開発, 日本ケミカルバイオロジー学会第11回年会, 2016年6月.
207.	水谷安通, 辻大輔, 渡邊綾佑, 山口沙恵香, 本窪田絢加, 田中裕大, 伊藤孝司 : Sandhoff病モデルマウスにおける神経細胞死に対するリソソーム制御因子Tfebの関与, 第57回日本生化学会中国・四国支部例会, 2016年5月.
208.	西岡宗一郎, 小林功, 原囿景, 久保勇樹, 松崎祐二, 真板宣夫, 日高朋, 辻大輔, 瀬筒秀樹, 町井博明, 石井明子, 川崎ナナ, 伊藤孝司 : TGカイコ由来ヒトリソソーム酵素の糖鎖リモデリングと治療への応用, 第57回日本生化学会中国・四国支部例会, 2016年5月.
209.	日高朋, 西岡宗一郎, 月本準, 近藤まり, 小林功, 笠嶋めぐみ, 辻大輔, 瀬筒秀樹, 伊藤孝司 : トランスジェニックカイコ由来ヒトカテプシンAの機能及び有効性の評価, 第57回日本生化学会中国・四国支部例会, 2016年5月.
210.	渡邊綾佑, 辻大輔, 山口沙恵香, 本窪田絢加, 水谷安通, 田中裕大, 伊藤孝司 : Tay-Sachs病患者iPS細胞由来神経病態モデル系における神経細胞死メカニズムの解明, 第57回日本生化学会中国・四国支部例会, 2016年5月.
211.	本窪田絢加, 辻大輔, 田中裕大, 山口沙恵香, 水谷安通, 渡邊綾佑, 伊藤孝司 : 蓄積する生体内基質の異なるリソソーム病患者由来細胞におけるオートリソソーム形成の比較解析, 第57回日本生化学会中国・四国支部例会, 2016年5月.
212.	木村麻里安, 池啓伸, 斎藤朱里, 山﨑尚志, 伊藤孝司, 南川典昭, 滝口祥令 : 塩基改変したU1 snRNAによるカテプシンAスプライス異常修復効果の検討, 第57回日本生化学会中国四国支部例会, 2016年5月.
213.	伊藤孝司 : 神経難病としての糖鎖蓄積症モデル系の構築と治療法開発への応用, 第57回日本生化学会中国・四国支部例会, 2016年5月.
214.	市野晨人, 奥平桂一郎, 川原遥華, 木村仁, 辻大輔, 西辻和親, 堂前純子, 道川誠, 坂下直実, 伊藤孝司, 斎藤博幸 : グリア細胞における ABCA7 発現制御機構の検討, 日本薬学会第136年会, 2016年3月.
215.	日高朋, 西岡宗一郎, 小林功, 近藤まり, 笠嶋めぐみ, 月本準, 辻大輔, 瀬筒秀樹, 伊藤孝司 : トランスジェニックカイコ絹糸腺由来ヒトカテプシンA の分子特性と生物機能評価, 日本薬学会第136年会(横浜), 2016年3月.
216.	水谷安通, 辻大輔, 山口沙恵香, 本窪田絢加, SPAMPANATO Carmine, BALLABIO Andrea, 伊藤孝司 : 神経症状を呈するリソソーム病モデルマウスにおけるオートファジーに関連した病態解析, 日本薬学会第136年会(横浜), 2016年3月.
217.	本窪田絢加, 辻大輔, 山口沙恵香, 水谷安通, 伊藤孝司 : リソソーム病におけるオートリソソームの形成異常, 日本薬学会第136年会(横浜), 2016年3月.
218.	辻大輔, 山口沙恵香, 本窪田絢加, 水谷安通, 伊藤孝司 : GM2 ガングリオシドーシス病患者由来iPS 細胞を用いた神経系病態モデルの構築及び病態シグナル解析, 日本薬学会第136年会(横浜), 2016年3月.
219.	池啓伸, 山﨑尚志, 金澤慶祐, 木村麻里安, 南川典昭, 辻大輔, 伊藤孝司 : 改変型U1 snRNAを用いたヒトカテプシンAの遺伝子発現におけるスプライシング異常の是正, 日本薬学会第136年会(横浜), 2016年3月.
220.	森崎巧也, 傳田将也, 中村太寛, 辻大輔, 山本純, 猪熊翼, 伊藤孝司, 重永章, 大髙章 : 標的タンパク質の高効率的同定を可能とする新規リンカー分子の開発研究, 日本薬学会第136年会, 2016年3月.
221.	水谷安通, 辻大輔, 山口沙恵香, 伊藤孝司 : リソソーム病モデルマウスにおけるオートファジーシグナル解析, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
222.	池啓伸, 山﨑尚志, 金澤慶祐, 木村麻里安, 南川典昭, 辻大輔, 伊藤孝司 : 改変型低分子RNAを用いたヒトカテプシンAの遺伝子発現におけるスプライシング異常の是正, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
223.	辻大輔, 本窪田絢加, 北風圭介, 山口沙恵香, 田崎智佳子, 伊藤孝司 : リソソーム病におけるオートリソソームの形成異常, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
224.	北風圭介, 水谷安通, 杉山栄二, 真板宣夫, 広川貴次, 瀬藤光利, 櫻庭均, 伊藤孝司 : 改変型ヒトβ- Hexosaminidase のGM2 蓄積症モデルに対する治療効果の評価, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
225.	山口沙恵香, 辻大輔, 難波健多郎, 伊藤孝司 : Tay-Sachs病患者由来iPS細胞を用いた中枢神経モデルの構築及び病態解析, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
226.	辻大輔, 水谷安通, 伊藤孝司 : リソソーム病におけるリソソーム制御因子TFEBの発現・局在解析, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
227.	木村麻里安, 金澤慶祐, 斎藤朱里, 山﨑尚志, 池啓伸, 伊藤孝司, 南川典昭, 滝口祥令 : 改変U1 snRNAを用いた変異カテプシンAスプライス異常の修復, BMB2015 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015年12月.
228.	金澤慶祐, 木村麻里安, 斎藤朱里, 山﨑尚志, 池啓伸, 伊藤孝司, 南川典昭, 滝口祥令 : 改変U1 snRNAを用いたヒトカテプシンAエクソンスキッピングの修復, 第54回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2015年10月.
229.	森崎巧也, 傳田将也, 辻大輔, 山本純, 折原賢祐, 猪熊翼, 伊藤孝司, 宍戸宏造, 重永章, 大髙章 : SEAlideを利用した標的タンパク質精製ツール ''トレーサブルリンカー''の開発研究, 第54回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2015年10月.
230.	森崎巧也, 傳田将也, 辻大輔, 山本純, 折原賢祐, 猪熊翼, 伊藤孝司, 宍戸宏造, 重永章, 大髙章 : 標的タンパク質の効率的精製および選択的ラベル化を可能とするケミカルツールの開発研究, 第三十一回若手化学者のための化学道場, 2015年8月.
231.	森崎巧也, 傳田将也, 辻大輔, 山本純, 折原賢裕, 猪熊翼, 伊藤孝司, 宍戸宏造, 重永章, 大髙章 : 標的タンパク質の高効率同定を可能とするケミカルツールの開発研究, 第47回若手ペプチド夏の勉強会, 2015年8月.
232.	津田雄介, 重永章, 辻耕平, 傳田将也, 佐藤浩平, 北風圭介, 中村太寛, 猪熊翼, 伊藤孝司, 大髙章 : タンパク質半化学合成を指向した配列特異的チオエステル化法の開発, 創薬懇話会2015 in 徳島, 2015年7月.
233.	伊藤孝司, 西岡宗一郎, 辻大輔, 東哲也, 真板宣夫, 小林功, 瀬筒秀樹, 湯本史明, 原囿景, 石井明子, 川崎ナナ : 新規組換えリソソーム酵素の創製とリソソーム病治療への応用, 第15回蛋白質科学会年会, 2015年6月.
234.	金澤慶佑, 山﨑尚志, 池啓伸, 伊藤孝司, 南川典昭, 滝口祥令 : 改変U1 snRNAによるヒトカテプシンAスプライス異常修復, 遺伝子・デリバリー研究会第15回シンポジウム, 2015年5月.
235.	伊藤孝司 : 組換えカイコを用いるネオグライコバイオロジクスの創製, 日本薬学会第135年会, 2015年3月.
236.	北風圭介, 田崎智佳子, 水谷安通, 杉山栄二, 神谷真子, 瀬藤光利, 浦野泰照, 伊藤孝司 : 改変型ヒトβ- Hexosaminidase のGM2 蓄積症モデルに対する治療効果の評価, 臨床遺伝子学公開シンポジウム2015, 2015年3月.
237.	伊藤孝司 : 糖タンパク医薬品の創製に向けた糖鎖改変技術, 第12回糖鎖科学コンソーシアムシンポジウム, 2014年12月.
238.	今滝泉, 辻大輔, 櫻庭均, 伊藤孝司 : Galactosialidosis 患者由来iPS 細胞の樹立と中枢神経系モデルの構築, 第53回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2014年11月.
239.	河野加菜子, 北風圭介, 辻大輔, 千葉靖典, 伊藤孝司 : メタノール資化性酵母株発現系による組換えマンノース6- リン酸受容体の生産・精製と機能検討, 第53回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2014年11月.
240.	津田雄介, 重永章, 傳田将也, 佐藤浩平, 北風圭介, 中村太寛, 猪熊翼, 伊藤孝司, 大髙章 : 新規タンパク質チオエステル調製法の開発, 第53回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2014年11月.
241.	田中翔子, 金澤慶祐, 山﨑尚志, 池啓伸, 伊藤孝司, 南川典昭, 滝口祥令 : 改変U1 snRNAによるヒトカテプシンAスプライス異常修復の試み, 第53回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2014年11月.
242.	北風圭介, 田崎智佳子, 水谷安通, 杉山栄二, 神谷真子, 瀬藤光利, 浦野泰照, 伊藤孝司 : 改変型ヒトβ- Hexosaminidase のGM2 蓄積症モデルに対する治療効果の評価, 第5回グライコバイオロジクス研究会, 2014年11月.
243.	西岡宗一郎, 小林功, 辻大輔, 原囿景, 久保勇樹, 真板宣夫, 池戸駿介, 東哲也, 辻大輔, 瀬筒秀樹, 町井博明, 石井明子, 川崎ナナ, 伊藤孝司 : 組換えカイコ由来ヒトリソソーム酵素の分子特性とグライコシンターゼによる in vitro 糖鎖修飾, 第5回グライコバイオロジクス研究会, 2014年11月.
244.	Yusuke Tsuda, Akira Shigenaga, Masaya Denda, Kohei Sato, Keisuke Kitakaze, Takahiro Nakamura, Tsubasa Inokuma, Kouji Itou and Akira Otaka : Preparation of Peptide/protein Thioesters Using a Chemical Protocol Applicable to Expressed Proteins., 51th The Japanese Peptide Society, Oct. 2014.
245.	Kohei Sato, Keisuke Kitakaze, Ken Sakamoto, Akira Shigenaga, Tsubasa Inokuma, Daisuke Tsuji, Kouji Itou and Akira Otaka : Development of N-glycosylated asparagine ligation and its application to total chemical synthesis of GM2 activator protein, 51th The Japanese Peptide Society, Oct. 2014.
246.	水谷安通, 北風圭介, 田崎智佳子, 伊藤孝司, 櫻庭均, 伊藤孝司 : 改変型ヒトβ-ヘキソサミニダーゼの分子特性解析とGM2蓄積症モデル細胞への補充効果, 第87回日本生化学会大会, 2014年10月.
247.	池啓伸, 山﨑尚志, 田中翔子, 金澤慶祐, 滝口祥令, 南川典昭, 伊藤孝司 : 改変U1 snRNAによるヒトカテプシンAの遺伝子発現におけるスプライシング異常の修復, 第87回日本生化学会, 2014年10月.
248.	今滝泉, 辻大輔, 櫻庭均, 伊藤孝司 : Galactosialidosis患者由来iPS細胞の樹立及び中枢神経系細胞への分化誘導, 第87回日本生化学会大会, 2014年10月.
249.	西岡宗一郎, 小林功, 辻大輔, 原囿景, 久保勇樹, 真板宣夫, 池戸駿介, 東哲也, 辻大輔, 瀬筒秀樹, 町井博明, 石井明子, 川崎ナナ, 伊藤孝司 : トランスジェニックカイコ由来ヒトリソソーム酵素の分子特性解析とグライコシンターゼによる糖鎖修飾, 第87回日本生化学会大会, 2014年10月.
250.	北風圭介, 田崎智佳子, 水谷安通, 杉山栄二, 神谷真子, 瀬藤光利, 浦野泰照, 伊藤孝司 : GM2蓄積症モデルマウスに対する改変型ヒトβーヘキソサミニダーゼの有効性評価, 第87回日本生化学会大会, 2014年10月.
251.	河野加菜子, 辻大輔, 千葉靖典, 伊藤孝司 : メタノール資化性酵母株発現系によるマンノース6-リン酸受容体の生産・精製と機能検討, 第87回日本生化学会大会, 2014年10月.
252.	北風圭介, 田崎智佳子, 水谷安通, 杉山栄二, 神谷真子, 瀬藤光利, 浦野泰照, 伊藤孝司 : 改変型ヒトβ-HexosaminidaseのGM2蓄積症モデルに対する有効性評価, 第13回若手ファーマ・バイオフォーラム2014, 2014年9月.
253.	北風圭介, 田崎智佳子, 水谷安通, 杉山栄二, 神谷真子, 瀬藤光利, 浦野泰照, 伊藤孝司 : GM2蓄積症モデルに対する改変型ヒトβーヘキソサミニダーゼの有効性と機能評価, 第33回日本糖質学会年会, 2014年8月.
254.	西岡宗一郎, 小林功, 辻大輔, 原囿景, 久保勇樹, 真板宣夫, 池戸駿介, 東哲也, 辻大輔, 瀬筒秀樹, 町井博明, 石井明子, 川崎ナナ, 伊藤孝司 : 組み換えカイコ絹糸腺由来ヒトカテプシンAの分子特性とエンドグリコシダーゼによる糖鎖改変, 第33回日本糖質学会年会, 2014年8月.
255.	津田雄介, 重永章, 佐藤浩平, 中村太寛, 北風圭介, 猪熊翼, 伊藤孝司, 大髙章 : 天然アミノ酸配列に適用可能な新規タンパク質チオエステル合成法の開発, 日本ケミカルバイオロジー学会第9回年会, 2014年6月.
256.	西岡宗一郎, 小林功, 辻大輔, 原囿景, 久保勇樹, 真板宣夫, 池戸駿介, 東哲也, 辻大輔, 瀬筒秀樹, 町井博明, 石井明子, 川崎ナナ, 伊藤孝司 : トランスジェニックカイコ由来ヒトリソソーム酵素の分子特性解析と化学酵素法に基づく人工糖鎖修飾, 第55回日本生化学会中国・四国支部例会, 2014年6月.
257.	北風圭介, 田崎智佳子, 水谷安通, 神谷真子, 浦野泰照, 伊藤孝司 : GM2蓄積症の新規治療薬開発を目指した機能改変型ヒトβーヘキソサミニダーゼの作製と評価, 第55回日本生化学会中国・四国支部例会, 2014年6月.
258.	山﨑尚志, 田中翔子, 金澤慶祐, 伊藤孝司, 南川典昭, 滝口祥令 : 改変U1snRNAによるヒトカテプシンAスプライス異常修復の試み, 第55回日本生化学会中国・四国支部例会, 2014年6月.
259.	伊藤孝司 : 中枢神経変性を伴うリソソーム病に対する脳指向性治療薬と新規評価系の開発, Biotech2014, 2014年5月.
260.	伊藤孝司 : リソソーム病に対するiPS創薬を目指して, --- 神経難病患者由来iPS細胞の病態解明・治療法開発への応用 ---, 京都大学iPS細胞研究所井上治久研究室セミナー, 2014年5月.
261.	佐藤浩平, 北風圭介, 坂本健, 重永章, 辻大輔, 伊藤孝司, 大髙章 : GM2活性化タンパク質の収束的合成研究, 日本薬学会第134年会, 2014年3月.
262.	津田雄介, 重永章, 佐藤浩平, 中村太寛, 北風圭介, 猪熊翼, 伊藤孝司, 大髙章 : 発現タンパク質に適用可能な新規タンパク質チオエステル合成法の開発, 日本薬学会第134年会, 2014年3月.
263.	北風圭介, 幾尾真理子, 杉山栄二, 浅沼大祐, 神谷真子, 瀬藤光利, 浦野泰照, 櫻庭均, 伊藤孝司 : 新規蛍光プローブおよびイメージングマススペクトロメトリーによるリソソーム酵素補充効果のイメージング, 日本薬学会第134年会, 2014年3月.
264.	伊藤孝司 : 改変型β-ヘキソサミニダーゼの開発と機能評価, 臨床遺伝学公開シンポジウム2014, 2014年3月.
265.	伊藤孝司 : ネオバイオメディシンの創製と医薬品開発への応用, 平成25年度革新的特色研究公開シンポジウム徳大薬学部創薬生命工学シーズの整備と蔵本ネットワークを基盤としたアカデミア創薬研究, 2014年3月.
266.	伊藤孝司 : リソソーム病患者iPS細胞からの神経系細胞の分化誘導と治療薬開発への応用, 大阪大学微生物病研究所セミナー, 2014年3月.
267.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : テイーサック病の新規治療薬開発を目指した機能改変型ヒトβーヘキソサミニダーゼの精製および評価, 第55回日本先天代謝異常学会, 2013年11月.
268.	東哲也, LM Chavas, F-X Gallat, 伊藤孝司 : Neuraminidase-1(NEU1)のin cell 結晶化と分子特性解析, 第35回生体膜と薬物の相互作用シンポジウム, 2013年11月.
269.	伊藤孝司 : ネオバイオロジクスの創製とリソソーム病治療薬開発へのアプローチ, 第5回全国共同利用・共同開発「酵素学研究拠点」シンポジウム, 2013年11月.
270.	西岡宗一郎, 小林功, 辻大輔, 池戸駿介, Md.RAHMAN Motiur, 東哲也, 真板宣夫, 瀬筒秀樹, 町井博明, 原園景, 石井明子, 川崎ナナ, 伊藤孝司 : リソソーム病治療薬候補としてのトランスジェニックカイコ絹糸腺由来組換えヒトカテプシンAの機能解析と分子装飾, 第4回グライコバイオロジクス研究会プログラム, 2013年11月.
271.	伊藤孝司 : 希少疾患に対するiPS細胞の実現を目指して, --- 神経難病患者由来iPS細胞を利用する治療薬開発へのアプローチ ---, 第10回HBS公開シンポジウム再生医学研究の現状と臨床応用への課題, 2013年11月.
272.	河野加菜子, 辻大輔, 伊藤孝司 : メタノール資化性酵母発現系を用いた組換えマンノース6リン酸受容体の精製とその応用, 第52回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2013年10月.
273.	今滝泉, 辻大輔, 伊藤孝司 : カテプシンA欠損患者由来iPS細胞の樹立と神経系への分化誘導, 第52回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, 2013年10月.
274.	佐藤浩平, 北風圭介, 坂本健, 重永章, 辻大輔, 伊藤孝司, 大髙章 : リソソーム病治療を指向したGM2活性化タンパク質アナログの完全化学合成, 生命分子機能研究会2013学術集会, 2013年9月.
275.	北風圭介, 野加菜子, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : テイーサック病の新規治療薬開発を目指した機能改変型ヒトβーヘキソサミニダーゼの精製および評価, 第12回次世代を担う若手ファーマ・バイオフォーラム2013, 2013年9月.
276.	山口沙恵香, 辻大輔, 難波健多郎, 今滝泉, 伊藤孝司 : Tay-Sachs病患者由来iPS細胞を用いた中枢神経モデルの構築, 第54回日本生化学会大会, 2013年9月.
277.	幾尾真理子, 齋藤裕樹, 大前陽輔, 毛瀚, 長野源太郎, 藤幸知子, 沼田俊介, 韓笑, 小幡佳津明, 長谷川節雄, 山口博樹, 猪口孝一, 伊藤輝代, 平松啓一, 伊藤孝司, 関水和久, 垣内力 : 新規機能性RNA psm-mecはagrA遺伝子の翻訳を抑制してメチシリン耐性黄色ブドウ球菌の病原性を抑制する, 第86回日本生化学会, 2013年9月.
278.	小川隆, 辻大輔, 伊藤孝司 : GM2ガングリオシド蓄積症モデルマウス由来単球系細胞におけるアクチン重合系と浸潤性の変動, 第86回日本生化学会大会, 2013年9月.
279.	Motiur Md Rahman, Hirokawa Takatsugu, Daisuke Tsuji, Hitaoka Seiji, Tatsusada Yoshida, Hiroshi Chuman and Kouji Itou : In vitro inhibitory and stabilizing effects of siastatin B toward human cytosolic sialidase 2 (NEU2), 第86回日本生化学会大会, Sep. 2013.
280.	西岡宗一郎, 小林功, 辻大輔, 池戸駿介, Md.RAHMAN Motiur, 東哲也, 真板宣夫, 瀬筒秀樹, 町井博明, 原園景, 石井明子, 川崎ナナ, 伊藤孝司 : ガラクシアリドーシス治療薬候補としてのトランスジェニックカイコ由来ヒトカテプシンAの解析, 第86回日本生化学会, 2013年9月.
281.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : テイーサック病の新規治療薬開発を目指した機能改変型ヒトβーヘキソサミニダーゼの精製および評価, 第86回日本生化学会大会, 2013年9月.
282.	北風圭介, 河野加菜子, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : テイーサック病の治療薬開発を目指した機能改変型ヒトβーヘキソサミニダーゼの精製及び評価, 第32回日本糖質学会大会, 2013年8月.
283.	伊藤孝司, 小林巧, 西岡宗一郎, 原園景, 久保勇樹, 真板宣夫, 辻大輔, Md Motiiur RAHMAN, 池戸駿介, 石井明子, 川崎ナナ, 町井博明, 瀬筒秀樹 : バイオ医薬品の生産基材としてのトランスジェニックカイコとネオグライコバイオロジクス創製への応用, 第32回日本糖質学会大会, 2013年8月.
284.	坂本健, 佐藤浩平, 重永章, 辻大輔, 伊藤孝司, 大髙章 : SEAlideユニットの効率的合成法の開発とその応用, 第45回若手ペプチド夏の勉強会, 2013年7月.
285.	山口沙恵香, 辻大輔, 難波健多郎, 今滝泉, 伊藤孝司 : Tay-Sachs病患者由来iPS細胞を用いた中枢神経モデルの構築, 第54回日本生化学会中国・四国支部例会, 2013年5月.
286.	東哲也, LM Chavas, 辻大輔, 伊藤孝司 : リソソーム性Neuraminidase-1(NEU1)のin cell結晶化, 第54回日本生化学会中国・四国支部例会, 2013年5月.
287.	Motiur Md Rahman, Hirokawa Takatsugu, Daisuke Tsuji, Hitaoka Seiji, Tatsusada Yoshida, Hiroshi Chuman and Kouji Itou : In vitro inhibitory and stabilizing effects of siastatin B toward human cytosolic sialidase 2 (NEU2), 第54回日本生化学会中国・四国支部例会, May 2013.
288.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : テイーサック病の新規治療薬開発を目指した機能改変型ヒトβーヘキソサミニダーゼの精製および評価, 第54回日本生化学会中国・四国支部例会, 2013年5月.
289.	西岡宗一郎, 小林功, 辻大輔, 池戸駿介, Md.RAHMAN Motiur, 東哲也, 真板宣夫, 瀬筒秀樹, 町井博明, 原園景, 石井明子, 川崎ナナ, 伊藤孝司 : ガラクシアリドーシス治療薬候補としてのトランスジェニックカイコ由来ヒトカテプシンAの解析, 第54回日本生化学会中国・四国支部例会, 2013年5月.
290.	関水和久, 伊藤孝司 : カイコを用いた新規医薬品と評価システムの開発, 日本薬学会第133年会一般シンポジウム, 2013年3月.
291.	伊藤孝司 : カイコを用いた新規医薬品と評価システムの開発, --- -トランスジェニックカイコを用いたリソソーム病治療薬の開発- ---, 日本薬学会第133年会, 2013年3月.
292.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : 酵素の分子構造改変に基づくTay-Sachs病治療薬の開発, 日本薬学会第133年会, 2013年3月.
293.	折原賢祐, 小林久剛, 兼松誠, 吉田昌裕, 中村崇洋, 辻大輔, 伊藤孝司, 重永章, 大髙章, 宍戸宏造 : Aspergillide Cの活性評価および標的タンパクの探索, 日本薬学会第133年会, 2013年3月.
294.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : CHO細胞による改変型リソソーム酵素の発現・精製と機能評価システムの開発, 平成24年度第5回先導技術交流会, 2013年1月.
295.	西岡宗一郎, 小林巧, 辻大輔, 池戸駿介, Md.RAHMAN Motiur, 東哲也, 真板宣夫, 瀬筒秀樹, 町井博明, 原園景, 石井明子, 川崎ナナ, 伊藤孝司 : リソソーム病治療への応用を目指したTGカイコ由来組換えヒトカテプシンAの分子特性評価, 第85回日本生化学会大会, 2012年12月.
296.	小川隆, 辻大輔, 伊藤孝司 : Sondhoff病モデルマウス由来単級系細胞内Actin重合関連タンパクの発現と運動性及び浸潤性との相関, 第85回日本生化学会大会, 2012年12月.
297.	難波建多郎, 辻大輔, 櫻庭均, 伊藤孝司 : Tay-Sachs病患者由来iPS細胞の樹立と中枢神経系モデルの構築, 第85回日本生化学会大会, 2012年12月.
298.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : 酵素の分子構造改変に基づくTay-Sachs病治療薬の開発, 第85回日本生化学会大会, 2012年12月.
299.	中村崇洋, 辻大輔, 伊藤孝司 : 多発性骨髄腫細胞株の薬剤抵抗性に関与するプロテオームの解析, 第85回日本生化学会大会, 2012年12月.
300.	佐藤浩平, 北風圭介, 坂本健, 重永章, 辻大輔, 伊藤孝司, 大髙章 : リソソーム病治療薬を指向したヒトGM2活性化タンパク質誘導体の化学合成と活性評価, 第30回メディシナルケミストリーシンポジウム, 2012年11月.
301.	辻大輔, 難波建多郎, 石丸直澄, 櫻庭均, 伊藤孝司 : Tay-Sachs病患者由来iPS細胞の樹立と分化神経系細胞に対する酵素補充効果の検討, 第54回日本先天代謝異常学会総会/第11回アジア先天代謝異常症シンポジウム, 2012年11月.
302.	北風圭介, 辻大輔, 浅沼大祐, 神谷真子, 浦野泰照, 櫻庭均, 伊藤孝司 : 新規人工蛍光基質を用いたリソソーム酵素の脳内補充効果のin vivoイメージング, 第54回日本先天異常学会総会/第11回アジア先天代謝異常症シンポジウム, 2012年11月.
303.	Kohei Sato, Keisuke Kitakaze, Ken Sakamoto, Akira Shigenaga, Daisuke Tsuji, Kouji Itou and Akira Otaka : Convergent chemical synthesis of human GM2 activator protein analog using SEAlide chemistry, 第49回ペプチド討論会, Nov. 2012.
304.	辻大輔, 北風圭介, 難波建多朗, 浅沼大祐, 神谷真子, 浦野泰照, 伊藤孝司 : 新規人工蛍光基質を用いた活性染色によるリソソーム酵素の脳内補充効果のin vivoイメージング, 第31回日本糖質学会年会, 2012年9月.
305.	西岡宗一郎, 小林巧, 辻大輔, 池戸駿介, Md.RAHMAN Motiur, 東哲也, 真板宣夫, 瀬筒秀樹, 町井博明, 原園景, 石井明子, 川崎ナナ, 伊藤孝司 : TG カイコを用いた組み換えヒトカテプシン A の分子特性とリソソーム病治療薬開発, 第31回日本糖質学会年会, 2012年9月.
306.	佐藤浩平, 北風圭介, 坂本健, 重永章, 辻大輔, 伊藤孝司, 大髙章 : タンパク質完全化学合成∼ケミストによるタンパク質医薬品開発を目指して∼, 第44回若手ペプチド夏の勉強会, 2012年8月.
307.	Motiur Md Rahman, Kitao Satoshi, Daisuke Tsuji, Matsuzawa Fumiko, Aikawa Sei-ichi and Kouji Itou : Inhibitory efects and specificity of synthetic sialyldendrimers on recomninant human neuraminidase 2(NEU2), 第52回日本生化学会中国・四国支部総会, May 2012.
308.	西岡宗一郎, 小林巧, 辻大輔, 北尾聡, Md.RAHMAN Motiur, 池戸駿介, 真板宣夫, 瀬筒秀樹, 町井博明, 伊藤孝司 : トランスジェニックカイコを用いた組み換えヒトカテプシンA発現の分子特性解析とリソソーム病治療薬開発, 第52回日本生化学会中国・四国支部総会, 2012年5月.
309.	辻大輔, 難波建多郎, 南條遥, 伊藤孝司 : リソソーム病に対するex vivo遺伝子治療法の開発, 第53回日本生化学会中国・四国支部例会, 2012年5月.
310.	小川隆, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウス由来単球系細胞におけるActin重合発現解析, 第53回日本生化学会中国・四国支部例会, 2012年5月.
311.	辻大輔, 難波建多郎, 浅沼大祐, 神谷真子, 浦野泰照, 伊藤孝司 : GM2 ガングリオシドーシス対する間葉系幹細胞を用いたex vivo遺伝子治療法によるクロスコレクション効果の検討, 日本薬学会第132年会(札幌), 2012年3月.
312.	伊藤孝司, 西岡宗一郎, 小林巧, 真板宣夫, 辻大輔, 北尾聡, Md.RAHMAN Motiur, 池戸駿介, 瀬筒秀樹, 町井博明 : ヒトカテプシンA発現トランスジェニックカイコ作製とリソソーム病治療薬開発への応用, 日本薬学会第132年会, 2012年3月.
313.	小川隆, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウスにおける単球系細胞の脳内浸潤機構の解析, 日本薬学会第132年会(札幌), 2012年3月.
314.	辻大輔, 伊藤孝司 : 化合物ライブラリーを用いた新規神経前駆細胞誘導剤の探索, IN Cell Users Day 2011, 2011年12月.
315.	比多岡清司, 的場弘, 原田政隆, 河野明大, 坂本修平, 岡田耕平, 吉田達貞, 辻大輔, 広川貴次, 伊藤孝司, 中馬寛 : Why does tamiflu have a branched alkoxy side chain?, 第39回構造活性相関シンポジウム, 39-40, 2011年11月.
316.	比多岡清司, 的場弘, 原田政隆, 河野明大, 坂本修平, 岡田耕平, 吉田達貞, 辻大輔, 広川貴次, 伊藤孝司, 中馬寛 : ヒトノイラミニダーゼ-シアル酸誘導体複合体相互作用の非経験的フラグメント分子軌道法計算に基づく相関解析 (LERE-QSAR), 第39回構造活性相関シンポジウム, 15-16, 2011年11月.
317.	Hiroshi Matoba, Seiji Hitaoka, Masataka Harada, Akihiro Kawano, Syuhei Sakamoto, Kohei Okada, Tatsusada Yoshida, Hiroshi Chuman, Daisuke Tsuji, Takatsugu Hirokawa, Kouji Itou and Hiroshi Chuman : Difference in Sensitivity of Antiinfluenza Drugs between Human and Influenza Neuraminidases, CBI(情報計算化学生物学会)/JSBi(日本バイオインフォマティクス学会)2011合同大会, Nov. 2011.
318.	北風圭介, 堂園幸恵, 辻大輔, 櫻庭均, 田島陽一, 伊藤孝司 : ヒトβ-hexosaminidaseとGM2 activator proteinとの相互作用の解析, 第84回日本生化学会大会, 2011年9月.
319.	難波建多郎, 辻大輔, 南條遥, 伊藤孝司 : 間葉系幹細胞に対する新規神経分化誘導法の開発とリソソーム病の細胞治療への可能性, 第84回日本生化学会大会, 2011年9月.
320.	辻大輔, 小川隆, 豊島優裕, 伊藤孝司 : GM2ガングリオシドーシス脳内におけるミクログリア及び浸潤単球系細胞の性質解析, 第84回日本生化学会大会, 2011年9月.
321.	堂園幸恵, 辻大輔, 松岡和彦, 北風圭介, 櫻庭均, 伊藤孝司 : 改変型ヒトβ-HexosaminidaseBの高発現CHO細胞株の樹立と無血清大量培養系の構築, 第84回日本生化学会大会, 2011年9月.
322.	岡野和真, 辻大輔, 中村崇洋, 土屋浩一郎, 伊藤孝司 : ヒト多発性骨髄腫細胞株におけるSide Population細胞の性質解析, 第84回日本生化学会大会, 2011年9月.
323.	中村崇洋, 辻大輔, 岡野和真, 伊藤孝司 : 様々ながん細胞株の薬剤抵抗性に関与するタンパクのプロテオーム解析, 第84回日本生化学会大会, 2011年9月.
324.	西岡宗一郎, 辻大輔, 北尾聡, Md. Motiur Rahman, 池戸駿介, 小林功, 瀬筒秀樹, 田村俊樹, 町井博明, 真板宣夫, 伊藤孝司 : トランスジェニックカイコ中部絹糸腺由来ヒト保護タンパク質/カテプシンAの生化学的解析, 第84回日本生化学会大会, 2011年9月.
325.	伊藤孝司, 西岡宗一郎, 小林功, 中北慎一, 辻大輔, 北尾聡, Md. Motiur Rahman, 池戸駿介, 瀬筒秀樹, 田村俊樹, 平林淳, 町井博明 : トランスジェニックカイコを用いたヒトカテプシンAの発現・精製・応用, 第30回日本糖質学会年会, 2011年7月.
326.	辻大輔, 難波建多郎, 南條遥, 伊藤孝司 : MSCsを用いたGM2ガングリオシドーシス対するex vivo遺伝子治療法の開発, 第30回日本糖質学会年会, 2011年7月.
327.	西岡宗一郎, Md. Motiur Rahman, 北尾聡, 池戸駿介, 辻大輔, 小林功, 瀬筒秀樹, 田村俊樹, 町井博明, 伊藤孝司 : トランスジェニックカイコ由来ヒト保護タンパク質/カテプシンAの精製と性質解析, 第52回日本生化学会中国・四国支部総会, 2011年5月.
328.	辻大輔, 豊島優裕, 伊藤孝司 : GM2 ガングリオシドーシスモデル由来ミクログリアにおける形態制御機構の解明, 第52回日本生化学会中国・四国支部総会, 2011年5月.
329.	北風圭介, 松岡和彦, 辻大輔, 櫻庭均, 田島陽一, 伊藤孝司 : 大腸菌発現系によるヒトGM2 activator protein の獲得およびヒトβ-Hexosaminidaseとの相互作用の解析, 第52回日本生化学会中国・四国支部総会, 2011年5月.
330.	中村崇洋, 岡野和真, 辻大輔, 伊藤孝司 : 多発性骨髄腫細胞株RPMI8226に対する薬剤耐性に関与するプロテオーム解析, 第52回日本生化学会中国・四国支部総会, 2011年5月.
331.	難波建多郎, 辻大輔, 金城奈美, 中尾允泰, 佐野茂樹, 伊藤孝司 : 未分化細胞に対する新規分化誘導剤の探索, 第52回日本生化学会中国・四国支部総会, 2011年5月.
332.	辻大輔, 難波建多郎, 浦上裕行, 辻耕平, 重永章, 大髙章, 柏田良樹, 高石喜久, 伊藤孝司 : ヒトiPS細胞に対する神経分化誘導能を持つ新規化合物の探索, 日本薬学会第131年会, 2011年3月.
333.	桑原淳, 北村明香, 伊藤孝司 : 転写因子Sp1 の zinc fingerに基づく核輸送蛋白質相互作用, 日本薬学会第131年会, 2011年3月.
334.	黒田麻祐子, 鈴木俊宏, 小谷政晴, 田島陽一, 川島育夫, 兎川忠靖, 辻大輔, 伊藤孝司, 千葉靖典, 福重智子, 金蔵拓郎, 櫻庭均 : Sandhoff 病モデルマウス由来ニューロスフェアにおけるヒト組み換えHex A 酵素の取り込み, 日本薬学会第131年会, 2011年3月.
335.	児玉敬, 兎川忠靖, 川島育夫, 石田洋一, 鈴木實, 辻大輔, 伊藤孝司, 千葉靖典, 月村考宏, 鈴木俊宏, 櫻庭均 : リゾ-GM2ガングリオシド:GM2ガングリオシドーシスのバイオマーカー, 日本薬学会第131年会, 2011年3月.
336.	北風圭介, 松岡和彦, 辻大輔, 櫻庭均, 田島陽一, 伊藤孝司 : 大腸菌発現系によるヒトGM2 activator proteinの獲得およびヒトbeta-Hexosaminidaseとの相互作用の解析, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
337.	北尾聡, Motiur MD. Rahman, 辻大輔, 伊藤孝司 : Origami B株を用いたヒトNeuraminidase-2の獲得とその機能評価, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
338.	黒田麻祐子, 鈴木俊宏, 小谷政晴, 田島陽一, 川島育夫, 兎川忠靖, 辻大輔, 伊藤孝司, 千葉靖典, 福重智子, 金蔵拓郎, 櫻庭均 : Sandhoff病モデルマウス由来ニューロスフェア株を用いた酵素補充モデルの構築, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
339.	徳田美幸, 辻大輔, 吉良太孝, 中村崇洋, 岡野和真, 南川典昭, 伊藤孝司 : 新規抗がん剤候補化合物探索を目指した構造活性相関研究, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
340.	南條遥, 辻大輔, 松岡和彦, 櫻庭均, 伊藤孝司 : Sandhoff病に対する ex vivo 遺伝子治療モデルの開発, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
341.	松岡和彦, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウスにおける血中グルココルチコイドの上昇と胸腺の萎縮, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
342.	辻大輔, 難波建多郎, 浦上裕行, 重永章, 大髙章, 柏田良樹, 高石喜久, 伊藤孝司 : 未分化細胞に対する神経分化誘導作用を持つ化合物の探索と構造活性相関, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
343.	豊島優裕, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウス由来ミクログリアの形態制御機構, BMB2010(第33回日本分子生物学会年会・第83回日本生化学会大会合同大会), 2010年12月.
344.	郡恵理, 比多岡清司, 原田政隆, 的場弘, 北尾聡, Motiur Md. Rahman, 吉田達貞, 門田佳人, 辻大輔, 広川貴次, 伊藤孝司, 中馬寛 : ヒトCathepsinA活性に対するArg344置換の影響に関する実験および分子科学計算に基づく解析, 第38回構造活性相関シンポジウム, 78-79, 2010年10月.
345.	原田政隆, 比多岡清司, 郡恵理, 的場弘, 北尾聡, Motiur Md.Rahman, 吉田達貞, 辻大輔, 広川貴次, 伊藤孝司, 中馬寛 : 分子モデリング・分子科学計算に基づくヒトノイラミニダーゼの構造-機能解析, 第38回構造活性相関シンポジウム, 70-71, 2010年10月.
346.	三好圭子, 辻大輔, 工藤景子, 里村一人, 武藤太郎, 伊藤孝司, 野間隆文 : ヒト口腔粘膜由来iPS細胞の樹立とその意義, 第52回歯科基礎医学会学術大会ならびに総会, 2010年9月.
347.	Daisuke Tsuji, Masahiro Toyoshima and Kouji Itou : Abnormal functions of hematopoietic cells in Sandhoff disease model mice, The 28th NAITO CONFERENCE ON Glycan Expression and Regulation, Jul. 2010.
348.	Kazuhiko Matsuoka, Tomomi Tamura, Yukie Dohzono, Keisuke Kitakaze, Daisuke Tsuji, Hitoshi Sakuraba and Kouji Itou : Development of Modified Human beta-Hexosaminidase B for Enzyme Replacement Therapy for Tay-Sachs Disease, The 28th NAITO CONFERENCE ON Glycan Expression and Regulation, Jul. 2010.
349.	豊島優裕, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウス由来ミクログリアの形態制御機構, 第51回日本生化学会中国・四国支部例会, 2010年5月.
350.	辻大輔, 小山毅, 浦上裕行, 難波建多郎, 柏田良樹, 高石喜久, 伊藤孝司 : ヒガンバナ科植物由来アルカロイドLycorineの神経分化誘導作用, 第51回日本生化学会中国・四国支部例会, 2010年5月.
351.	堀川靖, 北尾聡, Motiur Md Rahman, 辻大輔, 小林功, 瀬筒秀樹, 町井博明, 田村俊樹, 中北愼一, 平林淳, 伊藤孝司 : トランスジェニックカイコによる組換えヒトカテプシンAの生産と欠損症患者由来培養細胞への補充効果, 第51回日本生化学会中国・四国支部例会, 2010年5月.
352.	福石信之, 栗原大輔, 幡洋輔, 濱野裕章, 松井敦聡, 伊藤孝司, 辻大輔, 赤木正明 : マスト細胞の分化および成熟におけるβ-ヘキソサミニダーゼの役割, 日本薬学会第130年会, 2010年3月.
353.	伊藤孝司 : 神経症状を伴うリソソーム病モデルに対する改変型組換えヒト酵素の脳室内補充効果, 日本薬学会第130年会, 2010年3月.
354.	伊藤孝司 : リソソーム病に対する「ウルトラ・オーファンドラッグ」開発研究の展開, 日本薬学会第130年会シンポジウム, 2010年3月.
355.	黒田麻祐子, 鈴木俊宏, 小谷政晴, 田島陽一, 川島育夫, 兎川忠靖, 菅原佳奈子, 辻大輔, 伊藤孝司, 千葉靖典, 福重智子, 金蔵拓郎, 櫻庭均 : Sandhoff病の病態解析を目的としたSandhoff病モデルマウス由来ニューロスフェア株の樹立, 日本薬学会第130年会, 2010年3月.
356.	辻大輔, 岡野和真, 徳田美幸, 伊藤良和, 中村崇洋, 伊藤孝司 : ヒト多発性骨髄腫細胞株におけるメルファラン抵抗性細胞の性質解析, 日本薬学会第130年会, 2010年3月.
357.	Eri Kori, Seiji Hitaoka, Masataka Harada, Yoshito Kadota, Yasushi Horikawa, Tatsusada Yoshida, Kouji Itou and Hiroshi Chuman : Expression and Molecular Dynamics Studies on Effect of Amino Acid Substitutions at Arg344 in Human Cathepsin A, 第37回構造活性相関シンポジウム, Nov. 2009.
358.	辻大輔, 尾崎修治, 池亀彰茂, 伊藤良和, 徳田美幸, 岡野和真, 安倍正博, 松本俊夫, 伊藤孝司 : ヒト多発性骨髄腫由来ガン幹細胞の単離及び性質決定, 第82回日本生化学会大会, 2009年10月.
359.	堀川靖, 辻大輔, 佐野詩織, 中瀬生彦, 二木史朗, 伊藤孝司 : Cell penetrathing peptideを用いたリソソーム性保護タンパク質/カテプシンAの細胞内補充効果の解析, 第82回日本生化学会大会, 2009年10月.
360.	伊藤良和, 吉村好之, 湊拓也, 山村陽子, 沖津宏, 伊藤孝司 : 胃癌マーカー候補としてのヒト血漿Haptoglobinの生化学的解析, 第82回日本生化学会大会, 2009年10月.
361.	田村友美, 松岡和彦, 辻大輔, 櫻庭均, 伊藤孝司 : 遺伝子改変型ヒトβ-Hexosaminidase B の発現とGM2ガングリオシドーシス培養細胞に対する補充効果, 第82回日本生化学会大会, 2009年10月.
362.	豊島優裕, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウス由来Microglia細胞株の形態を制御するシグナリング解析, 第82回日本生化学会大会, 2009年10月.
363.	南條遥, 辻大輔, 伊藤孝司 : 骨髄ストローマ細胞を用いたGM2ガングリオシドーシスに対するex vivo遺伝子治療の開発, 第82回日本生化学会大会, 2009年10月.
364.	松岡和彦, 田村友美, 辻大輔, 櫻庭均, 伊藤孝司 : ヒトβ-Hexosaminidase B の機能改変とGM2ガングリオシド蓄積症モデルマウス脳室内への補充効果, 第82回日本生化学会大会, 2009年10月.
365.	堀川靖, 辻大輔, 二木史朗, 伊藤孝司 : Cell penetrathing peptideを用いたリソソーム性保護タンパク質/カテプシンAの細胞内補充効果の解析, 第29回日本糖質学会年会, 2009年9月.
366.	川島永子, 辻大輔, 奥田徹哉, 伊藤孝司, 仲山賢一 : GM2ガングリオシドーシス由来アストロサイトの異常増殖メカニズムの解明, 第29回日本糖質学会年会, 2009年9月.
367.	伊藤孝司, 辻大輔, 松岡和彦, 田村友美, 千葉靖典, 地神芳文, 川島育夫, 田島陽一, 櫻庭均 : GM2ガングリオシド蓄積症治療用のヒトβ-ヘキソサミニダーゼの機能改変, 第29回日本糖質学会年会, 2009年9月.
368.	辻大輔, 豊島優裕, 南條遥, 伊藤孝司 : GM2ガングリオシドーシスモデルマウスにおける骨髄由来細胞のケモカインシステムを介した脳内浸潤, 第29回日本糖質学会年会, 2009年9月.
369.	松岡和彦, 田村友美, 辻大輔, 櫻庭均, 伊藤孝司 : β-Hexosaminidase Bの機能改変とGM2ガングリオシドーシスに対する酵素補充療法への応用, 第29回日本糖質学会年会, 2009年9月.
370.	伊藤孝司, 辻大輔, 松岡和彦, 宮﨑絵梨, 明星裕美, 千葉靖典, 地神芳文, 櫻庭均 : 組換えリソソーム酵素の脳内補充療法の開発, 日本薬学会第129年会, 2009年3月.
371.	辻大輔, 松岡和彦, 廣瀬由記子, 余田英士, 宮﨑絵梨, 明星裕美, 笠原由子, 千葉靖典, 地神芳文, 二木史朗, 櫻庭均, 伊藤孝司 : Sandhoff病モデルマウスへの組換えヒトβ-ヘキソサミニダーゼの脳室内補充と治療効果, JST第三回糖鎖全体会議, 2009年1月.
372.	伊藤孝司 : 糖鎖機能を利用した組換えヒトβ-ヘキソサミニダーゼの脳内補充療法の開発, JST第三回糖鎖全体会議, 2009年1月.
373.	伊藤良和, 伊崎俊介, 高野正志, 増田由佳, 吉村佳之, 梅本淳, 沖津宏, 山村陽子, 湊拓也, 伊藤孝司 : 大腸がん患者に対するS-1の術前化学療法における組織内プロテオームの変動解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
374.	増田由佳, 辻大輔, 吉田有花, 余田英士, 伊藤孝司 : ヒト癌幹細胞株における癌幹細胞の単離及び性状解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
375.	高野正志, 辻大輔, 増田由佳, 伊藤良和, 徳田美幸, 梅本淳, 沖津宏, 湊拓也, 山村陽子, 伊藤孝司 : 胃癌におけるGastrokineの発現変動と機能解析に関する研究, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
376.	吉田有花, 辻大輔, 豊島優裕, 伊藤孝司 : ケモカインリガンド・レセプターシステムを介した病態マウス由来骨髄細胞の脳内移行に関する基礎研究, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
377.	余田英士, 辻大輔, 伊藤孝司, 若槻照彦 : Sandhoff病モデルマウス由来核移植胚性肝細胞から神経系への分化誘導系の確立, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
378.	田村友美, 松岡和彦, 辻大輔, 伊藤孝司 : レンチウイルスベクターを用いた高機能型ヒトbeta-Hexosaminidase A 発現間葉径幹細胞の樹立と性状解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
379.	辻大輔, 廣瀬由記子, 中瀬生彦, 二木史朗, 伊藤孝司 : Cell penetrating peptideを用いた中枢神経系疾患に対するProtein therapyに関する基礎研究, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
380.	堀川靖, 辻大輔, 田口雅浩, 廣瀬由記子, 二木史朗, 伊藤孝司 : Cell penetrating peptideを用いたヒト保護タンパク/カテプシンAの細胞内補充効果の検討, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
381.	田口雅浩, 辻大輔, 相川聖一, 松澤史子, 伊藤孝司 : ほ乳類シアリダーゼの発現と性質比較, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
382.	辻大輔, 宮﨑絵梨, 松岡和彦, 明星裕美, 笠原由子, 千葉靖典, 地神芳文, 川島育夫, 櫻庭均, 伊藤孝司 : Sandhoff 病モデルマウスに対するメタノール資化性酵母由来ヒトβ-ヘキソサミニダーゼの脳内補充効果, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
383.	松岡和彦, 辻大輔, 相川聖一, 松澤史子, 櫻庭均, 伊藤孝司 : α鎖へのN型糖鎖追加によるヒトβ-HexosaminidaseAの脳内酵素補充効果の改善, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
384.	川島永子, 辻大輔, 伊藤孝司, 仲山賢一 : GM2ガングリオシドーシス由来アストロサイトの異常増殖メカニズムの解明, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, 2008年12月.
385.	Seiji Hitaoka, Eri Kori, Yasushi Horikawa, Masahiro Taguchi, Tatsusada Yoshida, Kouji Itou and Hiroshi Chuman : Molecular Dynamics Study of the Effect of Arg344 Mutation on the Activation of Human Cathepsin A, CBI2008, Oct. 2008.
386.	Shugo Tsuda, Akira Shigenaga, Daisuke Tsuji, Naomi Nishioka, Yoshitake Sumikawa, Kouji Itou and Akira Otaka : Development of UV irradiation-responsive amino acid with peptide bond cleavage ability and its application to a nucleocytoplasmic shuttle peptide, 第22回内藤コンファレンス, Sep. 2008.
387.	明星裕美, 笠原由子, 辻大輔, 伊藤孝司, 櫻庭均, 千葉靖典, 地神芳文 : メタノール資化性酵母生産系を利用したリソソーム病治療薬の生産とその評価, 第28回日本糖質学会年会(JSCR), 2008年8月.
388.	伊藤孝司, 辻大輔, 松岡和彦, 宮﨑絵梨, 明星裕美, 笠原由子, 千葉靖典, 櫻庭均, 川島育夫, 地神芳文 : Sandhoff病モデルマウスに対する組換えヒトβ-ヘキソサミニダーゼの脳内補充効果, 第28回日本糖質学会年会(JSCR), 2008年8月.
389.	松岡和彦, 辻大輔, 相川聖一, 松澤史子, 櫻庭均, 伊藤孝司 : リン酸化N-グリカン追加型組換えヒトβ-ヘキソサミニダーゼAを用いたSandhoff病モデルマウスに対する効率的脳内補充, 第28回日本糖質学会年会(JSCR), 2008年8月.
390.	辻大輔, 廣瀬由記子, 伊藤孝司 : 中枢神経系構成細胞へのCell penetrating peptide 融合タンパクに対するヘパラン硫酸プロテオグリカンの関与, 第28回日本糖質学会年会(JSCR), 2008年8月.
391.	湊拓也, 沖津宏, 田中麻美, 山村陽子, 片山和久, 石倉久嗣, 木村秀, 坂田章聖, 藤井義幸, 伊藤孝司 : 胃癌に対するS-1術前2週投与前後のプロテオーム解析による有用性の検討, 第63回日本消化器外科学会総会, 2008年7月.
392.	辻大輔, 安岡寛子, 松岡和彦, 宮﨑絵梨, 廣瀬由記子, 明星裕美, 笠原由子, 千葉靖典, 地神芳文, 二木史朗, 櫻庭均, 伊藤孝司 : GM2ガングリオシドーシスモデルマウスに対する組換えヒトβ-ヘキソサミニダーゼの脳内補充効果, 第50回日本脂質生化学会, 2008年6月.
393.	余田英士, 辻大輔, 若山照彦, 伊藤孝司 : Sandhoff病モデルマウス由来核移植胚性幹細胞を用いた中枢神経系モデルの構築及び病態解析, 第49回日本生化学会中国・四国支部例会, 2008年5月.
394.	辻大輔, 安岡寛子, 松岡和彦, 宮﨑絵梨, 廣瀬由記子, 明星裕美, 笠原由子, 千葉靖典, 地神芳文, 櫻庭均, 伊藤孝司 : Sandhoff病モデルマウスに対するメタノール資化性酵母由来組換えヒトβ-ヘキソサミニダーゼの脳内補充効果, 第49回日本生化学会中国・四国支部例会, 2008年5月.
395.	廣瀬由記子, 辻大輔, 伊藤孝司 : Cell penetrating peptideを用いたProtein Therapyに関する基礎研究, 第49回日本生化学会中国・四国支部例会, 2008年5月.
396.	吉田有花, 辻大輔, 余田英士, 豊島優裕, 伊藤孝司 : Sandhoff病モデルマウス由来骨髄細胞の性質決定, 第49回日本生化学会中国・四国支部例会, 2008年5月.
397.	増田由佳, 辻大輔, 吉田有花, 伊藤孝司 : ヒト大腸癌細胞株における癌幹細胞の単離及び性質決定, 第49回日本生化学会中国・四国支部例会, 2008年5月.
398.	高野正志, 伊崎俊介, 梅本淳, 沖津宏, 湊拓也, 山村陽子, 伊藤孝司 : 胃がん特異的腫瘍マーカーとしてのGastrokine1の有用性の検討, 第49回日本生化学会中国・四国支部例会, 2008年5月.
399.	松岡和彦, 辻大輔, 相川聖一, 松澤史子, 櫻庭均, 伊藤孝司 : 新規糖鎖付加によるβ-HexosaminidaseAの高機能化, 第49回日本生化学会中国・四国支部例会, 2008年5月.
400.	伊藤孝司 : リソソーム病に対する次世代酵素補充療法の開発, 日本薬学会第128年会, 2008年3月.
401.	重永章, 辻大輔, 西岡直美, 山本純, 津田修吾, 伊藤孝司, 大髙章 : ペプチド結合切断能を有する光応答型アミノ酸の開発と核-細胞質シャトルペプチドへの応用, 日本薬学会年会, 2008年3月.
402.	伊藤孝司 : 糖鎖機能を利用した組換えリソソーム酵素の脳内補充療法開発, 第1回KSGCシンポジウム「糖鎖医学の曙光」, 2008年3月.
403.	湊拓也, 沖津宏, 田中麻美, 山村陽子, 片山和久, 木村秀, 坂田章聖, 山下理子, 藤井義幸, 丹黒章, 伊藤孝司, 伊崎俊介, 高野正志 : TS-1の術前2週投与により著効がえられた進行胃癌の2症例, 第80回日本胃癌学会総会, 2008年2月.
404.	辻大輔, 安岡寛子, 松岡和彦, 広瀬由記子, 明星裕美, 笠原由子, 千葉靖典, 地神芳文, 二木史朗, 桜庭均, 伊藤孝司 : Sandhoff病モデルマウスに対する組換えヒトβ-ヘキソサミニダーゼの脳内補充効果, JST第二回糖鎖全体会議, 2008年1月.
405.	伊藤孝司 : Sandhoff病モデルマウスの中枢神経系への組換えヒトβ-ヘキソサミニダーゼの補充効果, JST第二回糖鎖全体会議, 2008年1月.
406.	安岡寛子, 辻大輔, 広瀬由記子, 明星裕美, 千葉靖典, 地神芳文, 二木史朗, 桜庭均, 伊藤孝司 : Cell penetrating peptideを用いたヒトβ-ヘキソサミニダーゼの細胞内補充効果の検討, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
407.	明星裕美, 千葉靖典, 笠原由子, 八木絵美, 安岡寛子, 伊藤孝司, 桜庭均, 地神芳文 : メタノール資化生酵母Ogataea minutaによる高リン酸型糖鎖含有リソソーム酵素の生産, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
408.	松岡和彦, 辻大輔, 伊藤孝司, 明星裕美, 千葉靖典, 地神芳文, 土居洋文, 相川聖一, 松澤史子, 桜庭均 : in silicoデザインに基く組換えヒトβ-ヘキソサミニダーゼの高機能化, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
409.	広瀬由記子, 辻大輔, 安岡寛子, 二木史朗, 伊藤孝司 : オリゴアルギニンペプチド融合タンパクの細胞内局在解析, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
410.	河下映里, 辻大輔, 川島永子, 仲山賢一, 伊藤孝司 : Sandhoff病モデルマウス由来ミクログリアにおけるMIP-1α生産誘導メカニズムの解析, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
411.	伊崎俊介, 山内卓, 吉村好之, 梅本淳, 伊藤孝司 : レクチンブロッティングによる大腸がん患者由来組織における糖タンパク質の糖鎖構造解析, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
412.	辻大輔, 広瀬由記子, 安岡寛子, 二木史朗, 伊藤孝司 : オリゴアルギニンペプチド融合タンパクの細胞内導入機構解析, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
413.	川島永子, 辻大輔, 伊藤孝司, 仲山賢一 : GM2ガングリオシドーシス由来アストロサイトの異常増殖メカニズムの解明, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
414.	藤島加織, 辻大輔, 田島陽一, 桜庭均, 伊藤孝司 : リソソーム病におけるシアル酸トランスポーターsialin及びN-glycolyl型GM2の発現解析, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
415.	東根ゆかり, 辻大輔, 宮崎絵梨, 澤田誠, 伊藤孝司 : 血液脳関門を構成する細胞由来液性因子のミクログリアに与える影響, 第30回日本分子生物学会年会第80回日本生化学会大会合同大会, 2007年12月.
416.	山村陽子, 沖津宏, 湊拓也, 片山和久, 田中麻美, 石倉久, 一森敏弘, 木村秀, 阪田章聖, 高野正志, 伊藤孝司 : TS-1(100mg/日)の術前2週間投与によりリンパ節転移が消失した進行胃癌の1切除例, 第69回日本臨床外科学会総会, 2007年11月.
417.	櫻庭均, 吉永美智留, 田島陽一, 松澤史子, 相川聖一, 岩本邦彦, 小林俊秀, Tim Edmunds, 伊藤孝司 : 組換えヒト酸性α-グルコシダーゼとその基質アナログとの分子間相互作用, 第49回日本先天代謝異常学会, 2007年11月.
418.	田口雅浩, 辻大輔, 相川聖一, 松澤史子, 伊藤孝司 : ヒトシアリダーゼ遺伝子の相同性を利用した酵素機能改変, 第46回日本薬学会・日本薬剤師会日本病院薬剤師会中国四国支部学術大会, 2007年11月.
419.	辻大輔, 松岡和彦, 河下映里, 余田英士, 伊藤孝司 : Sandhoff病モデルマウス由来グリア細胞株の樹立, 第46回日本薬学会・日本薬剤師会日本病院薬剤師会中国四国支部学術大会, 2007年11月.
420.	Akira Shigenaga, Daisuke Tsuji, Nishioka Naomi, Tsuda Shugo, Kouji Itou and Akira Otaka : Development of stimulus-responsive amino acid with peptide bond-cleavage ability and its application to a nucleocytoplasmic shuttle peptide, 第44回ペプチド討論会, Nov. 2007.
421.	重永章, 辻大輔, 西岡直美, 津田修吾, 伊藤孝司, 大髙章 : ペプチド結合切断能を有する刺激応答型アミノ酸の開発と核-細胞質シャトルペプチドへの展開, 第33回反応と合成の進歩シンポジウム, 2007年11月.
422.	Shunsuke Izaki, Masashi Takano, Yoshiyuki Yoshimura, Atsushi Umemoto, Hiroshi Okitsu, Yoko Yamamura, Takuya Minato and Kouji Itou : Proteomic evaluation of neo-adjuvant S-1 chemotherapy for colorectal cancer patients, 66th Annual Meeting of the Japanese Cancer Association, Oct. 2007.
423.	Masashi Takano, Shunsuke Izaki, Yoshiyuki Yoshimura, Atsushi Umemoto, Hiroshi Okitsu, Yoko Yamamura, Takuya Minato and Kouji Itou : Significant decrease of gastrokine-1 expression in gastric tissues derived from patients with gastric adenocarcinoma, 66th Annual Meeting of the Japanese Cancer Association, Oct. 2007.
424.	湊拓也, 沖津宏, 田中麻美, 山村陽子, 片山和久, 木村秀, 坂田章聖, 山下理子, 藤井義幸, 丹黒章, 伊藤孝司, 伊崎俊介, 高野正志 : TS-1の術前2週投与によりほぼCRがえられた進行胃癌の1症例, 第82回中国四国外科学会総会, 2007年9月.
425.	プルワンティヌヌク, 辻大輔, アズリナアハマド, カラバシルミレーバ, 姚陳娟, 長谷川敬展, 赤松徹也, 伊藤孝司, 細井和雄 : 導管結紮によるマウス顎下腺での一過性のIL-6の増加が幹細胞マーカーSca-1の持続的な上昇を引き起す, 第49回歯科基礎医学会学術大会, 2007年8月.
426.	明星裕美, 笠原由子, 安岡寛子, 伊藤孝司, 桜庭均, 千葉靖典, 地神芳文 : メタノール資化性酵母Ogataea minutaにおける高リン酸化型糖鎖含有HexAの産生, 第27回日本糖質学会年会, 2007年8月.
427.	伊藤孝司, 松岡和彦, 安岡寛子, 辻大輔, 相川聖一, 松澤史子, 桜庭均, 明星裕美, 千葉靖典, 地神芳文 : Tay-Sachs病およびSandhoff病の酵素補充療法への応用を目指した高機能化ヒトβ-ヘキソサミニダーゼの発現, 第27回日本糖質学会年会, 2007年8月.
428.	辻大輔, 安岡寛子, 廣瀬由記子, 明星裕美, 千葉靖典, 地神芳文, 伊藤孝司 : メタノール資化性酵母由来糖鎖改変酵素のSandhoff病モデルマウス新生仔腹腔内投与に対する補充効果, 第27回日本糖質学会年会, 2007年7月.
429.	伊藤孝司 : 高機能型組換えリソソーム酵素の開発とリソソーム病の酵素補充療法への応用, 第6回国際バイオフォーラム, 2007年6月.
430.	伊崎俊介, 山内卓, 吉村好之, 梅本淳, 伊藤孝司 : 大腸がん患者由来腫組織における糖タンパク質の糖鎖構造の変動, 第48回日本生化学会中国・四国支部例会, 2007年5月.
431.	重永章, 辻大輔, 津田修吾, 伊藤孝司, 大髙章 : 刺激応答型アミノ酸を利用した核-細胞質シャトルペプチドの開発, 日本ケミカルバイオロジー研究会第2回年会, 2007年5月.
432.	松岡和彦, 辻大輔, 相川聖一, 相川史子, 櫻庭均, 伊藤孝司 : 糖鎖追加型変異導入に基くヒトb-Hexosaminidaseの高機能化, 第48回日本生化学会中国・四国支部例会, 2007年5月.
433.	廣瀬由記子, 辻大輔, 安岡寛子, 伊藤孝司 : PTD融合タンパクの細胞内導入及び局在解析, 第48回日本生化学会中国・四国支部例会, 2007年5月.
434.	辻大輔, 川島永子, 仲山賢一, 河下映里, 東根ゆかり, 伊藤孝司 : Sandhoff 病モデルマウス由来グリア細胞の単離・性質決定及び酵素補充効果, 第48回日本生化学会中国・四国支部例会, 2007年5月.
435.	東根ゆかり, 辻大輔, 松岡和彦, 櫻庭均, 伊藤孝司 : 抗GM2抗体を用いたCell-ELISAの確立とGM2ガングリオシドーシスの治療効果の評価, 日本薬学会第127年会, 2007年3月.
436.	明星裕美, 笠原由子, 高柴みな子, 安岡寛子, 伊藤孝司, 桜庭均, 千葉靖典, 地神芳文 : メタノール資化性酵母のMNN4遺伝子の解析と高リン酸化型糖鎖含有HexAの生産, 日本農芸学会2007年度大会, 2007年3月.
437.	松岡和彦, 相川聖一, 松澤史子, 櫻庭均, 辻大輔, 伊藤孝司 : 酵素補充療法への応用を目的としたヒトβヘキソサミニダーゼの高機能化, 日本薬学会第127年会, 2007年3月.
438.	安岡寛子, 辻大輔, 廣瀬由記子, 明星裕美, 千葉靖典, 地神芳文, 伊藤孝司 : メタノール資化性酵母由来糖鎖改変酵素のSandhoff病モデルマウス新生児への補充効果の検討, 日本薬学会第127年会, 2007年3月.
439.	河下映里, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウス由来ミクログリア細胞株の性質決定, 日本薬学会第127年会, 2007年3月.
440.	辻大輔, 河下映里, 伊藤孝司 : Sandhoff病モデルマウスにおけるグリア細胞の活性化, 日本薬学会第127年会, 2007年3月.
441.	伊藤孝司 : Sandhoff病モデルマウスの中枢神経系へのリソソーム酵素補充効果, JST CREST 糖鎖全体会議, 2007年1月.
442.	伊藤孝司 : リソソーム病の多因子性と治療ターゲット, 徳島大学大学院ヘルスバイオサイエンス研究部 21世紀COE「多因子疾患克服に向けたプロテオミクス研究」共催第3回公開シンポジウム多因子疾患克服へ向けた分子的戦略, 2006年11月.
443.	門田佳人, 相川聖一, 松澤史子, 桜庭均, 蔦幸児, 伊藤孝司 : ヒト保護タンパク質/カテプシンAの分子モデリングとアミノ酸置換効果の解析, 第7回長井長義記念シンポジウム, 2006年9月.
444.	蔦幸児, 門田佳人, 田口雅浩, 伊藤孝司 : 膜透過性ペプチド融合ノイラミニダーゼ-1による酵素補充療法を目指した基礎研究, 第7回長井長義記念シンポジウム, 2006年9月.
445.	藤島加織, 松澤史子, 相川聖一, 桜庭均, 門田佳人, 伊藤孝司 : 遊離シアル酸蓄積症患者由来培養fibroblastにおける含シアル酸複合糖鎖の解析とヒトsiallin遺伝子導入効果の検討, 第7回長井長義記念シンポジウム, 2006年9月.
446.	伊崎俊介, 高野正志, 山内卓, 吉村好之, 梅本淳, 伊藤孝司 : 日本人大腸がん患者由来組織におけるプロテオーム解析, 第7回長井長義記念シンポジウム, 2006年9月.
447.	高野正志, 伊崎俊介, 山内卓, 吉村好之, 梅本淳, 伊藤孝司 : 日本人胃がん患者由来組織におけるプロテオーム解析, 第7回長井長義記念シンポジウム, 2006年9月.
448.	辻大輔, 東根ゆかり, 余田英士, 伊藤孝司 : 中枢神経系における糖鎖レセプター発現解析及び酵素補充効果, 第7回長井長義記念シンポジウム, 2006年9月.
449.	安岡寛子, 廣瀬由記子, 辻大輔, 明星裕美, 千葉靖典, 地神芳文, 伊藤孝司 : メタノール資化性酵母由来糖鎖改変酵素のリソソーム病モデルマウス新生児腹腔内投与による治療効果, 第7回長井長義記念シンポジウム, 2006年9月.
450.	久我尚寛, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウスの脳におけるプロテオーム解析, 第7回長井長義記念シンポジウム, 2006年9月.
451.	東根ゆかり, 辻大輔, 余田英士, 伊藤孝司 : ミクログリア細胞表面における糖鎖発現解析, 第7回長井長義記念シンポジウム, 2006年9月.
452.	河下映里, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウス由来株化ミクログリアの樹立と性質決定, 第7回長井長義記念シンポジウム, 2006年9月.
453.	廣瀬由記子, 安岡寛子, 辻大輔, 伊藤孝司 : 脳内酵素補充を目指したPTD融合HexAの産生・獲得, 第7回長井長義記念シンポジウム, 2006年9月.
454.	プルワンティヌヌク, 辻大輔, カラバシルミレーバ, 李雪飛, 姚陳娟, 赤松徹也, 金森憲雄, 伊藤孝司, 細井和雄 : マウス顎下腺における腺房細胞/導管細胞マーカーの発現，およびサイドポピュレーション細胞群の挙動に及ぼす主導管結紮の影響, 第48回歯科基礎医学会学術大会, 2006年9月.
455.	笠原由子, 明星裕美, 千葉靖典, 川島育夫, 桜庭均, 伊藤孝司, 地神芳文 : GM2ガングリオシドーシスの酵素補充療法を目指した組換え酵素の生産と培養細胞による評価, 第26回日本糖質学会年会, 2006年8月.
456.	辻大輔, 河下映里, 奥野周蔵, 伊藤孝司 : Sandhoff病モデルマウス由来中枢神経系構成細胞における酵素補充効果, 第26回日本糖質学会年会, 2006年8月.
457.	伊藤孝司 : 糖鎖機能に基くリソソーム病の診断・治療法の開発, KAGAWA機能糖鎖フォーラム第3回シンポジウム, 2006年7月.
458.	東根ゆかり, 辻大輔, 松岡和彦, 伊藤孝司 : 抗GM2抗体を用いたCell-ELISA系の確立とGM2ガングリオシドーシス由来細胞の治療効果の評価, 第47回日本生化学会中国四国支部例会, 2006年5月.
459.	久我尚寛, 辻大輔, 伊藤孝司 : Sandhoff病モデルマウスの脳におけるプロテオーム解析, 第47回日本生化学会中国四国支部例会, 2006年5月.
460.	辻大輔, 久我尚寛, 奥野周蔵, 伊藤孝司 : Sandhoff病モデルマウス由来オリゴデンドロサイト前駆細胞の単離及び蓄積糖質解析, 第47回日本生化学会中国四国支部例会, 2006年5月.
461.	門田佳人, 佐藤匡史, 加藤龍一, 若槻壮市, 蔦幸児, 伊藤孝司 : ヒトノイラミニダーゼ-1の酵素活性発現に対するN末端領域の影響, 日本薬学会第126年会, 2006年3月.
462.	辻大輔, 石橋靖浩, 東根ゆかり, 松岡和彦, 伊藤孝司 : Sandhoff病モデルマウス由来間葉系幹細胞の神経細胞分化誘導, 第5回日本再生医療学会総会, 2006年3月.
463.	明星裕美, 笠原由子, 高岡友紀, 辻大輔, 伊藤孝司, 千葉靖典, 地神芳文 : メタノール資化性酵母によるヒトβ-ヘキソサミニダーゼAの発現と解析, 日本農芸学会2006年度大会, 2006年3月.
464.	辻大輔, 河下映里, 伊藤孝司 : レンチウィルスベクターによるSandhoff病モデルマウス由来ミクログリアに対する治療効果, 日本薬学会第126年会, 2006年3月.
465.	大澤真以, 小谷政晴, 三川浩輝, 田島陽一, 伊藤孝司, 渡部和彦, 桜庭均 : ザンドホッフ病マウス由来Schwann細胞の樹立と組み換えヒト・ベータ-ヘキソサミニダーゼの取り込みの解析, 第11回日本ライソゾーム病研究会, 2005年12月.
466.	Mai Murata, Masaharu Kotani, Youichi Tajima, Daisuke Tsuji, Yasuhiro Ishibashi, Kouji Itou, Kazuhiko Watabe and Hitoshi Sakuraba : Corrective effects of ecombinant human β-hexosaminidases on Sandhoff mice Schwann cells, 第78回日本生化学会大会, Oct. 2005.
467.	多田納豊, 竹内直博, 桜庭均, 高橋勉, 高田五郎, 伊藤孝司 : エラスチン繊維形成障害コステロ症候群患者由来皮膚線維芽細胞株の特徴付け, 第78回日本生化学会大会, 2005年10月.
468.	N Takeuchi, Y Tatano, H Sakuraba, T Takahashi, G Takada and Kouji Itou : Proteome alterations in fibroblasts with Costello syndrome, 第78回日本生化学会大会, Oct. 2005.
469.	Yutaka Tatano, Naohiro Takeuchi, Hitoshi Sakuraba, Tsutomu Takahashi, Goro Takada and Kouji Itou : Characterization of fibroblast from Costello syndrome with impaired elastogenesis, 第78回生化学会大会, Oct. 2005.
470.	Yoshito Kadota, seiichi Aikawa, Fumiko Matsuzawa, Kohji Tsuta, Hirofumi Doi and Kouji Itou : Effects of Amino Acid Substitutions on Processing of Human Cathepsin A (Serine Carboxypeptidase) Based on Homology Modeling, 第78回日本生化学会大会, Oct. 2005.
471.	Daisuke Tsuji, Yasuhiro Ishibashi, Akiko Itimiya, Naohiro Kuga, Hiroko Yasuoka, Aya Kuroki and Kouji Itou : Analysis of accumulated glycoconjugates in glial cells derived from Sandhoff disease model mice, 第78回生化学会大会, Oct. 2005.
472.	Daisuke Tsuji, Yasuhiro Ishibashi, Eri Kawashita, Akiko Itimiya, Aya Kuroki and Kouji Itou : Corrective effects of gene transfer on microglia derived from Sandhoff disease model mice, 第78回日本生化学会大会, Oct. 2005.
473.	Aya Kuroki, Daisuke Tsuji, Yasuhiro Ishibashi, Yukari Higashine, Mai Murata, Hitoshi Sakuraba and Kouji Itou : Gene transfer with lentiviral vector into immortalized glial precursor cell line derived from Sandhoff disease model mice, 第78回日本生化学会大会, Oct. 2005.
474.	Akiko Itimiya, Daisuke Tsuji, Yasuhiro Ishibashi, Yukari Higashine and Kouji Itou : Metabolic Correction in Myeloid Cells derived from Sandhoff Disease Model Mice, 第78回日本生化学大会, Oct. 2005.
475.	Daisuke Tsuji, Yasuhiro Ishibasi, Itimiya Akiko and Kouji Itou : Induction of neuronal cells from mesenchymal stem cells derived from Sandhoff disease model mice and effect of therapeutic administration, 第78回生化学会大会, Oct. 2005.
476.	辻大輔, 石橋靖浩, 一宮綾希子, 久我尚寛, 黒木綾, 伊藤孝司 : Sandhoff病モデルマウスの中枢神経系構成細胞における蓄積基質解析, 第25回日本糖質学会年会, 2005年7月.
477.	明星裕美, 笠原由子, 千葉靖典, 伊藤孝司, 地神芳文 : メタノール資化性酵母の生産する組換えヒトβ-ヘキソサミニダーゼのGM2ガングリオシドーシス酵素補充療法の検討, 第6回長井長義記念シンポジウム, 2005年7月.
478.	竹内直博, 多田納豊, 桜庭均, 高橋勉, 高田五郎, 伊藤孝司 : コステロ症候群患者由来皮膚繊維芽細胞におけるプロテオーム解析, 第6回長井長義記念シンポジウム, 2005年7月.
479.	多田納豊, 竹内直博, 桜庭均, 高橋勉, 高田五郎, 伊藤孝司 : エラスチン繊維形成不全を伴うコステロ症候群の発症機構の解析, 第6回長井長義記念シンポジウム, 2005年7月.
480.	千葉靖典, 明星裕美, 高岡友紀, 高柴みな子, 笠原由子, 小林和男, 伊藤孝司, 桜庭均, 地神芳文 : メタノール資化性酵母Ogataea minutaを利用した糖タンパク質生産と糖鎖改変, 第25回日本糖質学会年会, 2005年7月.
481.	伊藤孝司 : 糖鎖レセプターをターゲットとした酵素補充療法の進歩, 第6回長井長義記念シンポジウム, 2005年7月.
482.	久我尚寛, 辻大輔, 伊藤孝司 : マウスES細胞から神経幹細胞への新規分化誘導法の検討, 第6回長井長義記念シンポジウム, 2005年7月.
483.	一宮綾希子, 辻大輔, 石橋靖浩, 東根ゆかり, 伊藤孝司 : Sandhoff病モデルマウス由来骨髄系細胞に対する治療効果, 第6回長井長義記念シンポジウム, 2005年7月.
484.	石橋靖浩, 辻大輔, 東根ゆかり, 河下映里, 伊藤孝司 : β-Hexosaminidase欠損症患者由来培養皮膚線維芽細胞に対する遺伝子治療法及びクロスコレクション効果の検討, 第6回長井長義記念シンポジウム, 2005年7月.
485.	辻大輔, 石橋靖浩, 一宮綾希子, 伊藤孝司 : Sandhoff病モデルマウス骨髄間葉系幹細胞の神経細胞への分化誘導, 第6回長井長義記念シンポジウム, 2005年7月.
486.	石橋靖浩, 辻大輔, 黒木綾, 久我尚寛, 河下映里, 東根ゆかり, 安岡寛子, 伊藤孝司 : Lentiviral systemを用いたSandhoff病及びTay-Sachs病の治療効果の検討, 第46回日本生化学会中国四国支部例会, 2005年5月.
487.	辻大輔, 黒木綾, 石橋靖浩, 伊藤孝司 : Sandhoff病モデルマウス由来ミクログリアにおける遺伝子導入効果, 第46回日本生化学会中国・四国支部例会, 2005年5月.
488.	桑原淳, 一宮綾希子, 伊藤達生, 伊藤孝司 : 転写因子Sp1の核局在におけるzinc fingerによる蛋白質認識の可能性, 第125年会日本薬学会, 2005年3月.
489.	門田佳人, 相川聖一, 松澤史子, 土居洋文, 桑原淳, 伊藤孝司 : 分子モデリングに基づく人カテプシンA (セリンカルボキシペプチダーゼ)のキモスタチン感受性の遺伝的改変, 第125年会日本薬学会, 2005年3月.
490.	吉原隆浩, 吉村好之, 梅本淳, 沖津宏, 門田康正, 多田納豊, 門田佳人, 桑原淳, 山内卓, 伊藤孝司 : 日本人胃ガン患者由来組織におけるプロテオーム解析, 第125年会日本薬学会, 2005年3月.
491.	黒木綾, 辻大輔, 石橋靖浩, 板倉朋宏, 桑原淳, 伊藤孝司 : Sandhoff 病モデルマウス由来不死化中枢神経系細胞株に対する酵素補充効果, 第77回日本生化学会大会, 2004年10月.
492.	大枝由加子, 小谷政晴, 桜庭均, 門田佳人, 多田納豊, 桑原淳, 伊藤孝司 : レクチン染色を用いたノイラミニダーゼー1欠損細胞におけるシアル酸含有糖鎖蓄積の解析, 第77回日本生化学会大会, 2004年10月.
493.	門田佳人, 佐藤百合恵, 相川聖一, 松澤史子, 土居洋文, 桑原淳, 桜庭均, 伊藤孝司 : 分子モデリングに基づくヒトカテプシンA (セリンカルボキシペプチダーゼ)の微生物由来のインヒビターに対する感受性の遺伝的改変, 第77回日本生化学会大会, 2004年10月.
494.	多田納豊, 竹内直博, 桑原淳, 桜庭均, 高橋勉, 高田五郎, 伊藤孝司 : β-galactosidase欠損症とコステロ症候群における67-kDaエラスチン結合タンパク質(EBP)の発現解析, 第77回日本生化学会大会, 2004年10月.
495.	明星裕美, 笠原由子, 辻大輔, 多田納豊, 伊藤孝司, 櫻庭均, 千葉靖典, 地神芳文 : メタノール資化性酵母における組換えヒトβ-ヘキソサミニダーゼの精製と諸性質, 第77回日本生化学会大会, 2004年10月.
496.	辻大輔, 板倉朋宏, 黒木綾, 石橋靖浩, 桑原淳, 伊藤孝司 : Sandhoff病モデルマウスの中枢神経系におけるMIP-1αの特異的誘導, 第77回日本生化学会大会, 2004年10月.
497.	辻大輔, 板倉朋宏, 黒木綾, 石橋靖浩, 桑原淳, 伊藤孝司 : Sandhoff病モデルマウスの中枢神経系におけるケモカインの異常発現, 第45回日本生化学会中国四国支部例会, 2004年5月.
498.	桑原淳, 伊藤達生, 山野由紀子, 伊藤孝司 : 転写因子Sp1の核局在における蛋白質相互作用の可能性, 日本薬学会第124年会, 2004年3月.
499.	佐藤百合恵, 相川聖一, 松澤史子, 土居洋文, 吉田達貞, 中馬寛, 門田佳人, 桑原淳, 伊藤孝司 : ヒトカテプシンA(酸性セリンカルボキシペプチダーゼ)特異的阻害剤の分子デザイン, 日本薬学会第124年会, 2004年3月.
500.	板倉朋宏, 黒木綾, 辻大輔, 石橋靖宏, 桑原淳, 伊藤孝司 : マウス神経系不死化細胞株の樹立とGM2ガングリオシドーシスの治療法開発への応用, 日本薬学会第124年会, 2004年3月.
501.	伊藤孝司 : 糖鎖機能を利用したリソソーム病の酵素補充療法の実用化と展望, 第110回日本薬学会中国・四国支部例会, 2004年1月.
502.	黒木綾, 板倉朋宏, 辻大輔, 石橋靖浩, 桑原淳, 伊藤孝司, 松澤史子, 相川聖一, 土居洋文 : リソソーム性β-ヘキソサミニダーゼサブユニット間認識機構, 第42回日本薬学会・日本薬剤師会中四国支部学術大会, 2003年11月.
503.	吉田達貞, 佐藤百合恵, 林良雄, 伊藤孝司, 中馬寛 : リソソーム病に関与するCathepsin Aとその阻害剤間の相互作用様式の解析, 第31回構造活性相関シンポジウム, 2003年11月.
504.	Y Satoh, S Aikawa, F Matsuzawa, H Doi, K Oheda, Y Kadota, J Kuwahara, T Aoyagi, H Sakuraba and Kouji Itou : Actions of microbial inhibitors on serine caroxypeptidase from man, yeast and wheat, 第76回日本生化学会大会, Oct. 2003.
505.	板倉朋宏, 黒木綾, Daisuke Tsuji, 桑原淳 and Kouji Itou : Establishment and characterization of an immortalized neural cell line derived from murine ES cells, 第76回日本生化学会大会, Oct. 2003.
506.	板倉朋宏, 黒木綾, 辻大輔, 尼子尊行, 桑原淳, 山中正二, 伊藤孝司 : Sandhoff病モデルマウス由来細胞株に対するヒト及びマウスb-ヘキソサミニダーゼ遺伝子および酵素補充効果の解析, 日本薬学会第123年会, 2003年3月.
507.	尼子尊行, 辻大輔, 板倉朋宏, 桑原淳, 伊藤孝司 : マウス胚性幹細胞(ES細胞)の誘引因子に関する研究, 第41回日本薬学会・日本薬剤師会中四国支部学術大会, 2002年11月.
508.	辻大輔, 山中正二, 尼子尊行, 板倉朋宏, 黒木綾, 桑原淳, 伊藤孝司 : Sandhoff病モデルマウスの臓器におけるケモカイン発現の解析, 第75回日本生化学会大会, 2002年10月.
509.	板倉朋宏, 黒木綾, 辻大輔, 尼子尊行, 桑原淳, 山中正二, 伊藤孝司 : Sandhoff病モデルマウス由来培養細胞株におけるヒトβ-Hex遺伝子の発現解析, 第75回日本生化学会大会, 2002年10月.
510.	多田納豊, 小谷政晴, 櫻庭均, 辻大輔, 門田佳人, 桑原淳, 新本美智枝, 加瀬良一, 伊藤孝司 : ヒト酸性β-ガラクトシダーゼの遺伝子変異に基づく選択的スプライシング産物(エラスチン結合タンパク質)の発現変動, 日本薬学会第122年会, 2002年3月.

その他・研究会:

1.	Naoshi Yamazaki, Makiko Shinomiya, Hironobu Ike, Yasuo Shinohara, Noriaki Minakawa, Kouji Itou and Yoshiharu Takiguchi : Use of modified U1 small nuclear RNA for improved formation of properly spliced mRNA encoding human cathepsin A from the gene having an IVS7 +3a>g mutation, FEBS Open Bio, Vol.8, No.Supplement 1, ShT.35-1, Jul. 2018.
2.	辻大輔, 千葉靖典, 伊藤孝司 : 酵母で作製したリソソーム酵素でGM2ガングリオシドーシスモデルマウスを治療しました, 臨床遺伝学公開シンポジウム 2011「リソソーム病の診断と治療のために」, 2011年3月.
3.	豊島優裕, 辻大輔, 伊藤孝司 : Protein kinase C alpha and betaⅠregulate morphology of microglia derived from Sandhoff disease model mice, ソウル国立大学校薬学大学-徳島大学薬学部学術交流協定締結20周年記念シンポジウム, 2010年12月.
4.	Kouji Itou : Recent progress in therapeutic approach for inherited metabolic disorders. Molecular design and development of novel recombinant lysosomal enzymes for replacement therapy., Exchange Program between SNU and Tokushima Univ, Jun. 2010.

特許:

1.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, 特許第202080062553.3号.
2.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, 特許第20836020.6号.
3.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, 特許第3145622号.
4.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, 特許第17/623,302号.
5.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, 特許第2021-530672号.
6.	伊藤孝司, 辻大輔, 櫻庭均 : ヒトβ-ヘキソサミニダーゼBの基質特異性を変換し，且つ，プロテアーゼ抵抗性を付与した新規高機能酵素, 特許第6230158号.
7.	伊藤孝司, 中馬寛, 林良雄, 飯島希昌子 : 新規なカテプシンA阻害剤, 特願2003-382713, .
8.	伊藤孝司, 宍戸宏造, 新藤充 : 新規なアポトーシス誘導剤, 特願2001-372050, 特開2003-171278, .
9.	伊藤孝司 : β-ヘキソサミニダーゼとその量産方法, 特願2005-367983, .
10.	伊藤孝司, 桜庭均, 相川聖一, 相川史子 : β-ヘキソサミニダーゼA(HexA)を構成するα-サブユニット，前記α-サブユニットを有するHexA，前記α-サブユニットをコードする遺伝子，ベクターおよび形質転換細胞, 特願2007-044790, .
11.	伊藤孝司, 木下崇司, 三谷藍 : ライソゾームを標的とした新規DDSの開発, (2021年12月), 特許第PCT/JP2021/048780号.
12.	伊藤孝司, 木下崇司, 三谷藍 : ライソゾームを標的とした新規DDSの開発, (2021年10月), 特許第2021-178052(2021-000120)号.
13.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, (2020年7月), 特許第PCT/JP2020/026174号.
14.	中山淳, 寺町順平, 安倍正博, 難波康祐, 伊藤孝司, 辻大輔 : 新規イノン化合物及びその用途, (2019年10月), 特許第PCT/JP2019/042086号 (2019年10月).
15.	伊藤孝司, 月本準 : 改変ノイラミニダーゼ, (2019年7月), 特許第2019-126376号 (2019年7月).
16.	中山淳, 寺町順平, 安倍正博, 難波康祐, 伊藤孝司, 辻大輔 : 新規イノン化合物及びその用途, (2018年10月), 特許第2018-203219号 (2018年10月).
17.	伊藤孝司, 辻大輔, 村松慎一, 浅井克仁 : テイーサックス病及びサンドホッフ病治療用の新規アデノ随伴ウイルスビリオンテイーサックス病及びサンドホッフ病のin vivo遺伝子治療用の改変型Hex鎖遺伝子搭載AAV-modHEXBベクター, (2018年1月), 特許第2018-011705号.
18.	伊藤孝司, 西岡宗一郎, 松崎祐二, 飯野健太, 瀬筒秀樹, 小林功 : マンノース-6-リン酸基含有糖蛋白質の製造方法，及び蛍光基結合型マンノース-6-リン酸基含有糖蛋白質の細胞内分布を検出する方法, 特願PCT/JP2017/13322 (2017年3月), .
19.	伊藤孝司, 櫻庭均, 辻大輔 : ヒトβ-ヘキソサミニダーゼBの基質特異性を変換し，且つ，プロテアーゼ抵抗性を付与した新規高機能酵素, 特願PCT/JP2013/078179 (2013年10月), 特開2014-542171 (2013年10月), 特許第2014-542171号 (2013年10月).

科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

リソソーム性シアリダーゼ欠損症に対する新規遺伝子治療法開発 (研究課題/領域番号: 23K06116 )
遺伝子改変マウスと未固定遺体を用いた動脈硬化の新規の病態解明と治療法の開発 (研究課題/領域番号: 22H03069 )
翻訳後修飾部分に多様性を有するタンパク質ライブラリ精密構築への挑戦 (研究課題/領域番号: 20K21483 )
高機能型バイオスーパーの合理的デザインと疾患モデルによる治療評価システム開発 (研究課題/領域番号: 17H04102 )
放射光を用いたヒトノイラミニダーゼの細胞内結晶構造解析 (研究課題/領域番号: 16K18507 )
高いスプライス異常修復能を有した改変U1 snRNA発現ベクターの構築と疾病治療 (研究課題/領域番号: 16K08235 )
次世代タンパク性医薬品開発に向けた反応システム系の開発と展開 (研究課題/領域番号: 16H02611 )
中枢神経症状を伴うリソソーム病患者由来iN細胞の誘導と神経変性制御機構の解明 (研究課題/領域番号: 26670269 )
ネオグライコバイオロジクスの創製とリソソーム病治療薬開発への応用 (研究課題/領域番号: 26293120 )
神経変性を伴うリソソーム蓄積症におけるシナプス病態の解明と治療への応用 (研究課題/領域番号: 25110722 )
中枢神経症状を伴うリソソーム病における神経変性メカニズムの解明 (研究課題/領域番号: 25460389 )
動物の新規遺伝子病の分子基盤解明、診断、予防および治療法の開発 (研究課題/領域番号: 25292181 )
新規リソソーム指向性トラフィック制御化合物の探索と治療法開発への応用 (研究課題/領域番号: 24659262 )
核酸医薬品創製のための新素子と新戦略の開発 (研究課題/領域番号: 23659054 )
タンパク質間相互作用部位をターゲットとした新規バイオ医薬品の開発 (研究課題/領域番号: 23390140 )
天然物・生物有機化学を基盤とする創薬標的タンパク質同定効率化法の開拓と応用展開 (研究課題/領域番号: 23390026 )
血液脳関門透過能をもつES細胞由来細胞株の樹立と脳内ターゲッティング機構 (研究課題/領域番号: 18659023 )
機能領域の立体構造改変による新規高機能リソソーム病治療薬の開発 (研究課題/領域番号: 18390303 )
ヒト血管内皮細胞由来の幹細胞誘引因子の作用機構と組織ターゲッティングへの応用 (研究課題/領域番号: 14657583 )
細胞接着誘導阻害活性ポリケタイドの合成と機能解析 (研究課題/領域番号: 14370722 )
生物工学的手法に基づく組織指向性医薬資源の開発と応用 (研究課題/領域番号: 12470503 )
中枢神経系におけるエンドセリン分解酵素の欠損と病態 (研究課題/領域番号: 09670168 )
リソソーム酵素のプロセシング及び分解制御機構とその遺伝病の分子機構の解明 (研究課題/領域番号: 09267246 )
酵素蛋白質の構造解析と分子設計:遺伝性代謝病の病態解明と治療方開発への応用 (研究課題/領域番号: 08670932 )
リソソーム酵素のプロセシング及び分解制御機構とその遺伝病の分子病態の解明 (研究課題/領域番号: 08278241 )
多機能性蛋白による糖鎖分解酵素の制御機構とその欠損症の分子病理 (研究課題/領域番号: 07259222 )
中枢神経系における多機能性糖蛋白質とそのペプチド性基質の局在性に関する研究 (研究課題/領域番号: 06780521 )
細胞及び組織病理の3次元再構築:遺伝性代謝病の発症機構の解明と臨床への応用 (研究課題/領域番号: 06670847 )
CDG症候群の病因・病態解析 (研究課題/領域番号: 06454311 )
多機能性蛋白による糖鎖分解酵素の制御機構とその欠損症の分子病理 (研究課題/領域番号: 06267224 )
多機能性蛋白による糖鎖分解酵素の制御機構とその欠損症の分子病理 (研究課題/領域番号: 05274229 )
遺伝性ライソゾーム病における変異遺伝子発現機序の解析 (研究課題/領域番号: 05253222 )
遺伝性ライソゾーム病における変異遺伝子発現機序の解析 (研究課題/領域番号: 04260230 )
遺伝子大量発現による先天代謝異常症の病態研究及び治療法の開発 (研究課題/領域番号: 03670516 )
遺伝性ライソゾ-ム病における変異遺伝子発現機序の解析 (研究課題/領域番号: 03265219 )
軟骨形成不全症の病因と病態に関する分子生物学的研究 (研究課題/領域番号: 01480264 )
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名誉教授 : 伊藤孝司

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科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

名誉教授 : 伊藤 孝司

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科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

名誉教授 : 伊藤孝司