Tokushima University / Educator and Researcher Directory --- Kishimoto, Koji

Personal Web Page

https://researchmap.jp/researchmap-koji (researchmap)

https://orcid.org/0000-0003-1946-3286 (ORCID)

Field of Study

○	Cancer and Stem Cell Biology
○	Neuroscience
○	Cancer immunology
○	Lipid Biochemistry
○	Cancer and Stem Cell Biology

Subject of Study

○	Study of G2A that regulates stemness of cancer stem cells.
○	Study of KIDScPLA2 induced by neuronal excitation that regulates neurogeneration.
○	Study of cancer stem cells-specific cytotoxic T lymphocytes
○	神経新生を制御する興奮性神経刺激誘導性脂質代謝酵素の研究 (2)
○	Elucidate molecular mechanisms and identify critical molecules that give cancer stem cells a survival advantage in starvation. (stem cell, oncology, lipid peroxidation)

Book / Paper

Book:

1.	S Yamamoto, Hiroshi Suzuki and Koji Kishimoto : Lipoxygenases: transformation of their hydroperoxy products., Karger, Dec. 1997.
2.	S Yamamoto, Koji Kishimoto, T Arakawa, H Suzuki, M Nakamura, T Yoshimoto, T Takao, Y Shimonishi and T Tanabe : Arachidonate 12-lipoxygenases: Catalytic properties and regulation of the enzyme gene., Plenum Press, Sep. 1997.
3.	S Yamamoto, T Yoshimoto, Y Takahashi, H Suzuki, T Arakawa, Koji Kishimoto, T Oshima, GR Reddy, N Ueda, J Murakami, Y Yamamoto, C Yokoyama, Yousuke Ebina, S Matsuda, Y Konishi, Y Mimura, S Arase and M Okuma : Mammalian lipoxygenases with special reference to arachidonate 12-lipoxygenase., Excerpta Medica, Jun. 1993.
4.	S Yamamoto, T Yoshimoto, N Ueda, S Takahashi, H Matsuda, H Suzuki, T Oshima, H Ikawa, T Hada, GR Reddy, (名) Yamamoto, Koji Kishimoto, T Arakawa, K Ishimura, S Arase, C Yokoyama, T Tanabe, H Toh, M Nishiyama, H Okamoto, T Watanabe and T Hori : Arachidonate 12-lipoxygenases: Enzymology and molecular biology., Kluwer Academic Publishers, Jun. 1993.

Academic Paper (Judged Full Paper):

1.	Kosuke Sugiura, Katsuya Hirasaka, Tasuku Maeda, Takayuki Uchida, Koji Kishimoto, Motoko Oarada, Siegfried Labeit, Anayt Ulla, Iori Sakakibara, Reiko Nakao, Koichi Sairyo and Takeshi Nikawa : MuRF1 deficiency prevents age-related fat weight gain, possibly through accumulation of PDK4 in skeletal muscle mitochondria in older mice, Journal of Orthopaedic Research, Vol.40, No.5, 1026-1038, 2021. (Tokushima University Institutional Repository) ● Metadata: 116581 (Link to Publication Site) ● Publication site (DOI): 10.1002/jor.25131 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34185335 ● Summary page in Scopus @ Elsevier: 2-s2.0-85109422486 (Tokushima University Institutional Repository: 116581, DOI: 10.1002/jor.25131, PubMed: 34185335, Elsevier: Scopus)
2.	Ohno Ayako, Nobuo Maita, Tabata Takanori, Nagano Hikaru, Arita Kyohei, Ariyoshi Mariko, Takayuki Uchida, Reiko Nakao, Ulla Anayt, Kosuke Sugiura, Koji Kishimoto, Teshima-Kondo Shigetada, Okumura Yuushi and Takeshi Nikawa : Crystal structure of inhibitor-bound human MSPL that can activate high pathogenic avian influenza., Life Science Alliance, Vol.4, No.6, e202000849, 2021. (Summary) Infection of certain influenza viruses is triggered when its HA is cleaved by host cell proteases such as proprotein convertases and type II transmembrane serine proteases (TTSP). HA with a monobasic motif is cleaved by trypsin-like proteases, including TMPRSS2 and HAT, whereas the multibasic motif found in high pathogenicity avian influenza HA is cleaved by furin, PC5/6, or MSPL. MSPL belongs to the TMPRSS family and preferentially cleaves [R/K]-K-K-R sequences. Here, we solved the crystal structure of the extracellular region of human MSPL in complex with an irreversible substrate-analog inhibitor. The structure revealed three domains clustered around the C-terminal α-helix of the SPD. The inhibitor structure and its putative model show that the P1-Arg inserts into the S1 pocket, whereas the P2-Lys and P4-Arg interacts with the Asp/Glu-rich 99-loop that is unique to MSPL. Based on the structure of MSPL, we also constructed a homology model of TMPRSS2, which is essential for the activation of the SARS-CoV-2 spike protein and infection. The model may provide the structural insight for the drug development for COVID-19. (Keyword) Animals / Birds / Crystallography, X-Ray / Humans / Influenza in Birds / Membrane Proteins / Orthomyxoviridae / Protein Conformation / Serine Endopeptidases (Tokushima University Institutional Repository) ● Metadata: 116821 (Link to Publication Site) ● Publication site (DOI): 10.26508/LSA.202000849 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33820827 ● Summary page in Scopus @ Elsevier: 2-s2.0-85103997820 (Tokushima University Institutional Repository: 116821, DOI: 10.26508/LSA.202000849, PubMed: 33820827, Elsevier: Scopus)
3.	Hidekazu Utsunomiya, Riko Hiraishi, Koji Kishimoto, Sari Hamada, Shin Abe, Yusuke Bekki and Norio Kamemura : Cytotoxicity of Benzophenone-3, an organic UV filter, is caused by increases of intracellular Zn²⁺ levels in rat thymocytes., Chemico-Biological Interactions, Vol.298, 52-56, 2019. (Summary) Benzophenone-3 (BP-3) is often used as an ultraviolet (UV) light filter in sunscreen products. Although BP-3 protects the human skin and hair from damage caused by excessive UV radiation, it is reported to exhibit toxic effects in human. However, the cytotoxicity of BP-3 on various cells is still not well understood. In the present study, the cytotoxicity of BP-3 against rat thymocytes was evaluated using a flow cytometric technique with fluorescent probes. Cell mortality increased significantly after 3 h of exposure to 300 M BP-3, whereas the mean intensity of 5-chloromethylfluorescein diacetate (5-CMF) fluorescence and cellular content of non-protein thiols decreased significantly. However, the membrane potential of thymocytes was not change by BP-3 treatment. Moreover, intracellular Zn levels increased significantly in a concentration-dependent manner in response to 30 M BP-3 or higher. The BP-3-induced changes in intracellular Zn levels and non-protein thiol content increased the vulnerability of thymocytes to oxidative stress. We concluded that BP-3-induced cytotoxicity may be caused by oxidative stress associated with an increase in intracellular Zn levels. (Keyword) Animals / Benzophenones / Cell Survival / Drug Synergism / hydrogen peroxide / Male / oxidative stress / Rats, Wistar / Sulfhydryl Compounds / Sunscreening Agents / Thymocytes / zinc (Link to Publication Site) ● Publication site (DOI): 10.1016/j.cbi.2018.10.029 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30391638 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056212974 (DOI: 10.1016/j.cbi.2018.10.029, PubMed: 30391638, Elsevier: Scopus)
4.	Tomoharu Miyashita, Hidehiro Tajima, Isamu Makino, Mitsuyoshi Okazaki, Takahisa Yamaguchi, Yoshinao Ohbatake, Sinichi Nakanuma, Hironori Hayashi, Hiroyuki Takamura, Itasu Ninomiya, Sachio Fushida, Koji Kishimoto, John W. Harmon and Tetsuo Ohta : Neoadjuvant Chemotherapy with Gemcitabine Plus Nab-paclitaxel Reduces the Number of Cancer-associated Fibroblasts Through Depletion of Pancreatic Stroma., Anticancer Research, Vol.38, No.1, 337-343, 2018. (Summary) In this study, the effects of neoadjuvant chemotherapy (NAC) on cancer-associated fibroblasts (CAFs) in pancreatic cancer stroma were investigated. Density of -smooth muscle actin (SMA)-positive fibroblasts in resected surgical specimens from untreated patients, patients receiving conventional gemcitabine plus S-1 (GS), and patients receiving gemcitabine plus nab-paclitaxel (GnP) was determined by hybrid cell counting. 18F-Fluorodeoxyglucose positron-emission tomography (FDG-PET) scans and carbohydrate antigen 19-9 (CA19-9) concentrations were used to assess tumor activity before and after chemotherapy in the GnP group. In this retrospective study of 65 patients, SMA expression was reduced in the GnP group, as revealed by markedly disorganized collagen and a low density of SMA-positive fibroblasts. There were significantly fewer SMA-positive fibroblasts in the GnP than in the untreated and GS groups, but there was no significant difference between the latter two groups. SMA density reflected a decrease in standardized uptake value on FDG-PET, but not CA19-9 concentration, after GnP chemotherapy. These data suggest that the GnP regimen induces stromal depletion, resulting in fewer CAFs. (Keyword) Actins / Adenocarcinoma / Aged / Aged, 80 and over / Albumins / Antineoplastic Agents / CA-19-9 Antigen / Cancer-Associated Fibroblasts / collagen / Deoxycytidine / Disease-Free Survival / Female / Humans / Male / Middle Aged / Neoadjuvant Therapy / Paclitaxel / Pancreas / Pancreatic Neoplasms / Positron-Emission Tomography / Retrospective Studies / Stromal Cells (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.12227 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29277792 ● Summary page in Scopus @ Elsevier: 2-s2.0-85039774105 (DOI: 10.21873/anticanres.12227, PubMed: 29277792, Elsevier: Scopus)
5.	Norio Kamemura, Sara Murakami, Hiroaki Komatsu, Masahiro Sawanoi, Kenji Miyamoto, Kazumi Ishidoh, Koji Kishimoto, Akihiko Tsuji and Keizo Yuasa : Type II cGMP-dependent protein kinase negatively regulates fibroblast growth factor signaling by phosphorylating Raf-1 at serine 43 in rat chondrosarcoma cells., Biochemical and Biophysical Research Communications, Vol.483, No.1, 82-87, 2017. (Summary) Although type II cGMP-dependent protein kinase (PKGII) is a major downstream effector of cGMP in chondrocytes and attenuates the FGF receptor 3/ERK signaling pathway, its direct target proteins have not been fully explored. In the present study, we attempted to identify PKGII-targeted proteins, which are associated with the inhibition of FGF-induced MAPK activation. Although FGF2 stimulation induced the phosphorylation of ERK1/2, MEK1/2, and Raf-1 at Ser-338 in rat chondrosarcoma cells, pretreatment with a cell-permeable cGMP analog strongly inhibited their phosphorylation. On the other hand, Ser-43 of Raf-1 was phosphorylated by cGMP in a dose-dependent manner. Therefore, we examined the direct phosphorylation of Raf-1 by PKGII. Wild-type PKGII phosphorylated Raf-1 at Ser-43 in a cGMP-dependent manner, but a PKGII D412A/R415A mutant, which has a low affinity for cGMP, did not. Finally, we found that a phospho-mimic mutant, Raf-1 S43D, suppressed FGF2-induced MAPK pathway. These results suggest that PKGII counters FGF-induced MEK/ERK activation through the phosphorylation of Raf-1 at Ser-43 in chondrocytes. (Tokushima University Institutional Repository) ● Metadata: 111887 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbrc.2017.01.001 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28057484 ● Summary page in Scopus @ Elsevier: 2-s2.0-85008689720 (Tokushima University Institutional Repository: 111887, DOI: 10.1016/j.bbrc.2017.01.001, PubMed: 28057484, Elsevier: Scopus)
6.	C Aso, M Araki, N Ohshima, K Tatei, T Hirano, H Obinata, M Kishi, Koji Kishimoto, A Konishi, F Goto, H Sugimoto and T Izumi : Protein purification and cloning of diacylglycerol lipase from rat brain., The Journal of Biochemistry, Vol.159, No.6, 585-597, 2016. (Summary) Diacylglycerol (DG) lipase, which hydrolyses 1-stearoyl-2-arachidonyl-sn-glycerol to produce an endocannabinoid, 2-arachidonoylglycerol, was purified from the soluble fraction of rat brain lysates. DG lipase was purified about 1,200-fold by a sequential column chromatographic procedure. Among proteins identified by mass spectrometry analysis in the partially purified DG lipase sample, only DDHD domain containing two (DDHD2), which was formerly regarded as a phospholipase A1, exhibited significant DG lipase activity. Rat DDHD2 expressed in Chinese hamster ovary cells showed similar enzymatic properties to partially purified DG lipase from rat brain. The source of DG lipase activity in rat brain was immunoprecipitated using anti-DDHD2 antibody. Thus, we concluded that the DG lipase activity in the soluble fraction of rat brain is derived from DDHD2. DDHD2 is distributed widely in the rat brain. Immunohistochemical analysis revealed that DDHD2 is expressed in hippocampal neurons, but not in glia. (Keyword) Animals / Arachidonic Acids / CHO Cells / Cloning, Molecular / Cricetinae / Cricetulus / Endocannabinoids / Gene Expression Regulation, Enzymologic / Glycerides / Hippocampus / Lipoprotein Lipase / Nerve Tissue Proteins / Neuroglia / Neurons / Protein Domains / Rats (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvw002 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26790472 ● Search Scopus @ Elsevier (PMID): 26790472 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvw002 (DOI: 10.1093/jb/mvw002, PubMed: 26790472)
7.	Y Kawakami, S Hirano, M Kinoshita, A Otsuki, Toshiko Suzuki-Yamamoto, M MKimoto Suzuki, M Kimoto, S Sasabe, M Fukushima, Koji Kishimoto, T Izumi, T Oga, S Narumiya, M Sugahara, M Miyano, S Yamamoto and Y Takahashi : Neutralization of leukotriene C4 and D4 activity by monoclonal and single-chain antibodies., Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.1840, No.6, 1625-1633, 2014. (Summary) Cysteinyl leukotrienes (LTs) are key mediators in inflammation. To explore the structure of the antigen-recognition site of a monoclonal antibody against LTC4 (mAbLTC), we previously isolated full-length cDNAs for heavy and light chains of the antibody and prepared a single-chain antibody comprising variable regions of these two chains (scFvLTC). We examined whether mAbLTC and scFvLTC neutralized the biological activities of LTC4 and LTD4 by competing their binding to their receptors. mAbLTC and scFvLTC inhibited their binding of LTC4 or LTD4 to CysLT1 receptor (CysLT1R) and CysLT2 receptor (CysLT2R) overexpressed in Chinese hamster ovary cells. The induction by LTD4 of monocyte chemoattractant protein-1 and interleukin-8 mRNAs in human monocytic leukemia THP-1 cells expressing CysLT1R was dose-dependently suppressed not only by mAbLTC but also by scFvLTC. LTC4- and LTD4-induced aggregation of mouse platelets expressing CysLT2R was dose-dependently suppressed by either mAbLTC or scFvLTC. Administration of mAbLTC reduced pulmonary eosinophil infiltration and goblet cell hyperplasia observed in a murine model of asthma. Furthermore, mAbLTC bound to CysLT2R antagonists but not to CysLT1R antagonists. These results indicate that mAbLTC and scFvLTC neutralize the biological activities of LTs by competing their binding to CysLT1R and CysLT2R. Furthermore, the binding of cysteinyl LT receptor antagonists to mAbLTC suggests the structural resemblance of the LT-recognition site of the antibody to that of these receptors. mAbLTC can be used in the treatment of inflammatory diseases such as asthma. (Keyword) Animals / Antibodies, Monoclonal / Asthma / CHO Cells / Cricetinae / Cricetulus / Cytokines / Humans / Leukotriene Antagonists / Leukotriene C4 / Leukotriene D4 / Male / Mice / Mice, Inbred C57BL / Platelet Aggregation / Receptors, Leukotriene / Single-Chain Antibodies (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbagen.2013.12.016 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24361619 ● Search Scopus @ Elsevier (PMID): 24361619 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbagen.2013.12.016 (DOI: 10.1016/j.bbagen.2013.12.016, PubMed: 24361619)
8.	荒木麻理, 麻生知寿, 大嶋紀安, 立井一明, 平野瞳子, 杉本博之, 岸美紀子, Koji Kishimoto and 和泉孝志 : 新規脳ジアシルグリセロールリパーゼの同定., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.55, 118-120, 2013. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1571698601102958464 (CiNii: 1571698601102958464)
9.	川上祐生, 平野詩織, 木下麻衣, 大槻朱美, 下田一花, 鈴木麻希子, 青山沙絵, 山本登志子, 木本眞順美, 福島光夫, Koji Kishimoto, 和泉孝志, 小賀徹, 成宮周, 吉木谷博, 尚三山本 and 高橋吉孝 : ロイコトリエン作用に対する抗ロイコトリエンC4単鎖抗体の中和効果., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.54, 265-267, 2012.
10.	Koji Kishimoto, 谷畑貴俊, 原口崇, 清水健志, 大島紀安, 立井一明 and 和泉孝志 : Gタンパク質共役型受容体，G2Aを介したがん幹細胞性制御., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.54, 108-110, 2012.
11.	T Ohyama, K Sato, Koji Kishimoto, Y Yamazaki, N Horiguchi, T Ichikawa, S Kakizaki, H Takagi, T Izumi and M Mori : Azelnidipine is a calcium blocker that attenuates liver fibrosis and may increase antioxidant defense., British Journal of Pharmacology, Vol.165, No.4b, 1173-1187, 2012. (Summary) Oxidative stress plays a critical role in liver fibrogenesis. Reactive oxygen species (ROS) stimulate hepatic stellate cells (HSCs), and ROS-mediated increases in calcium influx further increase ROS production. Azelnidipine is a calcium blocker that has been shown to have antioxidant effects in endothelial cells and cardiomyocytes. Therefore, we evaluated the anti-fibrotic and antioxidative effects of azelnidipine on liver fibrosis. We used TGF-β1-activated LX-2 cells (a human HSC line) and mouse models of fibrosis induced by treatment with either carbon tetrachloride (CCl(4) ) or thioacetamide (TAA). Azelnidipine inhibited TGF-β1 and angiotensin II (Ang II)-activated α1(I) collagen mRNA expression in HSCs. Furthermore, TGF-β1- and Ang II-induced oxidative stress and TGF-β1-induced p38 and JNK phosphorylation were reduced in HSCs treated with azelnidipine. Azelnidipine significantly decreased inflammatory cell infiltration, pro-fibrotic gene expressions, HSC activation, lipid peroxidation, oxidative DNA damage and fibrosis in the livers of CCl(4) - or TAA-treated mice. Finally, azelnidipine prevented a decrease in the expression of some antioxidant enzymes and accelerated regression of liver fibrosis in CCl(4) -treated mice. Azelnidipine inhibited TGF-β1- and Ang II-induced HSC activation in vitro and attenuated CCl(4) - and TAA-induced liver fibrosis, and it accelerated regression of CCl(4) -induced liver fibrosis in mice. The anti-fibrotic mechanism of azelnidipine against CCl(4) -induced liver fibrosis in mice may have been due an increased level of antioxidant defence. As azelnidipine is widely used in clinical practice without serious adverse effects, it may provide an effective new strategy for anti-fibrotic therapy. (Keyword) Angiotensin II / Animals / Antioxidants / Azetidinecarboxylic Acid / Calcium / Calcium Channel Blockers / Carbon Tetrachloride / Cell Line / Cell Survival / Collagen Type I / Dihydropyridines / Disease Models, Animal / Gene Expression Regulation / Humans / Liver Cirrhosis / Male / Mice / Mice, Inbred C57BL / RNA, Messenger / Reactive Oxygen Species / Thioacetamide / Transforming Growth Factor beta1 (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1476-5381.2011.01599.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21790536 ● Search Scopus @ Elsevier (PMID): 21790536 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1476-5381.2011.01599.x (DOI: 10.1111/j.1476-5381.2011.01599.x, PubMed: 21790536)
12.	大嶋紀安, 岡崎優利, 吉澤郁美, 亀井康富, M Stefania, 岡本佳子, 立井一明, Koji Kishimoto, 小川佳宏, 加藤範久, C Daniela, 矢中規之 and 和泉孝志 : 哺乳動物のGDE群とマウスGDE5の非酵素的機構による骨格筋分化制御., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.54, 108-110, 2011. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1572261550735850880 (CiNii: 1572261550735850880)
13.	JC Russell, Koji Kishimoto, C O'Driascall and MA Hossain : Neuronal pentraxin 1 induction in hypoxic-ischemic neuronal death is regulated via a glycogen synthase kinase-3α/β dependent mechanism., Cellular Signalling, Vol.23, No.4, 673-682, 2010. (Summary) Intracellular signaling pathways that regulate the production of lethal proteins in central neurons are not fully characterized. Previously, we reported induction of a novel neuronal protein neuronal pentraxin 1 (NP1) in neonatal brain injury following hypoxia-ischemia (HI); however, how NP1 is induced in hypoxic-ischemic neuronal death remains elusive. Here, we have elucidated the intracellular signaling regulation of NP1 induction in neuronal death. Primary cortical neurons showed a hypoxic-ischemia time-dependent increase in cell death and that NP1 induction preceded the actual neuronal death. NP1 gene silencing by NP1-specific siRNA significantly reduced neuronal death. The specificity of NP1 induction in neuronal death was further confirmed by using NP1 (-/-) null primary cortical neurons. Declines in phospho-Akt (i.e. deactivation) were observed concurrent with decreased phosphorylation of its downstream substrate GSK-3α/β (at Ser21/Ser9) (i.e. activation) and increased GSK-3α and GSK-3β kinase activities, which occurred prior to NP1 induction. Expression of a dominant-negative inhibitor of Akt (Akt-kd) blocked phosphorylation of GSK-3α/β and subsequently enhanced NP1 induction. Whereas, overexpression of constitutively activated Akt (Akt-myr) or wild-type Akt (wtAkt) increased GSK-α/β phosphorylation and attenuated NP1 induction. Transfection of neurons with GSK-3α siRNA completely blocked NP1 induction and cell death. Similarly, overexpression of the GSK-3β inhibitor Frat1 or the kinase mutant GSK-3βKM, but not the wild-type GSK-3βWT, blocked NP1 induction and rescued neurons from death. Our findings clearly implicate both GSK-3α- and GSK-3β-dependent mechanism of NP1 induction and point to a novel mechanism in the regulation of hypoxic-ischemic neuronal death. (Keyword) Animals / C-Reactive Protein / Cell Culture Techniques / Cell Death / Cell Hypoxia / Cell Survival / Cells, Cultured / Enzyme Activation / Gene Knockdown Techniques / Glycogen Synthase Kinase 3 / Glycogen Synthase Kinase 3 beta / Hypoxia-Ischemia, Brain / Mice / Mice, Inbred C57BL / Mice, Knockout / Nerve Tissue Proteins / Neurons / Phosphorylation / Proto-Oncogene Proteins c-akt / RNA Interference / Rats / Rats, Inbred F344 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.cellsig.2010.11.021 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21130869 ● Search Scopus @ Elsevier (PMID): 21130869 ● Search Scopus @ Elsevier (DOI): 10.1016/j.cellsig.2010.11.021 (DOI: 10.1016/j.cellsig.2010.11.021, PubMed: 21130869)
14.	Koji Kishimoto, RC Li, J Zhang, JA Klaus, KK Kibler, S Doré, RC Koehler and A Sapirstein : Cytosolic phospholipase A₂alpha amplifies early cyclooxygenase-2 expression, oxidative stress and MAP kinase phosphorylation after cerebral ischemia in mice., Journal of Neuroinflammation, Vol.7, 42, 2010. (Summary) The enzyme cytosolic phospholipase A2 alpha (cPLA2alpha) has been implicated in the progression of cerebral injury following ischemia and reperfusion. Previous studies in rodents suggest that cPLA2alpha enhances delayed injury extension and disruption of the blood brain barrier many hours after reperfusion. In this study we investigated the role of cPLA2alpha in early ischemic cerebral injury. Middle cerebral artery occlusion (MCAO) was performed on cPLA2alpha+/+ and cPLA2alpha-/- mice for 2 hours followed by 0, 2, or 6 hours of reperfusion. The levels of cPLA2alpha, cyclooxygenase-2, neuronal morphology and reactive oxygen species in the ischemic and contralateral hemispheres were evaluated by light and fluorescent microscopy. PGE2 content was compared between genotypes and hemispheres after MCAO and MCAO and 6 hours reperfusion. Regional cerebral blood flow was measured during MCAO and phosphorylation of relevant MAPKs in brain protein homogenates was measured by Western analysis after 6 hours of reperfusion. Neuronal cPLA2alpha protein increased by 2-fold immediately after MCAO and returned to pre-MCAO levels after 2 hours reperfusion. Neuronal cyclooxygenase-2 induction and PGE2 concentration were greater in cPLA2alpha+/+ compared to cPLA2alpha-/- ischemic cortex. Neuronal swelling in ischemic regions was significantly greater in the cPLA2alpha+/+ than in cPLA2alpha-/- brains (+/+:2.2+/-0.3 fold vs. -/-:1.7+/-0.4 fold increase; P<0.01). The increase in reactive oxygen species following 2 hours of ischemia was also significantly greater in the cPLA2alpha+/+ ischemic core than in cPLA2alpha-/- (+/+:7.12+/-1.2 fold vs. -/-:3.1+/-1.4 fold; P<0.01). After 6 hours of reperfusion ischemic cortex of cPLA2alpha+/+, but not cPLA2alpha-/-, had disruption of neuron morphology and decreased PGE2 content. Phosphorylation of the MAPKs-p38, ERK 1/2, and MEK 1/2-was significantly greater in cPLA2a+/+ than in cPLA2alpha-/- ischemic cortex 6 hours after reperfusion. These results indicate that cPLA2alpha modulates the earliest molecular and injury responses after cerebral ischemia and have implications for the potential clinical use of cPLA2alpha inhibitors. (Keyword) Animals / Brain Ischemia / Cyclooxygenase 2 / Dinoprostone / Female / Group IV Phospholipases A2 / Infarction, Middle Cerebral Artery / Male / Mice / Mice, Knockout / Mitogen-Activated Protein Kinases / Neurons / Oxidative Stress / Phosphorylation / Reperfusion Injury (Link to Publication Site) ● Publication site (DOI): 10.1186/1742-2094-7-42 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20673332 ● Search Scopus @ Elsevier (PMID): 20673332 ● Search Scopus @ Elsevier (DOI): 10.1186/1742-2094-7-42 (DOI: 10.1186/1742-2094-7-42, PubMed: 20673332)
15.	MI Barliana, M KISHI, H Oninata, A Ogawa, Koji Kishimoto, N Ohshima, K Tatei and T Izumi : Novel function of 9(S)-hydroxyoctadecadienoic acid on proliferation of T cells., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.52, 212-215, 2010. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1571980075955359360 (CiNii: 1571980075955359360)
16.	Y Shen, Koji Kishimoto, DJ Linden and A Sapirstein : Cytosolic phospholipase A(2) alpha mediates electrophysiologic responses of hippocampal pyramidal neurons to neurotoxic NMDA treatment., Proceedings of the National Academy of Sciences of the United States of America, Vol.104, No.14, 6078-6083, 2007. (Summary) The arachidonic acid-generating enzyme cytosolic phospholipase A(2) alpha (cPLA(2)alpha) has been implicated in the progression of excitotoxic neuronal injury. However, the mechanisms of cPLA(2)alpha toxicity have yet to be determined. Here, we used a model system exposing mouse hippocampal slices to NMDA as an excitotoxic injury, in combination with simultaneous patch-clamp recording and confocal Ca(2+) imaging of CA1 pyramidal neurons. NMDA treatment caused significantly greater injury in wild-type (WT) than in cPLA(2)alpha null CA1 neurons. Bath application of NMDA evoked a slow inward current in voltage-clamped neurons (composed of both NMDA receptor-mediated and other conductances) that was smaller in cPLA(2)alpha null than in WT slices. This was not due to down-regulation of NMDA receptor function because NMDA receptor-mediated currents were equivalent in each genotype following brief photolysis of caged glutamate. Current-clamp recordings were made during and following NMDA exposure by eliciting a single action potential with a brief current injection. After NMDA exposure, WT CA1 neurons developed a spike-evoked plateau potential and an increased spike-evoked dendritic Ca(2+) transient. These effects were absent in CA1 neurons from cPLA(2)alpha null mice and WT neurons treated with a cPLA(2)alpha inhibitor. The Ca-sensitive K-channel toxins, apamin and paxilline, caused spike broadening and Ca(2+) enhancement in WT and cPLA(2)alpha null slices. NMDA application in WT and arachidonate applied to cPLA(2)alpha null cells occluded the effects of apamin/paxilline. These results indicate that cPLA(2)alpha activity is required for development of aberrant electrophysiologic events triggered by NMDA receptor activation, in part through attenuation of K-channel function. (Keyword) Animals / Cytosol / Electrophysiology / Hippocampus / Kinetics / Mice / Mice, Knockout / N-Methylaspartate / Neurons / Patch-Clamp Techniques / Phospholipases A / Pyramidal Cells (Link to Publication Site) ● Publication site (DOI): 10.1073/pnas.0605427104 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17389392 ● Search Scopus @ Elsevier (PMID): 17389392 ● Search Scopus @ Elsevier (DOI): 10.1073/pnas.0605427104 (DOI: 10.1073/pnas.0605427104, PubMed: 17389392)
17.	KM Brady, SJ Texel, Koji Kishimoto, RC Koehler and A Sapirstein : Cytosolic phospholipase A₂ alpha modulates NMDA neurotoxicity in mouse hippocampal cultures., The European Journal of Neuroscience, Vol.24, No.12, 3381-3386, 2006. (Summary) The arachidonic acid-specific cytosolic phospholipase A(2) alpha (cPLA(2)alpha) has been implicated in the generation of neurological injuries. cPLA(2)alpha-dependent neurological injury has been postulated to be mediated through inflammatory and eicosanoid pathways. We determined if cPLA(2)alpha amplifies the injury of a non-inflammatory, excitotoxic stimulus by modifying a well-described toxicity assay to measure the toxicity of N-methyl-d-aspartate (NMDA) in the CA1 region of organotypic, mouse hippocampal cultures. Hippocampal cultures from wild-type and cPLA(2)alpha knockout mice were exposed to 5, 7.5 or 10 microm NMDA for 1 h. Toxicity was measured 23 h later. Cultures derived from cPLA(2)alpha(-/-) mice and cultures treated with the selective inhibitor AACOCF(3) were significantly protected from NMDA toxicity, as compared with wild-type cultures. To determine if cPLA(2)alpha-dependent toxicity is cyclooxygenase (COX)-2 dependent, COX-2 and PGE(2) levels were measured 7 and 25 h after NMDA treatment. NMDA treatment failed to induce COX-2 protein or increase PGE(2) in the culture media in either genotype at either time. In contrast, phorbol 12-myristate 13-acetate and ionophore treatment caused robust induction of COX-2 and PGE(2) in both genotypes. We conclude that cPLA(2)alpha may have a hitherto unrecognized direct effect on excitatory neurotoxicity, suggesting that cPLA(2)alpha inhibition is a therapeutic candidate for treatment of the early, excitotoxic injury observed in stroke. (Keyword) Animals / Animals, Newborn / Arachidonic Acids / Blotting, Western / Cell Death / Cyclooxygenase 2 / Dose-Response Relationship, Drug / Drug Interactions / Enzyme Inhibitors / Excitatory Amino Acid Agonists / Hippocampus / Mice / Mice, Inbred BALB C / Mice, Knockout / N-Methylaspartate / Nitrobenzenes / Organ Culture Techniques / Phospholipases A / Sulfonamides / Tetradecanoylphorbol Acetate / Time Factors (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1460-9568.2006.05237.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17229087 ● Search Scopus @ Elsevier (PMID): 17229087 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1460-9568.2006.05237.x (DOI: 10.1111/j.1460-9568.2006.05237.x, PubMed: 17229087)
18.	K Yoshikawa, Y Kita, Koji Kishimoto and T Shimizu : Profiling of eicosanoid production in the rat hippocampus during kainic acid-induced seizure: dual phase regulation and differential involvement of COX-1 and COX-2., The Journal of Biological Chemistry, Vol.281, No.21, 14663-14669, 2006. (Summary) Kainic acid (KA)-induced seizure in rat involves eicosanoid production in the brain, but their production mechanism and biological functions are poorly understood. We profiled the eicosanoid production during KA-induced seizure by a comprehensive lipidomics analysis using liquid chromatography-tandem mass spectrometry. Systemic KA administration caused production of large amounts of prostaglandin (PG) F(2alpha) and PGD(2) in the hippocampus, with smaller amounts of other PGs and hydroxyeicosatetraenoic acids. The production was biphasic, which consisted of an initial burst in the first 30 min and a sustained late phase production. The initial phase was specific to the hippocampus and was blocked by intracerebroventricular administration of KA receptor antagonists. A selective cyclooxygenase (COX)-2 inhibitor, NS398, completely inhibited the initial phase productions, except for PGD(2) and thromboxane B(2), whose productions were also dependent on COX-1. These results suggest that KA signals directly stimulate the arachidonic acid cascade in the initial phase and that COX-1 and COX-2, both constitutively expressed at low levels, differentially contribute to PG productions. In the late phase, a sustained PG production in hippocampus appears due to the increased COX-2 levels even with a limited arachidonic acid supply. The present study demonstrates a dual phase regulatory mechanism of eicosanoid production during KA-induced seizure, providing a biochemical basis for understanding the biosynthesis and roles of eicosanoids in the brain. (Keyword) Animals / Arachidonic Acids / Brain / Cyclooxygenase 1 / Cyclooxygenase 2 / Cyclooxygenase 2 Inhibitors / Eicosanoids / Hippocampus / Kainic Acid / Male / Models, Biological / Nitrobenzenes / Rats / Rats, Wistar / Seizures / Sulfonamides (Link to Publication Site) ● Publication site (DOI): 10.1074/jbc.M511089200 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16569634 ● Search Scopus @ Elsevier (PMID): 16569634 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M511089200 (DOI: 10.1074/jbc.M511089200, PubMed: 16569634)
19.	吉川圭介, Koji Kishimoto, 北芳博 and 清水孝雄 : てんかん様痙攣刺激による脂質メディエーター及びその産生分子群の発現プロファイリング., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.46, 205-208, 2004.
20.	Koji Kishimoto, K Matsumura, Y Kataoka, H Morii and Y Watanabe : Localization of cytosolic phospholipase A2 messenger RNA mainly in neurons in the rat brain., Neuroscience, Vol.92, No.3, 1061-1077, 1999.
21.	Koji Kishimoto, K Matsumura, Y Kataoka, H Morii and Y Watanabe : Major population of 85-kDa cytosolic phospholipase A2 mRNA signals localized in neurons in rat brain., Neuroscience Research, Vol.22, S135, 1998.
22.	S Yamamoto, Koji Kishimoto, T Arakawa, Hiroshi Suzuki, Michihiro Nakamura, T Yoshimoto, T Takao, Y Shimonishi and T Tanabe : Arachidonate 12-lipoxygenases. Catalytic properties and regulation of the enzyme gene., Advances in Experimental Medicine and Biology, Vol.407, 191-196, 1997.
23.	B Langstrom, M Bergstrom, KJ Fasth, U Yngve, L Samuelsson, F Karimi, F Wu, L Lu, E Bergstrom, W Sihver, Koji Kishimoto and Y Watanabe : New probes for in vivo measurements of cell proliferation, antisense oligonucleotides pharmacokinetics, and receptor occupancy in acetylcholinergic and NK systems by using positron emission tomography., Neuroscience Research, Vol.23, S20, 1997.
24.	Hiroshi Suzuki, Koji Kishimoto and 尚三山本 : アラキドン酸酸素添加酵素の自殺的失活., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.39, 37-39, 1997.
25.	尚三山本, Hiroshi Suzuki and Koji Kishimoto : Lipoxygenase-Catalyzed Transformation of Its Primry Hydroperoxy Product., 過酸化脂質研究, Vol.20, No.1, 19, 1996.
26.	Koji Kishimoto, Hiroshi Suzuki, Michihiro Nakamura, 吉本谷博, 尚三山本, 高尾敏文, 下西康嗣 and 田辺忠 : ブタ白血球12-リポキシゲナーゼの自殺的失活に伴う酵素蛋白への15-ヒドロペルオキシエイコサテトラエン酸の取り込み., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.38, 276-279, 1996.
27.	Koji Kishimoto, Michihiro Nakamura, Hiroshi Suzuki, T Yoshimoto, S Yamamoto, T Takao, Y Shimonishi and T Tanabe : Suicide inactivation of porcine leukocyte 12-lipoxygenase associated with its incorporation of 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid derivative., Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, Vol.1300, No.1, 56-62, 1996. (Summary) Two isozymes of arachidonate 12-lipoxygenase, platelet-type and leukocyte-type, which were distinguished by their substrate specificities and primary structures, were investigated with reference to 'suicide' inactivation. Upon reaction with arachidonic acid the leukocyte-type enzyme was inactivated rapidly during the catalysis, whereas the platelet-type enzyme did not show such a rapid inactivation. The two 12-lipoxygenase isozymes were incubated with various hydroperoxy and hydroxy products from arachidonic acid. (15S)-Hydroperoxy-5,8,11,13-eicosatetraenoic acid (15-HPETE) was found to be a unique substrate of the leukocyte-type 12-lipoxygenase as follows. (1) 15-HPETE was an active substrate for porcine leukocyte 12-lipoxygenase, and converted anaerobically to a 14,15-epoxy compound (14,15-leukotriene A4). (2) A rapid inactivation of the enzyme was observed within 2 min upon aerobic and anaerobic incubations with 15-HPETE. (3) 15-HPETE was rapidly incorporated into the enzyme in a nearly equimolar amount under both aerobic and anaerobic conditions. (4) Several findings suggested a covalent binding of 15-HPETE or its derivative to the enzyme. (5) Such a rapid and stoichiometric incorporation of 15-HPETE was not observed with the platelet-type 12-lipoxygenase. On the basis of these findings we presumed that 15-HPETE was transformed to 14,15-leukotriene A4, which was covalently bound to the leukocyte-type 12-lipoxygenase leading to the suicide inactivation of the enzyme. (Keyword) Animals / Arachidonate 12-Lipoxygenase / Arachidonic Acid / Leukocytes / Leukotrienes / Lipid Peroxides / Lipoxygenase Inhibitors / Multienzyme Complexes / Swine (Link to Publication Site) ● Publication site (DOI): 10.1016/0005-2760(95)00241-3 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8608163 ● Search Scopus @ Elsevier (PMID): 8608163 ● Search Scopus @ Elsevier (DOI): 10.1016/0005-2760(95)00241-3 (DOI: 10.1016/0005-2760(95)00241-3, PubMed: 8608163)
28.	Koji Kishimoto, Michihiro Nakamura, Hiroshi Suzuki, 吉本谷博, 尚三山本, 高尾敏文, 下西康嗣 and 田辺忠 : 15-ヒドロペルオキシエイコサテトラエン酸のブタ白血球12-リポキシゲナーゼへの取り込みと酵素の自殺的失活., 過酸化脂質研究, Vol.19, No.1, 23, 1995.
29.	Michihiro Nakamura, N Ueda, Koji Kishimoto, T Yoshimoto, S Yamamoto and Kazunori Ishimura : Immunocytochemical localization of platelet-type arachidonate 12-lipoxygenase in mouse blood cells., The Journal of Histochemistry and Cytochemistry, Vol.43, No.3, 237-244, 1995.
30.	Hiroshi Suzuki, Koji Kishimoto, Tanihiro Yoshimoto, Shozo Yamamoto, Fumihiko Kanai, Yousuke Ebina, Akira Miyatake and Tadashi Tanabe : Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase., Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, Vol.1210, No.3, 308-316, 1994. (Summary) cDNA for arachidonate 12-lipoxygenase of porcine leukocytes was expressed in Escherichia coli. The recombinant 12-lipoxygenase was purified by immunoaffinity chromatography to near homogeneity with a specific activity of about 1.5 mumol/min per mg protein. Each of eight histidine residues, which were well-conserved among various mammalian lipoxygenases and presumed as ligands for non-heme iron, was substituted with leucine by site-directed mutagenesis. Each mutant enzyme was immunoaffinity-purified to near homogeneity. Mutations of His-361, -366 and -541 caused a total loss of enzyme activity, and the iron content was much lower (0.10, 0.06 and 0.06 g atom/mol protein) than that of the wild-type enzyme (0.53). Mutations of His-128 and -356 gave 159% and 162% specific activity of the wild-type enzyme, and the iron contents were 0.55 and 0.52 g atom/mol protein. Substitution of His-426 decreased the activity to 5%, but the iron content was 0.4 g atom/mol protein. The expression level of mutants at His-384 and -393 was too low to precisely determine the iron content. Taken together, His-361, -366 and -541 may play important roles for iron-binding in catalytically active 12-lipoxygenase. Since a high homology of amino acid sequence was known between porcine leukocyte 12-lipoxygenase and mammalian 15-lipoxygenases, we attempted to convert the 12-lipoxygenase to a 15-lipoxygenase. A double mutation of Val-418 and -419 to Ile and Met increased the ratio of 15- and 12-lipoxygenase activities from 0.1 to 5.7. (Keyword) Amino Acid Sequence / Animals / Arachidonate 12-Lipoxygenase / Base Sequence / Binding Sites / Escherichia coli / Iron / Leukocytes / Molecular Sequence Data / Mutagenesis, Site-Directed / Recombinant Proteins / Sequence Alignment / Swine (Link to Publication Site) ● Publication site (DOI): 10.1016/0005-2760(94)90234-8 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8305485 ● Summary page in Scopus @ Elsevier: 2-s2.0-0027958244 (DOI: 10.1016/0005-2760(94)90234-8, PubMed: 8305485, Elsevier: Scopus)
31.	吉本谷博, Hiroshi Suzuki, Koji Kishimoto, 尚三山本, 金井文彦, Yousuke Ebina, 宮武明 and 田辺忠 : アラキドン酸12-リポキシゲナーゼ反応におけるヒスチジン残基の役割., 過酸化脂質研究, Vol.17, No.1, 19, 1993.
32.	Hiroshi Suzuki, Koji Kishimoto, 吉本谷博, 山本尚三, 金井文彦, Yousuke Ebina, 宮武明 and 田辺忠 : ブタ白血球のアラキドン酸12-リポキシゲナーゼの部位特異的変異法による解析., 脂質生化学研究35, Vol.35, 415-418, 1993.
33.	S Yamamoto, T Yoshimoto, Y Takahashi, Hiroshi Suzuki, T Arakawa, Koji Kishimoto, T Hada, T Oshima, J Murakami, Y Yamamoto, C Yokoyama, Yousuke Ebina, E Takahashi, S Matsuda, Y Konishi, Y Mimura and M Okuma : Biochemical and molecular biological approaches to two types of arachidonate 12-lipoxygenase, Journal of Lipid Mediators, Vol.6, No.1-3, 69-73, 1993.
34.	T Arakawa, T Oshima, Koji Kishimoto, T Yoshimoto and S Yamamoto : Molecular structure and function of the porcine arachidonate 12-lipoxygenase gene., The Journal of Biological Chemistry, Vol.267, No.17, 12188-12191, 1992.
35.	吉本谷博, Hiroshi Suzuki, 荒川俊哉, Koji Kishimoto and 尚三山本 : 血小板および白血球の12-リポキシゲナーゼのcDNAクローニングと遺伝子発現., Proceedings of the Japanese Conference on the Biochemistry of Lipids, Vol.34, 402-406, 1992.

Academic Paper (Unrefereed Paper):

1.	N Mochizuki-Oda, Y Takeuchi, Koji Kishimoto and Y Watanabe : Cellular oxygen-sensing and potassium channels., The Japanese Journal of Physiology, Vol.50, S8, 2004.
2.	Koji Kishimoto and T Shimizu : Characterization of KIDScPLA2 and its role in the CNS., Journal of Pharmacological Sciences, Vol.94, No.1, 55, 2004.

Review, Commentary:

1.	Koji Kishimoto, 大日向英, 岸美紀子, 大嶋紀安, 立井一明 and 和泉孝志 : Oxidized free fatty acids as lipid mediators and functions of G2A as their receptor., Seikagaku, Vol.83, No.6, 545-554, Jun. 2011.

Proceeding of International Conference:

1.	(名) Nilofar, Kenshiro Katsura, Yoshitoshi Nakamura and Koji Kishimoto : Antioxidant activity of polyphenolic fraction of Shibataea kumasasa leaves, 2020 Sakura-Bio Meeting (On Line), Vol.ID 215 219 407, Online, Mar. 2020. (Keyword) lipophilic polyphenols
2.	M Araki, C Aso, C Aso, N Ohshima, K Tatei, T Hirano, S Sugimoto, M Kishi, Koji Kishimoto, H Obinata, H Obinata and T Izumi : Purification and characterization of a soluble diacylglycerol lipase from rat brain., 14th International Conference on Bioactive Lipids in Cancer, Inflammation and Related Diseases, Budapest, Hungary, Jul. 2015.
3.	M Araki, C Aso, N Ohshima, K Tatei, T Hirano, H Sugimoto, M Kishi, Koji Kishimoto and T Izumi : Identification and functional analysis of a novel diacylglycerol lipase from rat brain., The 6th International Conference on PLA2 and Lipid Mediators, Tokyo, Feb. 2015.
4.	C Isaji, T Kudo, N Ohshima, Y Yamashita, M Araki, A Honda, T Nagano, N Kato, A Konishi, Koji Kishimoto, K Tatei, N Yanaka and T Izumi : GDE4 and GDE7 produce lysophosphatidic acid by lisophospholipase D activity., The 6th International Conference on PLA2 and Lipid Mediators, Tokyo, Feb. 2015.
5.	T Yoshihara, M Hosaka, Koji Kishimoto, H Akiyama and S Tobita : Quantitative analysis of oxygen in living cells and tissues using Iridium (III) complexes with cationic substituent., 1st International Symposium of Gunma University Medical Innovation and 6th International Conference on Advanced Micro-Device Engineering (GUMI & AMDE), 62, Kiryu, Feb. 2014.
6.	Koji Kishimoto, T Haraguchi, K Shimizu, A Yamaguchi, T Yoshihara, N Ohshima, T Tatei, S Tobita, Y ida, Y Tsushima and T Izumi : 9-HODE-activated GPCR, G2A Regulates Stemness of Cancer Stem Cells in Human Astrocytoma Cell Lines., The Scripps Research Institute (invited speaker), San Diego, Nov. 2013.
7.	Koji Kishimoto, T Haraguchi, K Shimizu, A Yamaguchi, T Yoshihara, N Ohshima, T Tatei, S Tobita, Y ida, Y Tsushima and T Izumi : 9-HODE-activated GPCR, G2A induces epithelial-to-mesenchymal transition of human astrocytoma cells prior to generation of stem cell-like properties., Society of Neuroscience 2013, Vol.446, GG8, San Diego, Nov. 2013.
8.	A Yamaguchi, Y Iida, Y Fujisawa, S Inamoto, S Zhao, K Suzue, H Tominaga, Koji Kishimoto, T Higuchi, H Hisaeda, T Izumi, Y Kuge and Y Tsushima : Differentiation of malignant tumors from granulomas with dynamic [18F]-Fluoro-L-a-methyltyrosine PET imaging., European Association of Nuclear Medicine, Lyon, Oct. 2013.
9.	Koji Kishimoto, H Haraguchi, K Shimizu, A Yamaguchi, T Yoshihara, N Ohshima, T Tatei, S Tobita, Y Tsushima and T Izumi : Oxidized free fatty acids-activated GPCR, G2A regulates stemness and malignant behavior of an astrocytoma cell line., The Johns Hopkins University School of Medicine (invited speaker), Baltimore, Oct. 2012.
10.	Koji Kishimoto, H Haraguchi, K Shimizu, A Yamaguchi, T Yoshihara, N Ohshima, T Tatei, S Tobita, Y Tsushima and T Izumi : Oxidized free fatty acids-activated GPCR, G2A regulates stemness and malignant behavior of an astrocytoma cell line., Kennedy Krieger Institute (invited speaker), Baltimore, Oct. 2012.
11.	Koji Kishimoto, H Haraguchi, K Shimizu, A Yamaguchi, T Yoshihara, N Ohshima, T Tatei, S Tobita, Y Tsushima and T Izumi : Oxidized free fatty acids-activated GPCR, G2A regulates stemness and malignant behavior of an astrocytoma cell line., Society of Neuroscience 2012, Vol.558, R19, New Orleans, Oct. 2012.
12.	Koji Kishimoto, T Shirakawa, N Uozumi, T Izumi, H Kuroyanagi, Y Suzuki, T Shirasawa, K Nakadate, Y Watanabe and T Shimizu : A stimulus-dependent, dentate gyrus-specific novel phospholipase A2., Society for Neuroscience 31st Annual Meeting, San Diego, Nov. 2011.
13.	Y Takahashi, Y Kawakami, S Hirano, M Kinoshita, A Otsuki, TS Yamamoto, Y Kurahashi, H Daiyasu, H Toh, Koji Kishimoto, T Izumi and S Yamamoto : Expression of a single-chain antibody that neutralizes the effect of cysteinyl leukotrienes., 52nd International Conference on the Bioscience of Lipids, Warsaw, Aug. 2011.
14.	Koji Kishimoto, J Zhang, JA Kraus, RC Koehler and A Sapirsten : Cytosolic phospholipase A2 alpha modualtes early molecular events following cerebral ischemia and reperfusion in mice., Society for Neuroscience 38th Annual Meeting, Washington, D.C., Nov. 2008.
15.	Y Shen, Koji Kishimoto, DJ Linden and A Sapirstein : cPLA2 activity is required for the eletrophysiolosical sequelae of neurotoxic NMDA treatment in hippocampal CA1., Keystone Symposia on Eicosanoid in Inflammation and Chronic Diseases, Park City, Jan. 2006.
16.	Koji Kishimoto, SJ Texel, N Khodada, K Brady, J Klaus, K Kiber, S Dore, RC Koehler and A. Sapirstein : Cyclooxygenase-2 (COX-2) is regulated by cytosolic phospholinase A2 alfa (cPLA2 alpha)., Society for Neuroscience 35th Annual Meeting, Washington, D.C., Nov. 2005.
17.	K Yoshikawa, Koji Kishimoto, Y Kita and T Shimizu : Expression profiling of lipid mediators and their synthesizing enzymes after kainte-evoked seizure., 2nd International Conference Phospholipase A2 and 8th International Congress Platelet-Activating Factor and Related Lipid Mediators, Berlin, Oct. 2004.
18.	Koji Kishimoto, K Brady, SJ Texel and A Sapirstein : Cytosolic phospholipase A2 alpha in neuroinflammation., 2nd International Conference Phospholipase A2 and 8th International Congress Platelet-Activating Factor and Related Lipid Mediators, 111, Berlin, Oct. 2004.
19.	T Shimizu, N Uozumi, Y Kita, T Ohto, K Yoshikawa and Koji Kishimoto : Roles of cytosolic phospholipase A2 and related molecules in vitro and in vivo., 2nd International Conference Phospholipase A2 and 8th International Congress Platelet-Activating Factor and Related Lipid Mediators (special lecture), 93, Berlin, Oct. 2004.
20.	Koji Kishimoto, K Nakadate, A Sapirstein, H Kuroyanagi, T Houjou, N Uozumi, T Izumi, R Taguchi, T Shirasawa, Y Watanabe and T Shimizu : Kainate-inducible dentate gyrus specific (KIDS) phospholipase A2 is an endogenous neuroprotective protein., Society for Neuroscience 34th Annual Meeting, San Diego, Oct. 2004.
21.	Koji Kishimoto and T Shimizu : Role of an inducible, dentate gyrus specific phospholipase A2 in stroke., The Johns Hopkins University School of Medicine (invited speker), Baltimore, Nov. 2003.
22.	Koji Kishimoto, K Nakadate, T Shirasawa, T Izumi, N Uozumi, Y Watanabe and T Shimizu : Characterization of kainate-inducible, dentate gyrus-specific novel cytosolic phospholipase A2 (KIDScPLA2), Society for Neuroscience 33rd Annual Meeting, New Orleans, Nov. 2003.
23.	Koji Kishimoto, J Shirakawa, N Uozumi, T Izumi, H Kuroyanagi, Y Suzuki, T Shirasawa, K Nakadate, Y Watanabe and T Shimizu : Kainate-inducible dentate gyrus-specific novel cytosolic phospholipase A2., Society for Neuroscience 31st Annual Meeting, San Diego, Nov. 2001.
24.	Koji Kishimoto and T Shimizu : Kainate-inducible dentate gyrus-specific cytosolic phospholipase A2(KIDScPLA2)., University of California San Diego (invited speker), San Diego, Nov. 2001.
25.	Koji Kishimoto, K Brady, SJ Texel and A Sapirstein : Cytosolic phospholipase A2 alpha in neuroinflammation., 2nd International Conference Phospholipase A2 and 8th International Congress Platelet-Activating Factor and Related Lipid Mediators, Berlin, Oct. 2001.
26.	T Hirabayashi, Koji Kishimoto and T Shimizu : Cystenyl leukotriens activate microglia through the CysLT1 receptor., Seventh International Congress on Platelet-Activating Factor and Lipid Mediators, Tokyo, Sep. 2001.
27.	T Shimizu, N Uozumi, T Hirabayashi, T Shirakawa and Koji Kishimoto : Cytosolic phospholipase A2 and related molecules in the brain., Seventh International Congress on Platelet-Activating Factor and Lipid Mediators, Tokyo, Sep. 2001.
28.	T Hirabayashi, Koji Kishimoto and T Shimizu : Cystenyl leukotriens activate microglia through the CysLT1 receptor., Seventh International Congress on Platelet-Activating Factor and Lipid Mediators, Vol.67, 27-A-8, Tokyo, Sep. 2001.
29.	T Shimizu, N Uozumi, T Hirabayashi, T Shirakawa and Koji Kishimoto : Cytosolic phospholipase A2 and related molecules in the brain., Seventh International Congress on Platelet-Activating Factor and Lipid Mediators (special lecture), Vol.54, 26-B-10, Tokyo, Sep. 2001.
30.	Koji Kishimoto, M Ozaki, K Nakadate, LH X, H Kuroyanagi, Y Suzuki, T Shirasawa and Y Watanabe : A stimulus- and time-dependent, brain-specific novel phospholipase A2., Society for Neuroscience 29th Annual Meeting, Miami Beach, Oct. 1999.
31.	Koji Kishimoto, K Matsumura, Y Kataoka, H Morii and Y Watanabe : Localization of 85kDa cytosolic phospholipase A2 mRNA signals predominantly in neurons in rat brain., Society for Neuroscience 28th Annual Meeting, Los Angeles, Nov. 1998.
32.	S Yamamoto, H Suzuki, Koji Kishimoto, Michihiro Nakamura and Kazunori Ishimura : Arachidonate 12-lipoxygenase isozymes., International Conference on Lipoxygenases and Their Products: Biological Functions (special lecture), Vol.447, 37-44, St. Julians, May 1997.
33.	S Yamamoto, Koji Kishimoto, T Arakawa, Hiroshi Suzuki, Michihiro Nakamura, T Yoshimoto, T Takao, Y Shimonishi and T Tanabe : Arachidonate 12-lipoxygenases: Catalytic properties and regulation of the enzyme gene., Proceedings of The 5th International Conference on Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Related Diseases, Vol.407, 191-196, Feb. 1997.
34.	S Yamamoto, H Suzuki and Koji Kishimoto : Lipoxygenases: transformation of their hydroperoxy products., Pathophysiology of Lipid Peroxides and Related Free Radicals., Inuyama, Nov. 1996.
35.	S Yamamoto, Hiroshi Suzuki and Koji Kishimoto : Lipoxygenases: transformation of their hydroperoxy products., Symposium 'Pathophysiology of Lipid Peroxides and Related Free Radicals', Inuyama, Nov. 1996.
36.	S Yamamoto, Koji Kishimoto, T Arakawa, Hiroshi Suzuki, Michihiro Nakamura, T Yoshimoto, T Takao, Y Shimonishi and T Tanabe : Arachidonate 12-lipoxygenases Catalytic properties and regulation of the enzyme gene., Fourth International Conference on Eicosanoids and other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury (special lecture), Hong Kong, Oct. 1995.
37.	S Yamamoto, T Yoshimoto, N Ueda, Y Takahashi, S Matsuda, Hiroshi Suzuki, T Oshima, H Ikawa, T Hada, GR Reddy, Y Yamamoto, Koji Kishimoto, T Arakawa, K Ishimura, S Arase, C Yokoyama, T Tanabe, H Toh, M Nishiyama, H Okamoto, T Watanabe and T Hori : Arachidonate 12-lipoxygenases: enzymology and molecular biology., Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury 3rd International Conference (Special lecture), Washington, D.C., Oct. 1993.
38.	S Yamamoto, T Yoshimoto, Y Takahashi, Hiroshi Suzuki, T Arakawa, Koji Kishimoto, T Oshima, GR Reddy, N Ueda, J Murakami, Y Yamamoto, C Yokoyama, Yousuke Ebina, S Matsuda, Y Konishi, Y Mimura, S Arase and M Okuma : Mammalian lipoxygenases with special reference to arachidonate 12-lipoxygenase, Proceedings of The Fifth Scientific Meeting of the Society for Research on Polyunsaturated Fatty Acids, Vol.1025, 7-12, Jul. 1993.
39.	S Yamamoto, T Yoshimoto, Y Takahashi, H Suzuki, T Arakawa, Koji Kishimoto, T Oshima, GR Reddy, N Ueda, J Murakami, Y Yamamoto, C Yokoyama, Yousuke Ebina, S Matsuda, Y Konishi, Y Mimura, S Arase and M Okuma : Mammalian lipoxygenases with special reference to arachidonate 12-lipoxygenase., 5th Scientific Meeting of the Society for Research on Polyunsaturated Fatty Acid, Tokyo, Nov. 1992.
40.	S Yamamoto, T Yoshimoto, Y Takahashi, Hiroshi Suzuki, T Arakawa and Koji Kishimoto : Arachidonate 12-lipoxygenases., The 33rd International Conference on the Biochemistry of Lipids, Lyon, Sep. 1992.
41.	Hiroshi Suzuki, Koji Kishimoto, T Yoshimoto, S Yamamoto and Yousuke Ebina : Structure on iron-binding ligands of arachidonate 12-lipoxygenase of porcine leukocyte by site-directed mutagenesis., The 8th International conference on Prostaglandins and Related Compounds, Montreal, Jul. 1992.
42.	T Arakawa, T Oshima, Koji Kishimoto, T Yoshimoto and S Yamamoto : Molecular structure and function of porcine arachidonate 12-lipoxygenase gene., The 8th International conference on Prostaglandins and Related Compounds, Montreal, Jul. 1992.
43.	S Yamamoto, T Yoshimoto, Y Takahashi, H Suzuki, T Arakawa, Koji Kishimoto, T Hada, T Oshima, J Murakami, Y Yamamoto, C Yokoyama, Y Ebina, E Takahashi, S Matsuda, Y Konishi, Y Mimura and M Okuma : Biochemical and molecular biological approaches to two types of arachidonate 12-lipoxygenase, Proceedings of the 8th International Conference Prostaglandins and Related Compounds., Vol.6, 69-73, Jul. 1992.
44.	S Yamamoto, T Yoshimoto, N Ueda, S Takahashi, H Matsuda, H Suzuki, T Oshima, H Ikawa, T Hada, GR Reddy, Y Yamamoto, Koji Kishimoto, T Arakawa, K Ishimura, T Watanabe and T Hori : Arachidonate 12-lipoxygenases: Enzymology and molecular biology., Proceedings of The 2nd International Conference (Special lecture), Berlin, Sep. 1991.

Proceeding of Domestic Conference:

1.	Misuzu Nishida, Yuya Matsuda, Takahito Fukui, Mika Morihara, MD Abul Hassan, Yukio Nagasaki and Koji Kishimoto : Oxidized lipid receptors are involved in promoting tumor stem cell uptake activity., 第64回日本生化学会中国・四国支部例会, Vol.11:30, 2B13, May 2023.
2.	Takahito Fukui, Misuzu Nishida, Mika Morihara, Yuya Matsuda, Md Abul Hassan and Koji Kishimoto : Cancer cells gain resistance to therapy through compensatory autophagy, 第64回日本生化学会中国・四国支部例会, Vol.11:18, 2B12, May 2023.
3.	Daiti Kurisu, Misuzu Nishida, Takahito Fukui, Shiori Hirokawa, Miyu Nakai, ABUL MD HASSAN, Yukio Nagasaki and Koji Kishimoto : Cancer stem cells activate live cell-uptake in response to cellular stress, The 44th Annual Meeting of the Molecular Biology Society of Japan (Poster) (Yokohama), Nov. 2022. (Keyword) malignant tumor cells / tumor stem cells / living-cell engulfment / amino acid deprivation
4.	Daiti Kurisu, Misuzu Nishida, Takahito Fukui, Shiori Hirokawa, Miyu Nakai, ABUL MD HASSAN, Yukio Nagasaki and Koji Kishimoto : Cancer stem cells activate live cell-uptake in response to cellular stress, The 44th Annual Meeting of the Molecular Biology Society of Japan (Symposium) (Yokohama), Nov. 2022. (Keyword) malignant tumor cells / tumor stem cells / living-cell engulfment / amino acid deprivation
5.	Manami Yabumoto, Riho Satho, Taichi Kurisu, Misuzu Nishida, Takahito Fukui, Shiori Hirokawa and Koji Kishimoto : A mechanism of cell death resistance in response to a persisting autophagy inhibition in cancer cells, 44th Annual Meeting of Molecular Biology Society of Japan, 1223P-0575, Dec. 2021. (Keyword) autophagy
6.	Ayako Maita, Nobuo Maita, Yuushi Okumura, Takayuki Uchida, Reiko Nakao, Koji Kishimoto and Takeshi Nikawa : 高病原性インフルエンザ感染に関わる宿主酵素MSPLと阻害剤との複合体構造., 病態プロテアーゼ学会, Aug. 2018.
7.	Koji Kishimoto : 酸化作用が腫瘍細胞の悪性化を促進する., 平成30年度藍に関する研究プラットフォーム研究発表会(口頭), Jul. 2018.
8.	Koji Kishimoto, 原口崇, 清水健志, 清水健志 and 宮下知治 : 酸化脂質膜受容体であるヒトG2Aは脳腫瘍細胞の上皮間葉転換様プロセスを制御する, 第59回日本生化学会中国四国支部会プログラム講演要(口頭), 85, May 2018.
9.	Koji Kishimoto, Takashi Hraguchi, Kenji Shimizu, Ide Munenori, Miyashita Tomoharu, Ohno Ayako, Takeshi Nikawa and Izumi Tkashi : An oxidazed lipids-membrane receptor, human G2A regulates epithelial-mesenchymal transition-like proces of glioma cells., 第59回日本生化学会中国四国支部例会(口頭), 85, May 2018. (Keyword) G2A / 酸化脂質
10.	Koji Kishimoto, T Hraguchi, K Shimizu and T Izumi : An oxidazed lipids-membrane receptor, human G2A regulates epithelial-mesenchymal transition-like proces of glioma cells., 第76回日本癌学会学術総会(口頭), Sep. 2017. (Keyword) G2A / oxidized lipids / epithelial-mesenchy,al transition-like process
11.	Koji Kishimoto, T Hraguchi, K Shimizu and T Izumi : An oxidazed lipids-membrane receptor, human G2A regulates epithelial-mesenchymal transition-like proces of glioma cells., Proceeding of The 76th Annual Meeting of the Japanese Cancer Association, P3115, Sep. 2017. (Keyword) G2A / oxidized lipids / epithelial-mesenchy,al transition-like process
12.	Norio Kamemura, Sara Murakami, Hiroaki Komatsu, Masahiro Sawanoi, Kenji Miyamoto, 石堂一巳, Koji Kishimoto, Akihiko Tsuji and Keizo Yuasa : 軟骨形成におけるcGMP-dependent protein kinase Ⅱの作用機構の探索., 第58回日本生化学会中国・四国支部例会, May 2017.
13.	Koji Kishimoto, Takashi Hraguchi, Kenji Shimizu, Aiko Yamaguchi, Toshitada Yoshihara, Mikiko Kishi, Munenori Ide, Tetsunari Oyama, Yoshito Tsushima, Seishi Yobita, Akihiko Tsuji and Takashi Izumi : A GPCR, G2A, regulates stemness of cancer stem cells, 第56回日本生化学会中国四国支部例会(口頭), 16, May 2015.
14.	Koji Kishimoto, 原口崇, 清水健志, 山口藍子, 吉原利忠, 井出宗則, 小山徹也, 対馬義人, 飛田成史 and 和泉孝志 : 酸化脂質をリガンドとするGPCR, G2Aは幹細胞性制御に関わる., 第12回がんとハイポキシア研究会 2014, Nov. 2014.
15.	大嶋紀安, 荒木麻理, 麻生千寿, 立井一明, Koji Kishimoto and 和泉孝志 : ラット脳ジアシルグリセロールリパーゼの精製と機能解析, 生体情報研究シンポジウム, Aug. 2014.
16.	Koji Kishimoto, 原口崇, 清水健志, 山口藍子, 井出宗則, 吉原利忠, 大嶋紀安, 飯田靖彦, 飛田成史, 対島義人, 小山徹也 and 和泉孝志 : Gタンパク質共役型受容体，G2Aが制御する幹細胞性と上皮間葉転換., 第23回日本がん転移学会学術集会総会(シンポジウム講演者), 64, Jul. 2014.
17.	Koji Kishimoto, 原口崇, 清水健志, 山口藍子, 吉原利忠, 大島紀安, 立井一明, 飛田成史, 飯田靖彦, 対島義人 and 和泉孝志 : Gタンパク質共役型受容体，G2Aはヒトアストロサイトーマ細胞株のがん幹細胞性を制御する., 第86回日本生化学会大会(口頭), Sep. 2013.
18.	Koji Kishimoto, 原口崇, 清水健志, 山口藍子, 吉原利忠, 大島紀安, 立井一明, 飛田成史, 飯田靖彦, 対島義人 and 和泉孝志 : Gタンパク質共役型受容体，G2Aはヒトアストロサイトーマ細胞株のがん幹細胞性を制御する., 平成25年度日本生化学会関東支部例会(シンポジウム講演者), Jun. 2013.
19.	荒木麻理, 麻生知寿, 大嶋紀安, 立井一明, 立井一明, 平野瞳子, 杉本博之, 岸美紀子, Koji Kishimoto and 和泉孝志 : 新規脳ジアシルグリセロールリパーゼの同定., 第55回日本脂質生化学会, Jun. 2013.
20.	吉原利忠, 飛田成史, Koji Kishimoto, 和泉孝志, 秋山英雄 and 岸章治 : 発光測定に基づく低酸素細胞・組織イメージング技術の開発と医学応用., 平成25年度医理工連携シーズシンポジウム, Jun. 2013.
21.	吉原利忠, 飛田成史, Koji Kishimoto, 和泉孝志, 秋山英雄 and 岸章治 : 発光測定に基づく低酸素細胞・組織イメージング技術の開発と医学応用., 平成25年度医理工連携シーズシンポジウム, Apr. 2013.
22.	原口崇, 清水健志, Koji Kishimoto, 大嶋紀安, 立井一明 and 和泉孝志 : ヒトアストロサイトーマU251細胞の幹細胞性と上皮間葉転換制御に関わるG2Aの役割., 第85回日本生化学会大会, Dec. 2012.
23.	平野詩織, 木下麻衣, 大槻朱美, 下田一花, 川上祐生, Toshiko Suzuki-Yamamoto, 鈴木麻紀子, 青山沙絵, 木本眞順美, 福島光夫, Koji Kishimoto, 和泉孝志, 小賀徹, 成宮周, 吉本谷博, 山本尚三 and 高橋吉孝 : 抗ロイコトリエンC4モノクローナル抗体とその単鎖抗体によるロイコトリエン中和作用., 第85回日本生化学会大会, Dec. 2012.
24.	平野詩織, 木下麻衣, 大槻朱美, 川上祐生, Toshiko Suzuki-Yamamoto, Koji Kishimoto, 和泉孝志, 尚三山本 and 高橋吉孝 : ロイコトリエンに対する単鎖抗体を利用した抗体治療薬開発に向けた基礎研究., 第44回日本栄養・食糧学会中国・四国支部大会, Nov. 2012.
25.	Koji Kishimoto, 谷畑貴俊, 原口崇, 清水健志, 山口藍子, 吉原利忠, 大島紀安, 立井一明, 飛田成史, 対馬義人 and 和泉孝志 : G2Aはアストロサイトーマ細胞の幹細胞性と悪性度を制御する., 第71回日本癌学会学術総会(口頭), Sep. 2012.
26.	Koji Kishimoto, T Yabata, T Haraguchi, K Shimizu, A Yamaguchi, T Yoshihara, N Oshima, K Tatei, S Tobita, Y Tsushima and T Izumi : G2A regulates stemness and malignant behavior of astrocytoma cells., Proceedings of 71st Annual Meeting of the Japanese Cancer Association, Vol.288, J2101, Sep. 2012.
27.	大嶋紀安, 荒木麻理, Koji Kishimoto, 岸美紀子, 立井一明 and 和泉孝志 : 表面プラズモン共鳴現象を利用した効率的なGPCRリガンドスクリーニング方法, 平成24年度日本生化学会関東支部会, Jun. 2012.
28.	Koji Kishimoto, 谷畑貴俊, 原口崇, 清水健志, 山口藍子, 吉原利忠, 大島紀安, 立井一明, 飛田成史, 対馬義人 and 和泉孝志 : がん幹細胞性制御におけるG2Aの役割., 平成24年度日本生化学会関東支部例会(シンポジウム講演者), Jun. 2012.
29.	Koji Kishimoto, 谷畑貴俊, 原口崇, 清水健志, 大島紀安, 立井一明 and 和泉孝志 : Gタンパク質共役型受容体，G2Aを介したがん幹細胞性制御., 第54回日本脂質生化学会(口頭), May 2012.
30.	川上祐生, 平野詩織, 木下麻衣, 大槻朱美, 下田一花, 鈴木麻希子, 青山沙絵, Toshiko Suzuki-Yamamoto, 木本眞順美, 福島光夫, Koji Kishimoto, 和泉孝志, 小賀徹, 成宮周, 吉本谷博, 尚三山本 and 高橋吉孝 : ロイコトリエン作用に対する抗ロイコトリエンC4単鎖抗体の中和効果., 第54回日本脂質生化学会, May 2012.
31.	Koji Kishimoto and 和泉孝志 : グリオーマ細胞におけるG2Aを介した形質変化の制御., 群馬大学・秋田大学連携グローバル COE 若手シンポジウム(シンポジウム講演者), Nov. 2011.
32.	平野詩織, 木下麻衣, 大槻朱美, 川上祐生, Toshiko Suzuki-Yamamoto, Koji Kishimoto, 和泉孝志, 尚三山本 and 高橋吉孝 : ロイコトリエンに対する単鎖抗体を利用した抗体治療薬開発に向けた基礎研究., 第44回日本栄養・食糧学会中国・四国支部大会, Nov. 2011.
33.	Koji Kishimoto, RC Li, S Doré, RC Koehler, A Sapirstein and T Izumi : Cytosolic phospholipase A2 alpha amplifies early cyclooxygenase-2 expression, oxidative stress and MAP kinase phosphorylation after cerebral ischemia in mice., 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(口頭), Nov. 2011.
34.	Koji Kishimoto, 谷畑貴俊, 原口崇, 大嶋紀安, 立井一明 and 和泉孝志 : G2Aは神経膠腫細胞株U251に栄養飢餓及び低酸素刺激に対する抵抗性を賦与する., 第84回日本生化学会大会(口頭), Sep. 2011.
35.	川上祐生, 平野詩織, Toshiko Suzuki-Yamamoto, 倉橋優子, Koji Kishimoto, 和泉孝志, 小賀徹, 成宮周, 尚三山本 and 高橋吉孝 : 抗ロイコトリエンC4モノクローナル抗体とその単鎖抗体によるロイコトリエン中和作用., 第84回日本生化学会大会, Sep. 2011.
36.	大嶋紀安, 岡崎優利, 吉澤郁美, 亀井康富, Mariggiò S, 岡本佳子, 立井一明, Koji Kishimoto, 小川佳宏, 加藤範久, Corda D, 矢中規之 and 和泉孝志 : 哺乳動物のGDE群とマウスGDE5の非酵素的機構による骨格筋分化制御., 第53回日本脂質生化学会, May 2011.
37.	大嶋紀安, 青木公洋, 立井一明, 平野瞳子, Koji Kishimoto and 和泉孝志 : pColdベクターを用いた5-リポキシゲナーゼ (5-LO)の大量発現と精製., 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, Nov. 2010.
38.	MI Barliana, M KISHI, H Oninata, A Ogawa, Koji Kishimoto, N Ohshima, K Tatei and T Izumi : Novel function of 9(S)-hydroxyoctadecadienoic acid on proliferation of T cells., 第52回日本脂質生化学会大会, May 2010.
39.	Koji Kishimoto, RC Li, S Doré, RC Koehler, A Sapirstein and T Izumi : Cytosolic phospholipase A2 alpha amplifies early cyclooxygenase-2 expression, oxidative stress and MAP kinase phosphorylation after cerebral ischemia in mice., 第83回日本生化学会大会(口頭), 2010.
40.	吉川圭介, Koji Kishimoto, 北芳博 and 清水孝雄 : てんかん様痙攣刺激による脂質メディエーター及びその産生分子群の発現プロファイリング., 第46回脂質生化学会, May 2004.
41.	Koji Kishimoto and 清水孝雄 : カイニン酸刺激による脂質メディエーター産生分子の動態とその役割., 第77回日本薬理学会年会(シンポジウム講演者), Mar. 2004.
42.	平林哲也, Koji Kishimoto, 清水孝雄, 魚住尚紀, 渡辺恭良 and 清水孝雄 : ミクログリアの機能と脂質メディエーター, 戦略的基礎研究推進事業科学技術振興事業団研究領域「脳を知る」シンポジウム, Oct. 2003.
43.	Koji Kishimoto, 中館和彦, 白澤卓二, 魚住尚紀, 渡辺恭良 and 清水孝雄 : KIDScPLA2の中枢神経における役割, 戦略的基礎研究推進事業科学技術振興事業団研究領域「脳を知る」シンポジウム, Oct. 2003.
44.	平林哲也, Koji Kishimoto and 清水孝雄 : ロイコトリエンD4受容体を介したミクログリアの活性制御., 戦略的基礎研究推進事業科学技術振興事業団研究領域「脳を知る」合同シンポジウム''脳神経科学の最先端2002'', Nov. 2002.
45.	Koji Kishimoto, 魚住尚紀, 和泉孝志, 黒柳秀人, 白澤卓二, 中館和彦, 渡辺恭良 and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2(KIDScPLA2)の酵素学的検討., 戦略的基礎研究推進事業科学技術振興事業団研究領域「脳を知る」合同シンポジウム''脳神経科学の最先端2002''(シンポジウム講演者), Nov. 2002.
46.	Koji Kishimoto and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2 (KIDScPLA2)の神経機能に果たす役割の探索., 第75回日本生化学会大会(シンポジウム講演者), Oct. 2002.
47.	平林哲也, Koji Kishimoto, 小笠原英明, 和泉孝志 and 清水孝雄 : ロイコトリエンD4によるミクログリアの活性制御., 第74回日本生化学会大会, Oct. 2001.
48.	白川純, Koji Kishimoto, 魚住尚紀, 和泉孝志, 黒柳秀人, 鈴木陽一, 白澤卓二, 中舘和彦, 渡辺恭良 and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2 (KIDScPLA2)の酵素学的性質の検討., 第74回日本生化学会大会, Oct. 2001.
49.	Koji Kishimoto, 白川純, 魚住尚紀, 和泉孝志, 黒柳秀人, 鈴木陽一, 白澤卓二, 中舘和彦, 渡辺恭良 and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2(KIDScPLA2)., 第74回日本生化学会大会(シンポジスト講演者), Oct. 2001.
50.	Koji Kishimoto, 魚住尚紀, 和泉孝志, 白川純 and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2アイソフォーム., 戦略的基礎研究推進事業科学技術振興事業団科学技術振興事業団(JST)戦略的基礎研究推進事業科学技術振興事業団 (CREST)「脳を知る」「脳を守る」合同シンポジウム(シンポジスト講演者), Jun. 2001.
51.	Koji Kishimoto, 魚住尚紀, 和泉孝志, 清水孝雄, 黒柳秀人, 鈴木陽一, 白澤卓二, 中館和彦 and 渡辺恭良 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2アイソフォーム., 第73回日本生化学会大会(シンポジウム講演者), Oct. 2000.
52.	小田-望月紀子, 竹内裕子, Koji Kishimoto and 渡辺恭良 : 細胞における酸素センサーとK+チャネル., 第77回日本生理学会大会, Mar. 2000.
53.	Koji Kishimoto, 尾崎仁士, 中舘和彦, 許麗華, 黒柳秀人, 鈴木陽一, 白澤卓二 and 渡辺恭良 : 刺激依存性・時期特異的・脳特異的新規ホスホリパーゼA2., 第72回日本生化学会大会(シンポジウム講演者), Oct. 1999.
54.	B Langstrom, M Bergstrom, KJ Fasth, U Yngve, L Samuelsson, F Karimi, F Wu, L Lu, E Bergstrom, W Sihver, Koji Kishimoto and Y Watanabe : Novel molecular probes for in vivo measurements of cell proliferation, antisense oligonucleotides pharmacokinetics and receptor occupancy in cholinergic and neurokinin systems using PET., 第22回日本神経科学大会, Jul. 1999.
55.	Koji Kishimoto, 松村潔, 森井博史 and 渡辺恭良 : 85kDa細胞質型ホスホリパーゼA2の正常ラット脳神経細胞での発現., 第71回日本生化学会大会(口頭), Oct. 1998.
56.	Koji Kishimoto, 松村潔, 片岡洋祐, 森井博史 and 渡辺恭良 : 85kDa細胞質型ホスホリパーゼA2の正常ラット脳神経細胞での発現., 第21回日本神経科学,第41回日本神経科学合同大会(口頭), Sep. 1998.
57.	Hiroshi Suzuki, Koji Kishimoto and 尚三山本 : アラキドン酸酸素添加酵素の自殺的失活., 第39回日本脂質生化学研究会研究集会, Jun. 1997.
58.	Hiroshi Suzuki, Koji Kishimoto and S Yamamoto : Lipoxygenase-Catalyzed Transformation of Its Primry Hydroperoxy Product., 第20回日本過酸化脂質フリ-ラジカル学会, Nov. 1996.
59.	S Ymamaoto, Hiroshi Suzuki and Koji Kishimoto : Lipoxygenase-Catalyzed Transformation of Its Primry Hydroperoxy Product., 第20回日本過酸化脂質フリ-ラジカル学会, Nov. 1996.
60.	Koji Kishimoto, Hiroshi Suzuki, Michihiro Nakamura, 吉本谷博, 尚三山本, 高尾敏文, 下西康嗣 and 田辺忠 : ブタ白血球12-リポキシゲナーゼの自殺的失活と酵素蛋白への15-ヒドロペルオキシエイコサテトラエン酸の取り込み., 第38回日本脂質生化学研究会研究集会, Jun. 1996.
61.	Koji Kishimoto, Michihiro Nakamura, Hiroshi Suzuki, 吉本谷博, 尚三山本, 高尾敏文, 下西康嗣 and 田辺忠 : 15-ヒドロペルオキシエイコサテトラエン酸のブタ白血球12-リポキシゲナーゼへの取り込みと酵素の自殺的失活., 第19回日本過酸化脂質フリ-ラジカル学会, Nov. 1995.
62.	Koji Kishimoto, Michihiro Nakamura, Michihiro Nakamura, Hiroshi Suzuki, 尚三山本, 高尾敏文, 下西康嗣 and 田辺忠 : 15S-ヒドロペルオキシエイコサテトラエン酸のブタ白血球12-リポキシゲナーゼへの取り込み., 第68回日本生化学会大会(口頭), Oct. 1995.
63.	Koji Kishimoto, Michihiro Nakamura, Hiroshi Suzuki, 吉本谷博, 尚三山本, 高尾敏文, 下西康嗣 and 田辺忠 : ブタ白血球12-リポキシゲナーゼの自殺的失活と酵素蛋白への15-ヒドロペルオキシエイコサテトラエン酸の取り込み., 第19回日本過酸化脂質フリ-ラジカル学会, Jul. 1995.
64.	吉本谷博, Hiroshi Suzuki, 荒川俊哉, Koji Kishimoto and 尚三山本 : ブタ白血球のアラキドン酸 12-リポキシゲナーゼの位置特異的変異法による活性部位の検討と遺伝子の構造., 第18回日本過酸化脂質フリ-ラジカル学会, Sep. 1994.
65.	Hiroshi Suzuki, Koji Kishimoto, 吉本谷博, 尚三山本, 金井文彦, Yousuke Ebina, 宮武明 and 田辺忠 : 12-リポキシゲナーゼの鉄含有量に与えるヒスチジン残基部位特異的変異の影響., 第66回日本生化学会大会, Oct. 1993.
66.	吉本谷博, Hiroshi Suzuki, Koji Kishimoto, 尚三山本, 金井文彦, Yousuke Ebina, 宮武明 and 田辺忠 : アラキドン酸12-リポキシゲナーゼ反応におけるヒスチジン残基の役割., 第17回日本過酸化脂質フリ-ラジカル学会, Oct. 1993.
67.	Hiroshi Suzuki, Koji Kishimoto, 吉本谷博, 山本尚三, 金井文彦, Yousuke Ebina, 宮武明 and 田辺忠 : ブタ白血球のアラキドン酸12-リポキシゲナーゼの部位特異的変異法による解析., 第35回日本脂質生化学研究会研究集会, Jun. 1993.
68.	吉本谷博, Hiroshi Suzuki, 荒川俊哉, Koji Kishimoto, 山本恵史, 大島岳夫, 羽田尚彦 and 山本尚三 : アラキドン酸 12-リポキシゲナーゼの遺伝子クローニング., 第65回日本生化学会大会, Oct. 1992.
69.	Hiroshi Suzuki, Koji Kishimoto, 吉本谷博, 尚三山本 and Yousuke Ebina : ブタ白血球の 12-リポキシゲナーゼの鉄結合部位に関する検討., 第65回日本生化学会大会(本人口頭), Oct. 1992.
70.	Hiroshi Suzuki, Koji Kishimoto, 吉本谷博, 尚三山本 and Yousuke Ebina : 12-リポキシゲナーゼへの酸素添加部位を決定するアミノ酸残基の検索., 第65回日本生化学会大会, Oct. 1992.
71.	吉本谷博, Hiroshi Suzuki, 荒川俊哉, Koji Kishimoto and 尚三山本 : 血小板および白血球の12-リポキシゲナーゼのcDNAクローニングと遺伝子発現., 第34回日本脂質生化学研究会研究集会, Vol.34, 402-406, Jun. 1992.
72.	荒川俊哉, 大島岳夫, Koji Kishimoto, Hiroshi Suzuki, 吉本谷博 and 尚三山本 : ブタ白血球 12-リポキシゲナーゼの遺伝子クローニング., 第64回日本生化学会大会, Oct. 1991.
73.	Koji Kishimoto, 辻昭彦, Yoshiko Matsuda and 勝沼信彦 : ラットジストロフィンの精製とタンパク特性, 第63回日本生化学会大会(口頭), Sep. 1990.

Et cetera, Workshop:

1.	Koji Kishimoto : 細胞周囲の電子環境を人為的に調整することで細胞の幹細胞性を制御できるか, 一般財団法人電力中央研究所 (招待講演), Nov. 2014.
2.	Koji Kishimoto : 幹細胞性を制御するGタンパク質共役受容体に関する研究–酸化脂質と細胞分化に関する基礎的研究, 同志社女子大学, Oct. 2014.
3.	Koji Kishimoto, 和泉孝志 and 小西昭充 : 皮膚科学におけるG2Aの役割, 資生堂リサーチセンター, Jul. 2013.
4.	Koji Kishimoto, 白川純, 魚住尚紀 and 清水孝雄 : Kainate-inducible Dentate gyrus-Specific cPLA2 (KIDScPLA2)., 第4回東京プロスタノイド研究会(招待講演者), Oct. 2001.

Report:

1.	Misuzu Nishida, Takahito Fukui, Yukio Nagasaki and Koji Kishimoto : がん幹細胞が生残勝者となる新規機序を利用したPD-1 経路阻害の奏功率を高める併用法の開発, 令和4年度産学連携研究者育成支援事業(事業化推進研究者育成支援) 研究成果報告会, Jul. 2023.
2.	Koji Kishimoto, 白川純, 魚住尚紀, 和泉孝志, 黒柳秀人, 鈴木陽一, 白澤卓二, 中館和彦, 渡邊恭良 and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2 (KIDSScPLA2)., 老人研情報 2001年度業績特集号, 23, Jul. 2018.
3.	白川純, Koji Kishimoto, 魚住尚紀, 和泉孝志, 黒柳秀人, 鈴木陽一, 白澤卓二, 中館和彦, 渡邊恭良 and 清水孝雄 : 刺激依存性・海馬歯状回特異的新規ホスホリパーゼA2 (KIDSScPLA2)の酵素学的性質の検討., 老人研情報 2001年度業績特集号, 23, Jul. 2018.
4.	Koji Kishimoto, 清水孝雄 and 渡辺恭良 : カルシウム非依存性である新規なホスホリパーゼA2，その遺伝子及びそのプロモーター (米国)., 社会技術研究開発事業追跡調査報告書, 58, Apr. 2013.
5.	清水孝雄, Koji Kishimoto and 渡辺恭良 : カルシウム非依存性である新規なホスホリパーゼA2，その遺伝子及びそのプロモーター (日本)., 社会技術研究開発事業追跡調査報告書, 58, Apr. 2013.
6.	Koji Kishimoto, 魚住尚紀, 和泉孝志, 白川純, 清水孝雄, 黒柳秀人, 鈴木陽一, 白澤卓二, 中館和彦 and 渡辺恭良 : 刺激依存性・海馬歯状回特異的新規ホスホリバーゼA2 アイソフォーム., 「脳を知る」・「脳を守る」合同シンポジウム要旨脳の機能とその異常報告書, 22, Dec. 2002.

Patent:

1.	清水孝雄, Koji Kishimoto and 渡辺恭良 : カルシウム非依存性である新規なホスホリパーゼA2，その遺伝子およびそのプロモーター, 200796910(P200796910) (Apr. 2007), 2007222175(P2007222175A) (Sep. 2007), 4166811(P4166811) (Aug. 2008).
2.	清水孝雄, Koji Kishimoto and 渡辺恭良 : カルシウム非依存性である新規なホスホリパーゼA2，その遺伝子およびそのプロモーター, 200246953(P2002-46953) (Feb. 2003), 200333190(P200333190A) (Jul. 2007), 4119136(P4119136) (Jul. 2008).
3.	Koji Kishimoto, Shimizu Takao and Watanabe Yasuyoshi : NOVEL CALCIUM-INDEPENDENT PHOSPHOLIPASES A2, GENES THEREOF AND PROMOTER OF THE SAME, :PCT2001JP006071; : 10/468,519 (Jul. 2001), :WO 02/066655 A1 (Aug. 2002), 7332318(P7332318) (Jan. 2006).

Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)

Determining the molecular mechanisms allow cancer stem cells to retain a survival advantage under starvation conditions. (Project/Area Number: 22K06613 )
Alarm signal by dead cells activated progressive properties of tumor cells. (Project/Area Number: 16K01360 )
Studies on G protein-coupled receptor controlling cell cycle and stemness (Project/Area Number: 24390069 )
Analysis of receptor signaling in living cells by surface plasmon resonance (Project/Area Number: 23659106 )
Search by Researcher Number (50280699)

Associate Professor : Kishimoto, Koji

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Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)