Tokushima University / Educator and Researcher Directory --- Hiasa, Masahiro

Personal Web Page

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

https://orcid.org/0000-0002-4830-6274 (ORCID)

Field of Study

○	Dentistry

Subject of Study

○

Book / Paper

Academic Paper (Judged Full Paper):

1.	Yuta Matsuki, Masahiro Hiasa, Shigeki HANAWA, Motosumi NAKAGAWA, Shinya Horiuchi and Eiji Tanaka : A case of anterior open bite associated with idiopathic condylar resorption treated with miniscrew-assisted orthodontics, AJO-DO Clinical Companion, Vol.4, No.3, 211-228, 2024. (Tokushima University Institutional Repository) ● Metadata: 119698 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.xaor.2024.04.002 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.xaor.2024.04.002 (Tokushima University Institutional Repository: 119698, DOI: 10.1016/j.xaor.2024.04.002)
2.	Kimiko Sogabe, Shingen Nakamura, Yoshiki Higa, Hirokazu Miki, Asuka Oda, Tomoko Maruhashi, Ryohei Sumitani, Masahiro Oura, Mamiko Takahashi, Masafumi Nakamura, Yusaku Maeda, Tomoyo Hara, Hiroki Yamagami, Shiroh Fujii, Kumiko Kagawa, Shuji Ozaki, Kiyoe Kurahashi, Itsuro Endo, Ken-ichi Aihara, Emiko Nakaue, Masahiro Hiasa, Jumpei Teramachi, Takeshi Harada and Masahiro Abe : Acute accumulation of PIM2 and NRF2 and recovery of β5 subunit activity mitigate multiple myeloma cell susceptibility to proteasome inhibitors., International Journal of Hematology, Vol.119, No.3, 303-315, 2024. (Summary) Resistance to proteasome inhibitors (PIs) has emerged as an important clinical issue. We investigated the mechanisms underlying multiple myeloma (MM) cell resistance to PIs. To mimic their pharmacokinetic/pharmacodynamic (PK/PD) profiles, MM cells were treated with bortezomib and carfilzomib for 1 h at concentrations up to 400 and 1,000 nM, respectively. Susceptibility to these PIs markedly varied among MM cell lines. Pulsatile treatments with PIs suppressed translation, as demonstrated by incorporation of puromycin at 24 h in PI-susceptible MM.1S cells, but not PI-resistant KMS-11 cells. Inhibition of β5 subunit activity decreased at 24 h in KMS-11 cells, even with the irreversible PI carfilzomib, but not under suppression of protein synthesis with cycloheximide. Furthermore, the proteasome-degradable pro-survival factors PIM2 and NRF2 acutely accumulated in MM cells subjected to pulsatile PI treatments. Accumulated NRF2 was trans-localized into the nucleus to induce the expression of its target gene, HMOX1, in MM cells. PIM and Akt inhibition restored the anti-MM effects of PIs, even against PI-resistant KMS-11 cells. Collectively, these results suggest that increased synthesis of β5 proteasome subunit and acute accumulation of PIM2 and NRF2 reduce the anti-MM effects of PIs. (Keyword) Humans / Proteasome Inhibitors / NF-E2-Related Factor 2 / Multiple Myeloma / Proteasome Endopeptidase Complex / Drug Resistance, Neoplasm / Cell Line, Tumor / Bortezomib / Antineoplastic Agents / Proto-Oncogene Proteins / Protein Serine-Threonine Kinases (Tokushima University Institutional Repository) ● Metadata: 119384 (Link to Publication Site) ● Publication site (DOI): 10.1007/s12185-023-03705-9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38245883 ● Search Scopus @ Elsevier (PMID): 38245883 ● Search Scopus @ Elsevier (DOI): 10.1007/s12185-023-03705-9 (Tokushima University Institutional Repository: 119384, DOI: 10.1007/s12185-023-03705-9, PubMed: 38245883)
3.	TANAKA Mariko, Shinya Horiuchi, Masahiro Hiasa, Keiichiro Watanabe, Akihiko Iwasa, Natsumi Takamaru, Hirokazu Nagai, Youji Miyamoto and Eiji Tanaka : 術後に顎関節に疼痛を訴えた顎偏位を伴う骨格性上顎前突症例, The Journal of Chu-Shikoku Orthodontic Society, Vol.35, No.1, 77-86, 2023.
4.	HANAWA Shigeki, Masahiro Hiasa, Akihiko Iwasa, Keiichiro Watanabe, Hirofumi Tenshin, Nao Kinouchi, Shinya Horiuchi and Eiji Tanaka : 上顎左側第二小臼歯先天欠如を伴う片側性唇顎口蓋裂患者に対して下顎左側第二小臼歯を移植した一症例．, The Journal of Chu-Shikoku Orthodontic Society, Vol.35, No.1, 67-76, 2023. (Keyword) 中・四国矯正歯科学会雑誌 35(1):67-76.
5.	Keiichiro Watanabe, A Tichy, Kouhei Kamoi, Masahiro Hiasa, Kazuhide Yonekura, Eiji Tanaka, M Nakajima and Keiichi Hosaka : Restoration of a Microdont Using the Resin Composite Injection Technique With a Fully Digital Workflow: A Flexible 3D-printed Index With a Holding Clip., Operative Dentistry, 2023. (Summary) Direct composite restorations are accepted as a treatment option for microdontia, which is a relatively prevalent condition that poses esthetic concerns. While free-hand composite placement is technique-sensitive and time-consuming, the resin composite injection technique is more straightforward and predictable. A fully digital workflow has been recently introduced, but the 3D-printed resin index is rigid and challenged by undercuts, as opposed to the silicone index. This case report presents a flexible 3D-printed resin index, which can accurately transfer the digitally simulated functional and esthetic form to the final restoration. In addition, a rigid holding clip was designed to stabilize the flexible index. (Link to Publication Site) ● Publication site (DOI): 10.2341/23-007 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37503684 ● Search Scopus @ Elsevier (PMID): 37503684 ● Search Scopus @ Elsevier (DOI): 10.2341/23-007 (DOI: 10.2341/23-007, PubMed: 37503684)
6.	Ryoko Shioyasono, Atsushi Shioyasono, Ayami Ito, Kaoru Yoshinaga, Soichiro Kinjo, Keiichiro Watanabe, Masahiro Hiasa, Natsumi Takamaru and Eiji Tanaka : A patient with unilateral posterior crossbite treated with modified unilateral surgically-assisted rapid maxillary expansion., AJO-DO Clinical Companion, Vol.3, No.2, 149-162, 2023. (Tokushima University Institutional Repository) ● Metadata: 119697 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.xaor.2023.02.001 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.xaor.2023.02.001 (Tokushima University Institutional Repository: 119697, DOI: 10.1016/j.xaor.2023.02.001)
7.	Emiko Nakaue, Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Takeshi Harada, Asuka Oda, Yusuke Inoue, Sou Shimizu, Yoshiki Higa, Kimiko Sogabe, Masahiro Oura, Tomoyo Hara, Ryohei Sumitani, Tomoko Maruhashi, Hiroki Yamagami, Itsuro Endo, Eiji Tanaka and Masahiro Abe : Mechanisms of preferential bone formation in myeloma bone lesions by proteasome inhibitors., International Journal of Hematology, 2023. (Summary) Proteasome inhibitors (PIs) can preferentially restore bone in bone-defective lesions of patients with multiple myeloma (MM) who respond favorably to these drugs. Most prior in vitro studies on PIs used continuous exposure to low PI concentrations, although pharmacokinetic analysis in patients has shown that serum concentrations of PIs change in a pulsatile manner. In the present study, we explored the effects of pulsatile treatment with PIs on bone metabolism to simulate in vivo PI pharmacokinetics. Pulsatile treatment with bortezomib, carfilzomib, or ixazomib induced MM cell death but only marginally affected the viability of osteoclasts (OCs) with F-actin ring formation. Pulsatile PI treatment suppressed osteoclastogenesis in OC precursors and bone resorption by mature OCs. OCs robustly enhanced osteoblastogenesis in cocultures with OCs and MC3T3-E1 pre-osteoblastic cells, indicating OC-mediated coupling to osteoblastogenesis. Importantly, pulsatile PI treatment did not impair robust OC-mediated osteoblastogenesis. These results suggest that PIs might sufficiently reduce MM cell-derived osteoblastogenesis inhibitors to permit OC-driven bone formation coupling while suppressing OC differentiation and activity in good responders to PIs. OC-mediated coupling to osteoblastogenesis appears to be a predominant mechanism for preferential occurrence of bone regeneration at sites of osteoclastic bone destruction in good responders. (Tokushima University Institutional Repository) ● Metadata: 118380 (Link to Publication Site) ● Publication site (DOI): 10.1007/s12185-023-03601-2 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37039914 ● Search Scopus @ Elsevier (PMID): 37039914 ● Search Scopus @ Elsevier (DOI): 10.1007/s12185-023-03601-2 (Tokushima University Institutional Repository: 118380, DOI: 10.1007/s12185-023-03601-2, PubMed: 37039914)
8.	Ryoko Shioyasono, Kaoru Yoshinaga, Atsushi Shioyasono, Ayami Ito, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : Nonsurgical orthodontic treatment for a patient with Sotos syndrome., American Journal of Orthodontics and Dentofacial Orthopedics (AJO-DO), Vol.163, No.3, 426-442, 2023. (Summary) Sotos syndrome is a genetic disorder characterized by overgrowth in childhood, specific facial manifestations, advanced bone age, and mental retardation. The purpose of this article is to describe the nonsurgical orthodontic treatment of a 10-year-old boy with a skeletal mandibular protrusion, unilateral posterior crossbite, and Sotos syndrome. After maxillary lateral expansion, the skeletal Class III relationship with an anterior crossbite improved because of mandibular clockwise rotation, whereas the facemask had a marginal effect. After growth at 16 years, he had a skeletal Class I relationship, and thus, conventional orthodontic treatment with preadjusted edgewise appliances was initiated. After 41 months of multibracket treatment, acceptable occlusion with a functional Class I relationship was obtained. One year postretention, few changes in occlusion and facial features were observed. Our results demonstrate that considering the maxillofacial vertical growth during the peripubertal period associated with Sotos syndrome, more attention should be paid to the early orthopedic treatment with the facemask and/or chincap. (Keyword) male / Humans / children / Malocclusion, Angle Class III / Sotos Syndrome / Cephalometry / Malocclusion / Mandible / Palatal Expansion Technique / Extraoral Traction Appliances / Maxilla (Tokushima University Institutional Repository) ● Metadata: 118746 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.ajodo.2021.11.021 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36437146 ● CiNii @ National Institute of Informatics (CRID): 1871991017445518080 ● Summary page in Scopus @ Elsevier: 2-s2.0-85142425693 (Tokushima University Institutional Repository: 118746, DOI: 10.1016/j.ajodo.2021.11.021, PubMed: 36437146, CiNii: 1871991017445518080, Elsevier: Scopus)
9.	Takeshi Harada, Hiroto Ohguchi, Asuka Oda, Michiyasu Nakao, Jumpei Teramachi, Masahiro Hiasa, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, Tomoko Maruhashi, Mamiko Takahashi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Shuji Ozaki, Shigeki Sano, Teru Hideshima and Masahiro Abe : Novel antimyeloma therapeutic option with inhibition of the HDAC1-IRF4 axis and PIM kinase, Blood Advances, Vol.7, No.6, 1019-1032, 2023. (Summary) Multiple myeloma (MM) preferentially expands and acquires drug resistance in the bone marrow (BM). We herein examined the role of histone deacetylase 1 (HDAC1) in the constitutive activation of the master transcription factor IRF4 and the prosurvival mediator PIM2 kinase in MM cells. The knockdown or inhibition of HDAC1 by the class I HDAC inhibitor MS-275 reduced the basal expression of IRF4 and PIM2 in MM cells. Mechanistically, the inhibition of HDAC1 decreased IRF4 transcription through histone hyperacetylation and inhibiting the recruitment of RNA polymerase II at the IRF4 locus, thereby reducing IRF4-targeting genes, including PIM2. In addition to the transcriptional regulation of PIM2 by the HDAC1-IRF4 axis, PIM2 was markedly upregulated by external stimuli from BM stromal cells and interleukin-6 (IL-6). Upregulated PIM2 contributed to the attenuation of the cytotoxic effects of MS-275. Class I HDAC and PIM kinase inhibitors cooperatively suppressed MM cell growth in the presence of IL-6 and in vivo. Therefore, the present results demonstrate the potential of the simultaneous targeting of the intrinsic HDAC1-IRF4 axis plus externally activated PIM2 as an efficient therapeutic option for MM fostered in the BM. (Keyword) Histone Deacetylase 1 / Interleukin-6 / Benzamides / Pyridines (Tokushima University Institutional Repository) ● Metadata: 118211 (Link to Publication Site) ● Publication site (DOI): 10.1182/bloodadvances.2022007155 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36129197 ● Search Scopus @ Elsevier (PMID): 36129197 ● Search Scopus @ Elsevier (DOI): 10.1182/bloodadvances.2022007155 (Tokushima University Institutional Repository: 118211, DOI: 10.1182/bloodadvances.2022007155, PubMed: 36129197)
10.	Jumpei Teramachi, Hirokazu Miki, Shingen Nakamura, Masahiro Hiasa, Takeshi Harada and Masahiro Abe : Myeloma bone disease: pathogenesis and management in the era of new anti-myeloma agents., Journal of Bone and Mineral Metabolism, 1-16, 2023. (Summary) MM cells produce a variety of cytokines to stimulate receptor activator of nuclear factor-κB ligand-mediated osteoclastogenesis and suppress osteoblastic differentiation from bone marrow stromal cells, leading to extensive bone destruction with rapid loss of bone. MM cells alter the microenvironment through bone destruction where they colonize, which in turn favors tumor growth and survival, thereby forming a vicious cycle between tumor progression and bone destruction. Denosumab or zoledronic acid is currently recommended to be administered at the start of treatment in newly diagnosed patients with MM with bone disease. Proteasome inhibitors and the anti-CD38 monoclonal antibody daratumumab have been demonstrated to exert bone-modifying activity in responders. Besides their anti-tumor activity, the effects of new anti-MM agents on bone metabolism should be more precisely analyzed in patients with MM. Because prognosis in patients with MM has been significantly improved owing to the implementation of new agents, the therapeutic impact of bone-modifying agents should be re-estimated in the era of these new agents. (Link to Publication Site) ● Publication site (DOI): 10.1007/s00774-023-01403-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36856824 ● Search Scopus @ Elsevier (PMID): 36856824 ● Search Scopus @ Elsevier (DOI): 10.1007/s00774-023-01403-4 (DOI: 10.1007/s00774-023-01403-4, PubMed: 36856824)
11.	Tatsuo Okui, Masahiro Hiasa, Kazuaki Hasegawa, Tomoya Nakamura, Kisho Ono, Soichiro Ibaragi, Takahiro Kanno, Akira Sasaki and Toshiyuki Yoneda : Lactate secreted via MCT4 from bone‑colonizing breast cancer excites sensory neurons via GPR81., International Journal of Oncology, Vol.62, No.3, 2023. (Summary) assessment of cancer pain and (Keyword) Female / Humans / Bone Neoplasms / Breast Neoplasms / Lactic Acid / Monocarboxylic Acid Transporters / Pain / Quality of Life / Receptors, G-Protein-Coupled / Sensory Receptor Cells / Animals / Mice / MDA-MB-231 Cells (Tokushima University Institutional Repository) ● Metadata: 118864 (Link to Publication Site) ● Publication site (DOI): 10.3892/ijo.2023.5487 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36799150 ● Search Scopus @ Elsevier (PMID): 36799150 ● Search Scopus @ Elsevier (DOI): 10.3892/ijo.2023.5487 (Tokushima University Institutional Repository: 118864, DOI: 10.3892/ijo.2023.5487, PubMed: 36799150)
12.	Toshiyuki Yoneda, Masahiro Hiasa, Tatsuo Okui and Kenji Hata : Cancer-nerve interplay in cancer progression and cancer-induced bone pain., Journal of Bone and Mineral Metabolism, 2023. (Summary) It is suggested that SNs may be a newly-recognized important component of the bone microenvironment that contribute to not only in the pathophysiology of CIBP but also cancer progression in bone and dissemination from bone. Suppression of the activity of bone-innervating SNs, thus, may provide unique opportunities in the treatment of cancer progression and dissemination, as well as CIBP. (Link to Publication Site) ● Publication site (DOI): 10.1007/s00774-023-01401-6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36715764 ● Search Scopus @ Elsevier (PMID): 36715764 ● Search Scopus @ Elsevier (DOI): 10.1007/s00774-023-01401-6 (DOI: 10.1007/s00774-023-01401-6, PubMed: 36715764)
13.	Yoshiki Higa, Masahiro Hiasa, Hirofumi Tenshin, Emiko Nakaue, Mariko Tanaka, Sooha Kim, Motosumi Nakagawa, Sou Shimizu, Kotaro Tanimoto, Jumpei Teramachi, Takeshi Harada, Asuka Oda, Masahiro Oura, Kimiko Sogabe, Tomoyo Hara, Ryohei Sumitani, Tomoko Maruhashi, Hiroki Yamagami, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : The Xanthine Oxidase Inhibitor Febuxostat Suppresses Adipogenesis and Activates Nrf2., Antioxidants, Vol.12, No.1, 2023. (Summary) Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in purine catabolism that acts as a novel regulator of adipogenesis. In pathological states, xanthine oxidoreductase activity increases to produce excess reactive oxygen species (ROS). The nuclear factor erythroid 2-related factor 2 (Nrf2) is a critical inducer of antioxidants, which is bound and repressed by a kelch-like ECH-associated protein 1 (Keap1) in the cytoplasm. The Keap1-Nrf2 axis appears to be a major mechanism for robust inducible antioxidant defenses. Here, we demonstrate that febuxostat, a xanthine oxidase inhibitor, alleviates the increase in adipose tissue mass in obese mouse models with a high-fat diet or ovariectomy. Febuxostat disrupts in vitro adipocytic differentiation in adipogenic media. Adipocytes appeared at day 7 in absence or presence of febuxostat were 160.8 ± 21.2 vs. 52.5 ± 12.7 (p < 0.01) in 3T3L1 cells, and 126.0 ± 18.7 vs. 55.3 ± 13.4 (p < 0.01) in 10T1/2 cells, respectively. Adipocyte differentiation was further enhanced by the addition of hydrogen peroxide, which was also suppressed by febuxostat. Interestingly, febuxostat, but not allopurinol (another xanthine oxidase inhibitor), rapidly induced the nuclear translocation of Nrf2 and facilitated the degradation of Keap1, similar to the electrophilic Nrf2 activator omaveloxolone. These results suggest that febuxostat alleviates adipogenesis under oxidative conditions, at least in part by suppressing ROS production and Nrf2 activation. Regulation of adipocytic differentiation by febuxostat is expected to inhibit obesity due to menopause or overeating. (Tokushima University Institutional Repository) ● Metadata: 118313 (Link to Publication Site) ● Publication site (DOI): 10.3390/antiox12010133 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36670994 ● Search Scopus @ Elsevier (PMID): 36670994 ● Search Scopus @ Elsevier (DOI): 10.3390/antiox12010133 (Tokushima University Institutional Repository: 118313, DOI: 10.3390/antiox12010133, PubMed: 36670994)
14.	Bingzi Dong, Masahiro Hiasa, Yoshiki Higa, Yukiyo Ohnishi, Itsuro Endo, Takeshi Kondo, Yuichi Takashi, Maria Tsoumpra, Risa Kainuma, Shun Sawatsubashi, Hiroshi Kiyonari, Go Shioi, Hiroshi Sakaue, Tomoki Nakashima, Shigeaki Kato, Masahiro Abe, Seiji Fukumoto and Toshio Matsumoto : Osteoblast/osteocyte-derived interleukin-11 regulates osteogenesis and systemic adipogenesis., Nature Communications, Vol.13, No.1, 2022. (Summary) did not exhibit any abnormalities. We demonstrate that osteoblast/osteocyte-derived IL-11 controls both osteogenesis and systemic adiposity in response to mechanical loading, an important insight for our understanding of osteoporosis and metabolic syndromes. (Keyword) Animals / Mice / Adipogenesis / Interleukin-11 / Obesity / Osteoblasts / Osteocytes / Osteogenesis / Mice, Knockout (Tokushima University Institutional Repository) ● Metadata: 118940 (Link to Publication Site) ● Publication site (DOI): 10.1038/s41467-022-34869-3 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36424386 ● Search Scopus @ Elsevier (PMID): 36424386 ● Search Scopus @ Elsevier (DOI): 10.1038/s41467-022-34869-3 (Tokushima University Institutional Repository: 118940, DOI: 10.1038/s41467-022-34869-3, PubMed: 36424386)
15.	Fumiko Takahashi, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : 矯正歯科治療の経過予後からみた埋伏下顎大臼歯の歯科用CB-CT画像の特徴と牽引可否との関連性, The Journal of Chu-Shikoku Orthodontic Society, Vol.34, No.1, 75-82, 2022. (Summary) 【目的】埋伏下顎大臼歯は，発生率は低いものの骨性癒着が認められた際は重大な不正咬合の原因となる．その治療予後の予測は未だ困難であり，重要な臨床課題の一つである．本研究では臨床的に牽引が不可能であった下顎大臼歯のエックス線画像を見直し，牽引可能であった例と比較することで，牽引の可否を鑑別するための特徴的な画像所見を検討した．【方法】資料として徳島大学病院矯正歯科を受診した第三大臼歯を除く下顎大臼歯の埋伏を有する患者5 名の歯科用コーンビームCT (以下CB-CT) 画像とパノラマエックス線画像を用いた．Ducommun らの骨性癒着歯の評価項目である歯根膜腔消失・歯根吸収・組織置換に加え，置換性歯根吸収(歯根吸収により生じた歯根表面の凹凸部の骨硬化像)，歯根彎曲の有無を評価した．【結果】パノラマエックス線画像では5 例全てで歯根膜腔の消失を認めたが，歯根吸収や組織置換像は観察されなかった．一方，CB-CT 画像では牽引が不可能であった3 例全てで歯根膜腔の消失と置換性歯根吸収像を認めた．牽引が可能であった2 例でも歯根膜腔の消失がみられ，うち1 例では歯根吸収像も認めたがその近傍に骨硬化像はなかった．【考察】Ducommun らの評価項目のみでは，牽引可能であった1 例が偽陽性となったが，置換性歯根吸収の評価項目への追加により偽陽性はなくなった．このことから置換性歯根吸収の評価が埋伏下顎大臼歯の牽引の可否の鑑別に極めて重要であると考えられた．【結論】埋伏下顎大臼歯の診断において，CB-CT 画像での当該歯の周囲組織の詳細な観察により，牽引が可能であるかを非常に高い精度で診断できる可能性が示唆された． (Keyword) 骨性癒着歯 / コーンビームCT (Tokushima University Institutional Repository) ● Metadata: 118828 (Tokushima University Institutional Repository: 118828)
16.	Sou Shimizu, Jumpei Teramachi, Takeshi Harada, Masahiro Hiasa, Hirofumi Tenshin, A Oda, A Seki, Y Inoue, Kotaro Tanimoto, Yoshiki Higa, M Oura, K Sogabe, Takeshi Harada, Ryohei Sumitani, T Maruhashi, H Yamagami, Y Sawa, Itsuro Endo, K Tsuneyama, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : Aberrant upregulation of the endogenous PP2A inhibitor CIP2A is vital for myeloma cell growth and survival, International Journal of Myeloma, Vol.12, No.2, 14-23, 2022. (Summary) <p>The serine/threonine kinase TAK1 is constitutively overexpressed and auto-phosphorylated in multiple myeloma (MM) cells. Protein phosphatase 2A (PP2A) is a major serine/threonine phosphatase which dephosphorylates proteins phosphorylated by various serine/threonine kinases to regulate multiple cellular functions. We recently reported that the serine/threonine kinase TGF-β-activated kinase-1 (TAK1) is highly expressed and auto-phosphorylated to mediate critical growth and survival signaling in MM cells. We demonstrate here that regulation of PP2A activity inversely affects the phosphorylation levels of TAK1 in MM cells, and that MM cells aberrantly overexpress cancerous inhibitor of PP2A (CIP2A), an endogenous inhibitor for PP2A. <i>CIP2A</i> gene silencing as well as treatment with the CIP2A inhibitor TD52 potently induced MM cell death along with suppression of TAK1 expression in MM cells. These results suggest the critical role of PP2A inactivation via CIP2A upregulation in TAK1 phosphorylation and its protein expression and thereby MM cell growth and survival, posing the CIP2A-PP2A axis as an important therapeutic target.</p> (Keyword) multiple myeloma / TAK1 / CIP2A / PP2A (Tokushima University Institutional Repository) ● Metadata: 117150 (Link to Publication Site) ● Publication site (DOI): 10.57352/ijm.12.2_14 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390573947533793024 ● Search Scopus @ Elsevier (DOI): 10.57352/ijm.12.2_14 (Tokushima University Institutional Repository: 117150, DOI: 10.57352/ijm.12.2_14, CiNii: 1390573947533793024)
17.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Asuka Oda, Takeshi Harada, Yoshiki Higa, Kimiko Sogabe, Masahiro Oura, Ryohei Sumitani, Tomoyo Hara, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : Mechanical unloading aggravates bone destruction and tumor expansion in myeloma., Haematologica, Vol.107, No.3, 744-749, 2022. (Keyword) Bone Resorption / Humans / Multiple Myeloma / Osteoclasts / Osteolysis (Tokushima University Institutional Repository) ● Metadata: 116715 (Link to Publication Site) ● Publication site (DOI): 10.3324/haematol.2021.278295 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34788982 ● Search Scopus @ Elsevier (PMID): 34788982 ● Search Scopus @ Elsevier (DOI): 10.3324/haematol.2021.278295 (Tokushima University Institutional Repository: 116715, DOI: 10.3324/haematol.2021.278295, PubMed: 34788982)
18.	Hirofumi Tenshin, Jumpei Teramachi, Mohannad Ashtar, Masahiro Hiasa, Yusuke Inoue, Asuka Oda, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Takeshi Harada, Masahiro Oura, Kimiko Sogabe, Tomoyo Hara, Ryohei Sumitani, Tomoko Maruhashi, Mayu Sebe, Rie Tsutsumi, Hiroshi Sakaue, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : TGF-β-activated kinase-1 inhibitor LL-Z1640-2 reduces joint inflammation and bone destruction in mouse models of rheumatoid arthritis by inhibiting NLRP3 inflammasome, TACE, TNF-α and RANKL expression., Clinical & translational immunology, Vol.11, No.1, 2022. (Summary) TAK1 inhibition with LLZ may become a novel treatment strategy to effectively alleviate inflammasome-mediated inflammation and RANKL-induced osteoclastic bone destruction in joints alongside its potent suppression of TNF-α and IL-6 production and proteinase-mediated pathological processes in RA. (Tokushima University Institutional Repository) ● Metadata: 117260 (Link to Publication Site) ● Publication site (DOI): 10.1002/cti2.1371 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35079379 ● Search Scopus @ Elsevier (PMID): 35079379 ● Search Scopus @ Elsevier (DOI): 10.1002/cti2.1371 (Tokushima University Institutional Repository: 117260, DOI: 10.1002/cti2.1371, PubMed: 35079379)
19.	Shinya Horiuchi, Hiroko Sato, Akihiko Iwasa, Aki Ichihara, Hirofumi Tenshin, Keiichiro Watanabe, Masahiro Hiasa, Ichiro Hashimoto and Eiji Tanaka : Long-term Management of a Patient with Apert Syndrome., The Journal of Contemporary Dental Practice, Vol.22, No.10, 1184-1190, 2021. (Summary) The two-stage operation combining early distraction osteogenesis and postgrowth orthognathic surgery proves to be an effective therapy for correcting midfacial hypoplasia and skeletal mandibular protrusion caused by Apert syndrome. (Keyword) Acrocephalosyndactylia / Adolescent / Adult / Cephalometry / Humans / Infant / Male / Open Bite / Osteogenesis, Distraction / Osteotomy, Le Fort / Young Adult (Tokushima University Institutional Repository) ● Metadata: 117255 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35197388 ● Search Scopus @ Elsevier (PMID): 35197388 (Tokushima University Institutional Repository: 117255, PubMed: 35197388)
20.	Masahiro Hiasa, Takeshi Harada, Eiji Tanaka and Masahiro Abe : Pathogenesis and treatment of multiple myeloma bone disease., Japanese Dental Science Review, Vol.57, 164-173, 2021. (Summary) Multiple myeloma (Plasma cell myeloma), a malignancy of the plasma cells, exhibits tumor expansion preferentially in the bone marrow and the development of bone-destructive lesions. Multiple myeloma is still an incurable disease with changes in the bone marrow microenvironment in favor of the survival and proliferation of multiple myeloma cells and bone destruction. In this review, we described the recent findings on the regulators involved in the development of myeloma bone diseases, and succinctly summarize currently available therapeutic options and the development of novel bone modifying agents for myeloma treatment. (Tokushima University Institutional Repository) ● Metadata: 117254 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jdsr.2021.08.006 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34611468 ● Search Scopus @ Elsevier (PMID): 34611468 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jdsr.2021.08.006 (Tokushima University Institutional Repository: 117254, DOI: 10.1016/j.jdsr.2021.08.006, PubMed: 34611468)
21.	Toshiyuki Yoneda, Masahiro Hiasa, Tatsuo Okui and Kenji Hata : Sensory nerves: A driver of the vicious cycle in bone metastasis?, Journal of Bone Oncology, Vol.30, 2021. (Summary) Bone is one of the preferential target organs of cancer metastasis. Bone metastasis is associated with various complications, of which bone pain is most common and debilitating. The cancer-associated bone pain (CABP) is induced as a consequence of increased neurogenesis, reprogramming and axonogenesis of sensory nerves (SNs) in harmony with sensitization and excitation of SNs in response to the tumor microenvironment created in bone. Importantly, CABP is associated with increased mortality, of which precise cellular and molecular mechanism remains poorly understood. Bone is densely innervated by autonomic nerves (ANs) (sympathetic and parasympathetic nerves) and SNs. Recent studies have shown that the nerves innervating the tumor microenvironment establish intimate communications with tumors, producing various stimuli for tumors to progress and disseminate. In this review, our current understanding of the role of SNs innervating bone in the pathophysiology of CABP will be overviewed. Then the hypothesis that SNs facilitate cancer progression in bone will be discussed in conjunction with our recent findings that SNs play an important role not only in the induction of CABP but also the progression of bone metastasis using a preclinical model of CABP. It is suggested that SNs are a critical component of the bone microenvironment that drives the vicious cycle between bone and cancer to progress bone metastasis. Suppression of the activity of bone-innervating SNs may have potential therapeutic effects on the progression of bone metastasis and induction of CABP. (Tokushima University Institutional Repository) ● Metadata: 118872 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jbo.2021.100387 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34504741 ● Search Scopus @ Elsevier (PMID): 34504741 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbo.2021.100387 (Tokushima University Institutional Repository: 118872, DOI: 10.1016/j.jbo.2021.100387, PubMed: 34504741)
22.	Kaoru Yoshinaga, 塩屋園玲子, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : 歯科矯正用アンカースクリューの導入に伴う治療方針の変化(第一報) 抜歯・非抜歯および抜歯部位の判定に関する検討, The Journal of Chu-Shikoku Orthodontic Society, Vol.33, No.1, 19-28, 2021. (Summary) 【目的】近年，歯科矯正用アンカースクリュー(以降アンカーと明記する)の普及により，臼歯の固定や移動が容易に行えるようになり，抜歯，非抜歯，抜歯部位の選択についても変化が起きている．今回，アンカーの導入前後での治療方針の変化について，とくに臼歯抜歯の適応に関する調査を行ったので報告する．【方法】徳島大学病院矯正歯科を受診した初診時年齢12歳以上の患者を対象とし，2002年以前にマルチブラケット治療の診断を受けた100名(Pre群)と2008年以降に診断を受けた100名(Post群)を無作為に抽出した．先天性疾患および歯牙欠損症例，顎変形症は除外した．診断内容における臼歯抜歯(第三大臼歯は除く)の有無，抜歯部位等に関する比較検討を行った．【結果および考察】Pre群とPost群の間で抜歯症例数および抜歯部位に違いは認められなかった．一方，skeletal Class IIの症例はPre群では上顎片顎小臼歯抜歯によるカムフラージュ治療が多かったのに対し，Post群ではその割合は減少していた．また，skeletal Class IIIの症例ではアンカーを用いた非抜歯治療の割合が増加していた．High mandibular plane angle caseにおいてはアンカーの使用により，上顎第一大臼歯の挺出防止ならびに圧下が可能となり上下顎第一小臼歯を抜去する割合が増えた．【結論】アンカー導入で，臼歯の移動や挺出の防止および圧下が可能となり抜歯部位の選択基準に変化が生じたと考えられた．(著者抄録) (Keyword) 下顎骨上顎骨小臼歯(外科的療法) 抜歯不正咬合-アングルI級(治療) 不正咬合-アングルII級(治療) 不正咬合-アングルIII級(治療) 治療成績歯科矯正用固定源埋込みヒト歯学
23.	Akiko Mino-Oka, Shinya Horiuchi, Rie Matsuda, Ryoko Shioyasono, Mohannad Ashtar, Masahiro Hiasa, Akihiro Yasue, Keiji Moriyama and Eiji Tanaka : A Long-term Follow-up of Mandibular Deviation Caused by Congenital Cervical Lymphangioma Treated with an Orthodontic Approach., The Journal of Contemporary Dental Practice, Vol.22, No.6, 713-720, 2021. (Summary) The hybrid technique combining functional appliance and intermaxillary elastics proves to be an effective therapy for correcting occlusal cant and mandibular deviation caused by cervical lymphangioma. (Keyword) Cephalometry / Facial Asymmetry / female / Follow-Up Studies / Humans / Lymphangioma / Malocclusion / Mandible (Tokushima University Institutional Repository) ● Metadata: 116185 (Link to Publication Site) ● Publication site (DOI): 10.5005/jp-journals-10024-3115 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34393132 ● Summary page in Scopus @ Elsevier: 2-s2.0-85112843821 (Tokushima University Institutional Repository: 116185, DOI: 10.5005/jp-journals-10024-3115, PubMed: 34393132, Elsevier: Scopus)
24.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Asuka Oda, Ariunzaya Bat-Erdene, Takeshi Harada, Shingen Nakamura, Mohannad Ashtar, Sou Shimizu, Masami Iwasa, Kimiko Sogabe, Masahiro Oura, Shiroh Fujii, Kumiko Kagawa, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : TAK1 is a pivotal therapeutic target for tumor progression and bone destruction in myeloma, Haematologica, Vol.106, No.5, 1401-1413, 2021. (Summary) Along with the tumor progression, the bone marrow microenvironment is skewed in multiple myeloma (MM), which underlies the unique pathophysiology of MM and confers aggressiveness and drug resistance in MM cells. TGF-β-activated kinase-1 (TAK1) mediates a wide range of intracellular signaling pathways. We demonstrate here that TAK1 is constitutively overexpressed and phosphorylated in MM cells, and that TAK1 inhibition suppresses the activation of NF-κB, p38MAPK, ERK and STAT3 to decrease the expression of critical mediators for MM growth and survival, including PIM2, MYC, Mcl-1, IRF4, and Sp1, along with a substantial reduction in the angiogenic factor VEGF in MM cells. Intriguingly, TAK1 phosphorylation was also induced along with upregulation of vascular cell adhesion molecule-1 (VCAM-1) in bone marrow stromal cells (BMSCs) in cocultures with MM cells, which facilitated MM cell-BMSC adhesion while inducing IL-6 production and receptor activator of nuclear factor κ-Β ligand (RANKL) expression by BMSCs. TAK1 inhibition effectively impaired MM cell adhesion to BMSCs to disrupt the support of MM cell growth and survival by BMSCs. Furthermore, TAK1 inhibition suppressed osteoclastogenesis enhanced by RANKL in cocultures of bone marrow cells with MM cells, and restored osteoblastic differentiation suppressed by MM cells or inhibitory factors for osteoblastogenesis overproduced in MM. Finally, treatment with the TAK1 inhibitor LLZ1640-2 markedly suppressed MM tumor growth and prevented bone destruction and loss in mouse MM models. Therefore, TAK1 inhibition may be a promising therapeutic option targeting not only MM cells but also the skewed bone marrow microenvironment in MM. (Keyword) Animals / Bone Marrow Cells / MAP Kinase Kinase Kinases / Mice / Multiple Myeloma / NF-kappa B / Osteoclasts / Osteolysis / RANK Ligand / Tumor Microenvironment (Tokushima University Institutional Repository) ● Metadata: 116529 (Link to Publication Site) ● Publication site (DOI): 10.3324/haematol.2019.234476 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32273474 ● Search Scopus @ Elsevier (PMID): 32273474 ● Search Scopus @ Elsevier (DOI): 10.3324/haematol.2019.234476 (Tokushima University Institutional Repository: 116529, DOI: 10.3324/haematol.2019.234476, PubMed: 32273474)
25.	Ayami Ito, Kazuna Tachiki, Ryoko Shioyasono, Mohannad Ashtar, Keiichiro Watanabe, Masahiro Hiasa and Eiji Tanaka : Hemifacial Microsomia Caused by First and Second Brachial Arch Syndrome Treated with Orthodontic Approach: A Case Report., The Journal of Contemporary Dental Practice, Vol.21, No.10, 1189-1195, 2020. (Summary) This report proposes an efficacy of conventional orthodontic treatment for growing patients with hemifacial microsomia involved in the FSBAS. (Keyword) Child / Dental Occlusion / Facial Asymmetry / female / Goldenhar Syndrome / Humans / infant / Mandible / Maxilla (Tokushima University Institutional Repository) ● Metadata: 116453 (Link to Publication Site) ● Publication site (DOI): 10.5005/JP-JOURNALS-10024-2957 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33686045 ● Summary page in Scopus @ Elsevier: 2-s2.0-85099979923 (Tokushima University Institutional Repository: 116453, DOI: 10.5005/JP-JOURNALS-10024-2957, PubMed: 33686045, Elsevier: Scopus)
26.	Mohannad Ashtar, Hirofumi Tenshin, Jumpei Teramachi, Ariunzaya Bat-Erdene, Masahiro Hiasa, Asuka Oda, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Takeshi Harada, Masahiro Oura, Kimiko Sogabe, Shingen Nakamura, Shiroh Fujii, Ryohei Sumitani, Hirokazu Miki, Kengo Udaka, Mamiko Takahashi, Kumiko Kagawa, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : The Roles of ROS Generation in RANKL-Induced Osteoclastogenesis: Suppressive Effects of Febuxostat., Cancers, Vol.12, No.4, 2020. (Summary) Receptor activator of NF-κB ligand (RANKL), a critical mediator of osteoclastogenesis, is upregulated in multiple myeloma (MM). The xanthine oxidase inhibitor febuxostat, clinically used for prevention of tumor lysis syndrome, has been demonstrated to effectively inhibit not only the generation of uric acid but also the formation of reactive oxygen species (ROS). ROS has been demonstrated to mediate RANKL-mediated osteoclastogenesis. In the present study, we therefore explored the role of cancer-treatment-induced ROS in RANKL-mediated osteoclastogenesis and the suppressive effects of febuxostat on ROS generation and osteoclastogenesis. RANKL dose-dependently induced ROS production in RAW264.7 preosteoclastic cells; however, febuxostat inhibited the RANKL-induced ROS production and osteoclast (OC) formation. Interestingly, doxorubicin (Dox) further enhanced RANKL-induced osteoclastogenesis through upregulation of ROS production, which was mostly abolished by addition of febuxostat. Febuxostat also inhibited osteoclastogenesis enhanced in cocultures of bone marrow cells with MM cells. Importantly, febuxostat rather suppressed MM cell viability and did not compromise Dox's anti-MM activity. In addition, febuxostat was able to alleviate pathological osteoclastic activity and bone loss in ovariectomized mice. Collectively, these results suggest that excessive ROS production by aberrant RANKL overexpression and/or anticancer treatment disadvantageously impacts bone, and that febuxostat can prevent the ROS-mediated osteoclastic bone damage. (Tokushima University Institutional Repository) ● Metadata: 115041 (Link to Publication Site) ● Publication site (DOI): 10.3390/cancers12040929 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32283857 ● Search Scopus @ Elsevier (PMID): 32283857 ● Search Scopus @ Elsevier (DOI): 10.3390/cancers12040929 (Tokushima University Institutional Repository: 115041, DOI: 10.3390/cancers12040929, PubMed: 32283857)
27.	Dong Bingzi, Itsuro Endo, Ohnishi Yukoyo, Mitsui Yukari, Kiyoe Kurahashi, Mai Kanai, Masahiro Hiasa, Jumpei Teramachi, Hirofumi Tenshin, Seiji Fukumoto, Masahiro Abe and Toshio Matsumoto : Persistent Activation of Calcium-Sensing Receptor Suppresses Bone Turnover, Increases Microcracks, and Decreases Bone Strength., JBMR Plus, Vol.3, No.7, e10182, 2019. (Summary) Activating mutations of calcium-sensing receptor (CaSR) cause autosomal dominant hypocalcemia type 1 (ADH1). Patients with ADH1 exhibit similar features to patients with hypoparathyroidism, including reduced serum parathyroid hormone (PTH) and Ca with low bone turnover. Although persistent suppression of bone turnover may increase bone fragility, bone strength in ADH1 patients has been unclear. We created knock-in mice harboring the A843E activating mutation of CaSR, mimicking severe features of ADH1 patients. The severe form of ADH1 model mice showed smaller body and bone size with lower bone mineral density (BMD) and cortical area of the femur compared with age-matched wild-type (WT) mice. Bone strength in the femur was lower in ADH1 mice even after correction by bone geometry and/or BMD. Microcracks were markedly increased in ADH1 mice, but were rarely detected in WT mice. There was a negative correlation between bone strength corrected by bone geometry and/or BMD and microcrack number or density in ADH1 and WT mice. Among ADH1 mice, negative correlation was still observed between bone strength and microcrack number or density. Microcracks increased with age in ADH1 mice, and were negatively correlated with bone strength. Treatment with PTH(1-34) or a calcilytic, JTT-305, increased bone turnover, reduced microcracks, and increased bone strength to similar levels to those in WT mice. The increase in microcracks was associated with a reduction in bone strength in ADH1 mice, and aging aggravates these changes. These results demonstrate that activating mutation of CaSR causes reduction in PTH secretion with suppressed bone turnover, that reduced bone turnover is associated with an age-dependent increase in microcracks with a reduction in bone strength, and that both PTH(1-34) and calcilytic ameliorate all these changes in bone turnover and strength. It is suggested that fracture susceptibility may be increased in severe types of ADH1 patients especially in the elderly. © 2019 The Authors. published by Wiley Periodicals, Inc. on behalf of American Society for Bone and Mineral Research. (Link to Publication Site) ● Publication site (DOI): 10.1002/jbm4.10182 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31372589 ● Search Scopus @ Elsevier (PMID): 31372589 ● Search Scopus @ Elsevier (DOI): 10.1002/jbm4.10182 (DOI: 10.1002/jbm4.10182, PubMed: 31372589)
28.	Ariunzaya Bat-Erdene, Shingen Nakamura, Asuka Oda, Masami Iwasa, Jumpei Teramachi, Mohannad Ashtar, Takeshi Harada, Hirokazu Miki, Hirofumi Tenshin, Masahiro Hiasa, Shiroh Fujii, Kimiko Sogabe, Masahiro Oura, Kengo Udaka, Kumiko Kagawa, Sumiko Yoshida, Ken-ichi Aihara, Kiyoe Kurahashi, Itsuro Endo and Masahiro Abe : Class 1 HDAC and HDAC6 inhibition inversely regulates CD38 induction in myeloma cells via interferon-α and ATRA., British Journal of Haematology, 2018. (Tokushima University Institutional Repository) ● Metadata: 113393 (Link to Publication Site) ● Publication site (DOI): 10.1111/bjh.15673 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30474853 ● Summary page in Scopus @ Elsevier: 2-s2.0-85057280798 (Tokushima University Institutional Repository: 113393, DOI: 10.1111/bjh.15673, PubMed: 30474853, Elsevier: Scopus)
29.	Shinya Horiuchi, Hiromichi Yumoto, Tomoko Kimura, Minami Sato, Silvia Naomi Mitsui Akagi, Masahiro Hiasa, Eiji Nishikawa, Tarek El-Bialy and Eiji Tanaka : Effect of pulsed ultrasound toothbrush on Streptococcus mutans biofilm removal., American Journal of Dentistry, Vol.31, No.2, 67-70, 2018. (Summary) The sonic vibration with pulsed ultrasound showed more reduction of the biofilm compared to the control and the sonic vibration with and without continuous ultrasound. Thus, pulsed ultrasound action may be beneficial for biofilm removal of interproximal regions. (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29630788 ● Summary page in Scopus @ Elsevier: 2-s2.0-85047330699 (PubMed: 29630788, Elsevier: Scopus)
30.	Yoneda Toshiyuki, Masahiro Hiasa and Tatuso Okui : Bone Pain Associated with Acidic Cancer Microenvironment, Current Molecular Biology Reports, Vol.4, No.2, 59-68, 2018. (Link to Publication Site) ● Publication site (DOI): 10.1007/s40610-018-0089-7 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1007/s40610-018-0089-7 (DOI: 10.1007/s40610-018-0089-7)
31.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Takeshi Harada, Shingen Nakamura, Ryota Amachi, Hirofumi Tenshin, Masami Iwasa, Shiroh Fujii, Kumiko Kagawa, Hirokazu Miki, Kiyoe Kurahashi, Sumiko Yoshida, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Pim-2 is a critical target for treatment of osteoclastogenesis enhanced in myeloma., British Journal of Haematology, Vol.180, No.4, 581-585, 2018. (Tokushima University Institutional Repository) ● Metadata: 112935 (Link to Publication Site) ● Publication site (DOI): 10.1111/bjh.14388 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27748523 ● Search Scopus @ Elsevier (PMID): 27748523 ● Search Scopus @ Elsevier (DOI): 10.1111/bjh.14388 (Tokushima University Institutional Repository: 112935, DOI: 10.1111/bjh.14388, PubMed: 27748523)
32.	Shiroh Fujii, Shingen Nakamura, Asuka Oda, Hirokazu Miki, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Ariunzaya Bat-Erdene, Yusaku Maeda, Masahiro Oura, Mamiko Takahashi, Masami Iwasa, Itsuro Endo, Sumiko Yoshida, Ken-ichi Aihara, Kiyoe Kurahashi, Takeshi Harada, Kumiko Kagawa, Michiyasu Nakao, Shigeki Sano and Masahiro Abe : Unique anti-myeloma activity by thiazolidine-2,4-dione compounds with Pim inhibiting activity., British Journal of Haematology, Vol.180, No.2, 246-258, 2018. (Summary) Proviral Integrations of Moloney virus 2 (PIM2) is overexpressed in multiple myeloma (MM) cells, and regarded as an important therapeutic target. Here, we aimed to validate the therapeutic efficacy of different types of PIM inhibitors against MM cells for their possible clinical application. Intriguingly, the thiazolidine-2,4-dione-family compounds SMI-16a and SMI-4a reduced PIM2 protein levels and impaired MM cell survival preferentially in acidic conditions, in contrast to other types of PIM inhibitors, including AZD1208, CX-6258 and PIM447. SMI-16a also suppressed the drug efflux function of breast cancer resistance protein, minimized the sizes of side populations and reduced in vitro colony-forming capacity and in vivo tumourigenic activity in MM cells, suggesting impairment of their clonogenic capacity. PIM2 is known to be subject to ubiquitination-independent proteasomal degradation. Consistent with this, the proteasome inhibitors bortezomib and carfilzomib increased PIM2 protein levels in MM cells without affecting its mRNA levels. However, SMI-16a mitigated the PIM2 protein increase and cooperatively enhanced anti-MM effects in combination with carfilzomib. Collectively, the thiazolidine-2,4-dione-family compounds SMI-16a and SMI-4a uniquely reduce PIM2 protein in MM cells, which may contribute to their profound efficacy in addition to their immediate kinase inhibition. Their combination with proteasome inhibitors is envisioned. (Keyword) Animals / Antineoplastic Agents / Cell Line, Tumor / Cell Survival / Cell Transformation, Neoplastic / Disease Models, Animal / Humans / Hydrogen-Ion Concentration / Mice / Multiple Myeloma / Proteasome Inhibitors / Protein-Serine-Threonine Kinases / Proteolysis / Proto-Oncogene Proteins / Thiazolidinediones (Tokushima University Institutional Repository) ● Metadata: 112752 (Link to Publication Site) ● Publication site (DOI): 10.1111/bjh.15033 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29327347 ● Summary page in Scopus @ Elsevier: 2-s2.0-85040344893 (Tokushima University Institutional Repository: 112752, DOI: 10.1111/bjh.15033, PubMed: 29327347, Elsevier: Scopus)
33.	Akihiko Iwasa, Shinya Horiuchi, Nao Kinouchi, Takashi Izawa, Masahiro Hiasa, Nobuhiko Kawai, Akihiro Yasue, H Ali Hassan and Eiji Tanaka : Skeletal anchorage for intrusion of bimaxillary molars in a patient with skeletal open bite and temporomandibular disorders., Journal of Orthodontic Science, Vol.6, No.4, 152-158, 2017. (Summary) The treatment of severe skeletal anterior open bite is extremely difficult in adults, and orthognathic surgery is generally selected for its treatment. We report the case of an 18-year-old adult patient with skeletal anterior open bite and temporomandibular disorders who was successfully treated using temporary anchorage devices. She had an open bite of -2.0 mm and an increased facial height. Miniplates were implanted in both the maxilla and mandible, and molar intrusion resulted in counterclockwise rotation of the mandible over a period of 12 months. After active treatment, her upper and lower first molars were intruded by approximately 2 mm and her overbite became +2.5 mm. Her retrognathic profile improved with counterclockwise rotation of the mandible. Orthodontic treatment aided with skeletal anchorage is beneficial for intrusion of bimaxillary molars in patients with anterior open bite. (Tokushima University Institutional Repository) ● Metadata: 113509 (Link to Publication Site) ● Publication site (DOI): 10.4103/jos.JOS_63_17 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29119097 ● Search Scopus @ Elsevier (PMID): 29119097 ● Search Scopus @ Elsevier (DOI): 10.4103/jos.JOS_63_17 (Tokushima University Institutional Repository: 113509, DOI: 10.4103/jos.JOS_63_17, PubMed: 29119097)
34.	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. (Summary) 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. (Tokushima University Institutional Repository) ● Metadata: 113059 (Link to Publication Site) ● Publication site (DOI): 10.18632/oncotarget.23121 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29535808 ● Summary page in Scopus @ Elsevier: 2-s2.0-85041952629 (Tokushima University Institutional Repository: 113059, DOI: 10.18632/oncotarget.23121, PubMed: 29535808, Elsevier: Scopus)
35.	Hirofumi Tenshin, Jumpei Teramachi, Asuka Oda, Ryota Amachi, Masahiro Hiasa, Ariunzaya Bat-Erdene, Keiichiro Watanabe, Masami Iwasa, Takeshi Harada, Shiroh Fujii, Kumiko Kagawa, Kimiko Sogabe, Shingen Nakamura, Hirokazu Miki, Kiyoe Kurahashi, Sumiko Yoshida, Kenichi Aihara, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1 inhibition subverts the osteoclastogenic action of TRAIL while potentiating its antimyeloma effects., Blood Advances, Vol.1, No.24, 2124-2137, 2017. (Summary) Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) agonists induce tumor-specific apoptosis indicating that they may be an attractive therapeutic strategy against cancers, including multiple myeloma (MM). Osteoclastogenesis is highly induced in MM, which in turn enhances MM growth, thereby forming a vicious cycle between MM tumor expansion and bone destruction. However, the effects of TRAIL on MM-enhanced osteoclastogenesis remain largely unknown. Here, we show that TRAIL induced apoptosis in MM cells, but not in osteoclasts (OCs), and that it rather facilitated receptor activator of NF-B ligand-induced osteoclastogenesis along with upregulation of cellular FLICE inhibitory protein (c-FLIP). TRAIL did not induce death-inducing signaling complex formation in OCs, but formed secondary complex (complex II) with the phosphorylation of transforming growth factor -activated kinase-1 (TAK1), and thus activated NF-B signaling. c-FLIP knockdown abolished complex II formation, thus permitting TRAIL induction of OC cell death. The TAK1 inhibitor LLZ1640-2 abrogated the TRAIL-induced c-FLIP upregulation and NF-B activation, and triggered TRAIL-induced caspase-8 activation and cell death in OCs. Interestingly, the TRAIL-induced caspase-8 activation caused enzymatic degradation of the transcription factor Sp1 to noticeably reduce c-FLIP expression, which further sensitized OCs to TRAIL-induced apoptosis. Furthermore, the TAK1 inhibition induced antiosteoclastogenic activity by TRAIL even in cocultures with MM cells while potentiating TRAIL's anti-MM effects. These results demonstrated that osteoclastic lineage cells use TRAIL for their differentiation and activation through tilting caspase-8-dependent apoptosis toward NF-B activation, and that TAK1 inhibition subverts TRAIL-mediated NF-B activation to resume TRAIL-induced apoptosis in OCs while further enhancing MM cell death in combination with TRAIL. (Tokushima University Institutional Repository) ● Metadata: 111724 (Link to Publication Site) ● Publication site (DOI): 10.1182/bloodadvances.2017008813 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29296860 ● Search Scopus @ Elsevier (PMID): 29296860 ● Search Scopus @ Elsevier (DOI): 10.1182/bloodadvances.2017008813 (Tokushima University Institutional Repository: 111724, DOI: 10.1182/bloodadvances.2017008813, PubMed: 29296860)
36.	Hannah M. Davis, Rafael Pacheco-Costa, Emily G. Atkinson, Lucas R. Brun, Arancha R. Gortazar, Julia Harris, Masahiro Hiasa, Surajudeen A. Bolarinwa, Toshiyuki Yoneda, Mircea Ivan, Angela Bruzzaniti, Teresita Bellido and Lilian I. Plotkin : Disruption of the Cx43/miR21 pathway leads to osteocyte apoptosis and increased osteoclastogenesis with aging., Aging Cell, Vol.16, No.3, 551-563, 2017. (Summary) Skeletal aging results in apoptosis of osteocytes, cells embedded in bone that control the generation/function of bone forming and resorbing cells. Aging also decreases connexin43 (Cx43) expression in bone; and osteocytic Cx43 deletion partially mimics the skeletal phenotype of old mice. Particularly, aging and Cx43 deletion increase osteocyte apoptosis, and osteoclast number and bone resorption on endocortical bone surfaces. We examined herein the molecular signaling events responsible for osteocyte apoptosis and osteoclast recruitment triggered by aging and Cx43 deficiency. Cx43-silenced MLO-Y4 osteocytic (Cx43(def) ) cells undergo spontaneous cell death in culture through caspase-3 activation and exhibit increased levels of apoptosis-related genes, and only transfection of Cx43 constructs able to form gap junction channels reverses Cx43(def) cell death. Cx43(def) cells and bones from old mice exhibit reduced levels of the pro-survival microRNA miR21 and, consistently, increased levels of the miR21 target phosphatase and tensin homolog (PTEN) and reduced phosphorylated Akt, whereas PTEN inhibition reduces Cx43(def) cell apoptosis. miR21 reduction is sufficient to induce apoptosis of Cx43-expressing cells and miR21 deletion in miR21(fl/fl) bones increases apoptosis-related gene expression, whereas a miR21 mimic prevents Cx43(def) cell apoptosis, demonstrating that miR21 lies downstream of Cx43. Cx43(def) cells release more osteoclastogenic cytokines [receptor activator of NFB ligand (RANKL)/high-mobility group box-1 (HMGB1)], and caspase-3 inhibition prevents RANKL/HMGB1 release and the increased osteoclastogenesis induced by conditioned media from Cx43(def) cells, which is blocked by antagonizing HMGB1-RAGE interaction. These findings identify a novel Cx43/miR21/HMGB1/RANKL pathway involved in preventing osteocyte apoptosis that also controls osteoclast formation/recruitment and is impaired with aging. (Tokushima University Institutional Repository) ● Metadata: 118999 (Link to Publication Site) ● Publication site (DOI): 10.1111/acel.12586 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28317237 ● Search Scopus @ Elsevier (PMID): 28317237 ● Search Scopus @ Elsevier (DOI): 10.1111/acel.12586 (Tokushima University Institutional Repository: 118999, DOI: 10.1111/acel.12586, PubMed: 28317237)
37.	Masahiro Hiasa, Tatsuo Okui, Yohance M. Allette, Matthew S. Ripsch, Ge-Hong Sun-Wada, Hiroki Wakabayashi, G David Roodman, Fletcher A. White and Toshiyuki Yoneda : Bone Pain Induced by Multiple Myeloma Is Reduced by Targeting V-ATPase and ASIC3., Cancer Research, Vol.77, No.6, 1283-1295, 2017. (Summary) Multiple myeloma patients experience severe bone pain (MMBP) that is undertreated and poorly understood. In this study, we studied MMBP in an intratibial mouse xenograft model that employs JJN3 human multiple myeloma cells. In this model, mice develop MMBP associated in bone with increased sprouting of calcitonin gene-related peptide-positive (CGRP(+)) sensory nerves and in dorsal root ganglia (DRG) with upregulation of phosphorylated ERK1/2 (pERK1/2) and pCREB, two molecular indicators of neuron excitation. We found that JJN3 cells expressed a vacuolar proton pump (V-ATPase) that induced an acidic bone microenvironment. Inhibition of JJN3-colonized bone acidification by a single injection of the selective V-ATPase inhibitor, bafilomycin A1, decreased MMBP, CGRP(+) sensory neuron sprouting, and pERK1/2 and pCREB expression in DRG. CGRP(+) sensory nerves also expressed increased levels of the acid-sensing nociceptor ASIC3. Notably, a single injection of the selective ASIC3 antagonist APETx2 dramatically reduced MMBP in the model. Mechanistic investigations in primary DRG neurons cocultured with JJN3 cells showed increased neurite outgrowth and excitation inhibited by bafilomycin A1 or APETx2. Furthermore, combining APETx2 with bafilomycin A1 reduced MMBP to a greater extent than either agent alone. Finally, combining bafilomycin A1 with the osteoclast inhibitor zoledronic acid was sufficient to ameliorate MMBP, which was refractory to zoledronic acid. Overall, our results show that osteoclasts and multiple myeloma cooperate to induce an acidic bone microenvironment that evokes MMBP as a result of the excitation of ASIC3-activated sensory neurons. Furthermore, they present a mechanistic rationale for targeting ASIC3 on neurons along with the multiple myeloma-induced acidic bone microenvironment as a strategy to relieve MMBP in patients. Cancer Res; 77(6); 1283-95. ©2017 AACR. (Link to Publication Site) ● Publication site (DOI): 10.1158/0008-5472.CAN-15-3545 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28254863 ● Search Scopus @ Elsevier (PMID): 28254863 ● Search Scopus @ Elsevier (DOI): 10.1158/0008-5472.CAN-15-3545 (DOI: 10.1158/0008-5472.CAN-15-3545, PubMed: 28254863)
38.	Ariunzaya Bat-Erdene, Hirokazu Miki, Asuko Oda, Shingen Nakamura, Jumpei Teramachi, Ryota Amachi, Hirofumi Tenshin, Masahiro Hiasa, Masami Iwasa, Takeshi Harada, Shiroh Fujii, Kimiko Sogabe, Kumiko Kagawa, Sumiko Yoshida, Itsuro Endo, Ken-ichi Aihara and Masahiro Abe : Synergistic targeting of Sp1, a critical transcription factor for myeloma cell growth and survival, by panobinostat and proteasome inhibitors., Oncotarget, Vol.7, No.48, 79064-79075, 2016. (Summary) Panobinostat, a pan-deacetylase inhibitor, synergistically elicits cytotoxic activity against myeloma (MM) cells in combination with the proteasome inhibitor bortezomib. Because precise mechanisms for panobinostat's anti-MM action still remain elusive, we aimed to clarify the mechanisms of anti-MM effects of panobinostat and its synergism with proteasome inhibitors. Although the transcription factor Sp1 was overexpressed in MM cells, the Sp1 inhibitor terameprocol induced MM cell death in parallel with reduction of IRF4 and cMyc. Panobinostat induced activation of caspase-8, which was inversely correlated with reduction of Sp1 protein levels in MM cells. The panobinostat-mediated effects were further potentiated to effectively induce MM cell death in combination with bortezomib or carfilzomib even at suboptimal concentrations as a single agent. Addition of the caspase-8 inhibitor z-IETD-FMK abolished the Sp1 reduction not only by panobinostat alone but also by its combination with bortezomib, suggesting caspase-8-mediated Sp1 degradation. The synergistic Sp1 reduction markedly suppressed Sp1-driven prosurvival factors, IRF4 and cMyc. Besides, the combinatory treatment reduced HDAC1, another Sp1 target, in MM cells, which may potentiate HDAC inhibition. Collectively, caspase-8-mediated post-translational Sp1 degradation appears to be among major mechanisms for synergistic anti-MM effects of panobinostat and proteasome inhibitors in combination. (Tokushima University Institutional Repository) ● Metadata: 109988 (Link to Publication Site) ● Publication site (DOI): 10.18632/oncotarget.12594 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27738323 ● Search Scopus @ Elsevier (PMID): 27738323 ● Search Scopus @ Elsevier (DOI): 10.18632/oncotarget.12594 (Tokushima University Institutional Repository: 109988, DOI: 10.18632/oncotarget.12594, PubMed: 27738323)
39.	Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, Takeshi Harada, Asuka Oda, Shingen Nakamura, Derek Hanson, Keiichiro Watanabe, Shiroh Fujii, Hirokazu Miki, Kumiko Kagawa, Masami Iwasa, Itsuro Endo, Takeshi Kondo, Sumiko Yoshida, Ken-ichi Aihara, Kiyoe Kurahashi, Yoshiaki Kuroda, Hideaki Horikawa, Eiji Tanaka, Masahiro Abe and Toshio Matsumoto : A vicious cycle between acid sensing and survival signaling in myeloma cells: acid-induced epigenetic alteration., Oncotarget, Vol.7, No.43, 70447-70461, 2016. (Summary) Myeloma (MM) cells and osteoclasts are mutually interacted to enhance MM growth while creating acidic bone lesions. Here, we explored acid sensing of MM cells and its role in MM cell response to acidic conditions. Acidic conditions activated the PI3K-Akt signaling in MM cells while upregulating the pH sensor transient receptor potential cation channel subfamily V member 1 (TRPV1) in a manner inhibitable by PI3K inhibition. The acid-activated PI3K-Akt signaling facilitated the nuclear localization of the transcription factor Sp1 to trigger the expression of its target genes, including TRPV1 and HDAC1. Consistently, histone deacetylation was enhanced in MM cells in acidic conditions, while repressing a wide variety of genes, including DR4. Indeed, acidic conditions deacetylated histone H3K9 in a DR4 gene promoter and curtailed DR4 expression in MM cells. However, inhibition of HDAC as well as either Sp1 or PI3K was able to restore DR4 expression in MM cells suppressed in acidic conditions. These results collectively demonstrate that acid activates the TRPV1-PI3K-Akt-Sp1 signaling in MM cells while inducing HDAC-mediated gene repression, and suggest that a positive feedback loop between acid sensing and the PI3K-Akt signaling is formed in MM cells, leading to MM cell response to acidic bone lesions. (Tokushima University Institutional Repository) ● Metadata: 113048 (Link to Publication Site) ● Publication site (DOI): 10.18632/oncotarget.11927 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27626482 ● Search Scopus @ Elsevier (PMID): 27626482 ● Search Scopus @ Elsevier (DOI): 10.18632/oncotarget.11927 (Tokushima University Institutional Repository: 113048, DOI: 10.18632/oncotarget.11927, PubMed: 27626482)
40.	Jesus Delgado-Calle, Judith Anderson, Meloney D. Cregor, Masahiro Hiasa, John M. Chirgwin, Nadia Carlesso, Toshiyuki Yoneda, Khalid S. Mohammad, Lilian I. Plotkin, G David Roodman and Teresita Bellido : Bidirectional Notch Signaling and Osteocyte-Derived Factors in the Bone Marrow Microenvironment Promote Tumor Cell Proliferation and Bone Destruction in Multiple Myeloma., Cancer Research, Vol.76, No.5, 1089-1100, 2016. (Summary) In multiple myeloma, an overabundance of monoclonal plasma cells in the bone marrow induces localized osteolytic lesions that rarely heal due to increased bone resorption and suppressed bone formation. Matrix-embedded osteocytes comprise more than 95% of bone cells and are major regulators of osteoclast and osteoblast activity, but their contribution to multiple myeloma growth and bone disease is unknown. Here, we report that osteocytes in a mouse model of human MM physically interact with multiple myeloma cells in vivo, undergo caspase-3-dependent apoptosis, and express higher RANKL (TNFSF11) and sclerostin levels than osteocytes in control mice. Mechanistic studies revealed that osteocyte apoptosis was initiated by multiple myeloma cell-mediated activation of Notch signaling and was further amplified by multiple myeloma cell-secreted TNF. The induction of apoptosis increased osteocytic Rankl expression, the osteocytic Rankl/Opg (TNFRSF11B) ratio, and the ability of osteocytes to attract osteoclast precursors to induce local bone resorption. Furthermore, osteocytes in contact with multiple myeloma cells expressed high levels of Sost/sclerostin, leading to a reduction in Wnt signaling and subsequent inhibition of osteoblast differentiation. Importantly, direct contact between osteocytes and multiple myeloma cells reciprocally activated Notch signaling and increased Notch receptor expression, particularly Notch3 and 4, stimulating multiple myeloma cell growth. These studies reveal a previously unknown role for bidirectional Notch signaling that enhances MM growth and bone disease, suggesting that targeting osteocyte-multiple myeloma cell interactions through specific Notch receptor blockade may represent a promising treatment strategy in multiple myeloma. Cancer Res; 76(5); 1089-100. ©2016 AACR. (Link to Publication Site) ● Publication site (DOI): 10.1158/0008-5472.CAN-15-1703 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26833121 ● Summary page in Scopus @ Elsevier: 2-s2.0-84961683824 (DOI: 10.1158/0008-5472.CAN-15-1703, PubMed: 26833121, Elsevier: Scopus)
41.	James Derek Hanson, Shingen Nakamura, Ryota Amachi, Masahiro Hiasa, Asuka Oda, Daisuke Tsuji, Kohji Itoh, Takeshi Harada, Kazuki Horikawa, Jumpei Teramachi, Hirokazu Miki, Toshio Matsumoto and Masahiro Abe : Effective impairment of myeloma cells and their progenitors by blockade of monocarboxylate transportation., Oncotarget, Vol.6, No.32, 33568-33586, 2015. (Summary) Cancer cells robustly expel lactate produced through enhanced glycolysis via monocarboxylate transporters (MCTs) and maintain alkaline intracellular pH. To develop a novel therapeutic strategy against multiple myeloma (MM), which still remains incurable, we explored the impact of perturbing a metabolism via inhibiting MCTs. All MM cells tested constitutively expressed MCT1 and MCT4, and most expressed MCT2. Lactate export was substantially suppressed to induce death along with lowering intracellular pH in MM cells by blockade of all three MCT molecules with -cyano-4-hydroxy cinnamate (CHC) or the MCT1 and MCT2 inhibitor AR-C155858 in combination with MCT4 knockdown, although only partially by knockdown of each MCT. CHC lowered intracellular pH and severely curtailed lactate secretion even when combined with metformin, which further lowered intracellular pH and enhanced cytotoxicity. Interestingly, an ambient acidic pH markedly enhanced CHC-mediated cytotoxicity, suggesting preferential targeting of MM cells in acidic MM bone lesions. Furthermore, treatment with CHC suppressed hexokinase II expression and ATP production to reduce side populations and colony formation. Finally, CHC caused downregulation of homing receptor CXCR4 and abrogated SDF-1-induced migration. Targeting tumor metabolism by MCT blockade therefore may become an effective therapeutic option for drug-resistant MM cells with elevated glycolysis. (Tokushima University Institutional Repository) ● Metadata: 109501 (Link to Publication Site) ● Publication site (DOI): 10.18632/oncotarget.5598 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26384349 ● Summary page in Scopus @ Elsevier: 2-s2.0-84946086135 (Tokushima University Institutional Repository: 109501, DOI: 10.18632/oncotarget.5598, PubMed: 26384349, Elsevier: Scopus)
42.	Toshiyuki Yoneda, Masahiro Hiasa, Yuki Nagata, Tatsuo Okui and Fletcher A. White : Acidic microenvironment and bone pain in cancer-colonized bone., BoneKEy Reports, Vol.4, 690, 2015. (Summary) Solid cancers and hematologic cancers frequently colonize bone and induce skeletal-related complications. Bone pain is one of the most common complications associated with cancer colonization in bone and a major cause of increased morbidity and diminished quality of life, leading to poor survival in cancer patients. Although the mechanisms responsible for cancer-associated bone pain (CABP) are poorly understood, it is likely that complex interactions among cancer cells, bone cells and peripheral nerve cells contribute to the pathophysiology of CABP. Clinical observations that specific inhibitors of osteoclasts reduce CABP indicate a critical role of osteoclasts. Osteoclasts are proton-secreting cells and acidify extracellular bone microenvironment. Cancer cell-colonized bone also releases proton/lactate to avoid intracellular acidification resulting from increased aerobic glycolysis known as the Warburg effect. Thus, extracellular microenvironment of cancer-colonized bone is acidic. Acidosis is algogenic for nociceptive sensory neurons. The bone is densely innervated by the sensory neurons that express acid-sensing nociceptors. Collectively, CABP is evoked by the activation of these nociceptors on the sensory neurons innervating bone by the acidic extracellular microenvironment created by bone-resorbing osteoclasts and bone-colonizing cancer cells. As current treatments do not satisfactorily control CABP and can elicit serious side effects, new therapeutic interventions are needed to manage CABP. Understanding of the cellular and molecular mechanism by which the acidic extracellular microenvironment is created in cancer-colonized bone and by which the expression and function of the acid-sensing nociceptors on the sensory neurons are regulated would facilitate to develop novel therapeutic approaches for the management of CABP. (Link to Publication Site) ● Publication site (DOI): 10.1038/bonekey.2015.58 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25987988 ● Search Scopus @ Elsevier (PMID): 25987988 ● Search Scopus @ Elsevier (DOI): 10.1038/bonekey.2015.58 (DOI: 10.1038/bonekey.2015.58, PubMed: 25987988)
43.	Toshiyuki Yoneda, Masahiro Hiasa, Yuki Nagata, Tatsuo Okui and Fletcher White : Contribution of acidic extracellular microenvironment of cancer-colonized bone to bone pain., Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol.1848, No.10, 2677-2684, 2015. (Summary) Solid and hematologic cancer colonized bone produces a number of pathologies. One of the most common complications is bone pain. Cancer-associated bone pain (CABP) is a major cause of increased morbidity and diminishes the quality of life and affects survival. Current treatments do not satisfactorily control CABP and can elicit adverse effects. Thus, new therapeutic interventions are needed to manage CABP. However, the mechanisms responsible for CABP are poorly understood. The observation that specific osteoclast inhibitors can reduce CABP in patients indicates a critical role of osteoclasts in the pathophysiology of CABP. Osteoclasts create an acidic extracellular microenvironment by secretion of protons via vacuolar proton pumps during bone resorption. In addition, bone-colonized cancer cells also release protons and lactate via plasma membrane pH regulators to avoid intracellular acidification resulting from increased aerobic glycolysis known as the Warburg effect. Since acidosis is algogenic for sensory neurons and bone is densely innervated by sensory neurons that express acid-sensing nociceptors, the acidic bone microenvironments can evoke CABP. Understanding of the mechanism by which the acidic extracellular microenvironment is created in cancer-colonized bone and the expression and function of the acid-sensing nociceptors are regulated should facilitate the development of novel approaches for management of CABP. Here, the contribution of the acidic microenvironment created in cancer-colonized bone to elicitation of CABP and potential therapeutic implications of blocking the development and recognition of acidic microenvironment will be described. This article is part of a Special Issue entitled: Membrane channels and transporters in cancers. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbamem.2015.02.004 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25687976 ● Summary page in Scopus @ Elsevier: 2-s2.0-84941260672 (DOI: 10.1016/j.bbamem.2015.02.004, PubMed: 25687976, Elsevier: Scopus)
44.	Hirokazu Miki, Shingen Nakamura, A Oda, R Amachi, Keiichiro Watanabe, D Hanson, Jumpei Teramachi, Masahiro Hiasa, H Yagi, K Sogabe, M Takahashi, T Maruhashi, K Udaka, T Harada, Shiroh Fujii, A Nakano, Kumiko Kagawa, M Ri, S Iida, Shuji Ozaki, T Matsumoto and Masahiro Abe : Induction of endoplasmic reticulum stress by bortezomib sensitizes myeloma cells to DR5-mediated cell death, International Journal of Myeloma, Vol.5, No.1, 1-7, 2015. (Summary) <p>TNF-related apoptosis-including ligand/Apo2 (TRAIL)-mediated immunotherapy is an attractive anti-tumor modality with high tumor specificity. In order to improve its therapeutic efficacy, we further need to implement a novel maneuver for sensitization of malignant cells to TRAIL. Bortezomib (BTZ), a novel anti-myeloma (MM) agent, potently induces endoplasmic reticulum (ER) stress to cause apoptosis. Here, we explored the roles of BTZ in the cytotoxicity of anti-TRAIL receptor agonistic antibodies against MM cells with special reference to ER stress. BTZ enhanced the expression of death receptor 5 (DR5) but not DR4 in MM cells at surface protein as well as mRNA levels. However, the DR5 expression was not affected by BTZ without ER stress induction in MM cells with a point mutation in a BTZ-binding proteasome β<sub>5</sub> subunit. Tunicamycin, an ER stress inducer, was able to enhance the DR5 expression even in the BTZ-resistant MM cells, suggesting the role of ER stress in up-regulation of DR5 expression. Interestingly, BTZ facilitated extrinsic caspase-mediated apoptosis by anti-DR5 agonistic antibody in MM cells along with reducing c-FLICE-like interleukin protein, a caspase 8 inhibitor. These results suggest that BTZ enhances DR5 expression and its downstream apoptotic signaling through ER stress to sensitize MM cells to TRAIL-mediated immunotherapy.</p> (Keyword) multiple myeloma / bortezomib / TRAIL / DR5 / ER stress (Link to Publication Site) ● Publication site (DOI): 10.57352/ijm.5.1_1 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390292815284471040 ● Search Scopus @ Elsevier (DOI): 10.57352/ijm.5.1_1 (DOI: 10.57352/ijm.5.1_1, CiNii: 1390292815284471040)
45.	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. (Summary) 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. (Link to Publication Site) ● Publication site (DOI): 10.1038/leu.2014.147 (Link to Search Site for Scientific Articles) ● 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)
46.	Shinya Horiuchi, Masahiro Hiasa, Akihiro Yasue, Kazumitsu Sekine, Kenichi Hamada, Kenzo Asaoka and Eiji Tanaka : Fabrications of zinc-releasing biocement combining zinc calcium phosphate to calcium phosphate cement., Journal of the Mechanical Behavior of Biomedical Materials, Vol.29C, 151-160, 2014. (Summary) Recently, zinc-releasing bioceramics have been the focus of much attention owing to their bone-forming ability. Thus, some types of zinc-containing calcium phosphate (e.g., zinc-doped tricalcium phosphate and zinc-substituted hydroxyapatite) are examined and their osteoblastic cell responses determined. In this investigation, we studied the effects of zinc calcium phosphate (ZCP) derived from zinc phosphate incorporated into calcium phosphate cement (CPC) in terms of its setting reaction and MC3T3-E1 osteoblast-like cell responses. Compositional analysis by powder X-ray diffraction analysis revealed that HAP crystals were precipitated in the CPC containing 10 or 30wt% ZCP after successfully hardening. However, the crystal growth observed by scanning electron microscopy was delayed in the presence of additional ZCP. These findings indicate that the additional zinc inhibits crystal growth and the conversion of CPC to the HAP crystals. The proliferation of the cells and alkaline phosphatase (ALP) activity were enhanced when 10wt% ZCP was added to CPC. Taken together, ZCP added CPC at an appropriate fraction has a potent promotional effect on bone substitute biomaterials. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jmbbm.2013.09.005 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24090874 ● Summary page in Scopus @ Elsevier: 2-s2.0-84884959362 (DOI: 10.1016/j.jmbbm.2013.09.005, PubMed: 24090874, Elsevier: Scopus)
47.	Shingen Nakamura, Hirokazu Miki, Shinsuke Kido, Ayako Nakano, Masahiro Hiasa, Asuka Oda, Hiroe Amou, Keiichiro Watanabe, Takeshi Harada, Shiroh Fujii, Kyoko Takeuchi, Kumiko Kagawa, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Activating transcription factor 4, an ER stress mediator, is required for, but exce ssive ER stress suppresses osteoblastogenesis by bortezomib., International Journal of Hematology, Vol.98, No.1, 66-73, 2013. (Summary) Endoplasmic reticulum (ER) stress is induced in matrix-producing osteoblasts and plays an essential role in osteoblastogenesis. Although the bone anabolic activity of proteasome inhibitors has been demonstrated, the roles of ER stress induced by proteasome inhibition in osteoblastogenesis remain largely unknown. Here we show that bortezomib translationally increases protein levels of activating transcription factor 4 (ATF4), a downstream mediator of ER stress, in bone marrow stromal cells and MC3T3-E1 preosteoblastic cells. The suppression of ATF4 expression by siRNA abrogated osteocalcin expression and mineralized nodule formation by MC3T3-E1 cells induced by bortezomib, indicating a critical role for ATF4 in bortezomib-mediated osteoblastogenesis. However, bortezomib at 20 nM or higher abolished the mineralized nodule formation along with reductions in the expression of osteoblastogenesis mediators β-catenin and Osterix. Furthermore, at 50 nM, bortezomib induced the expression of C/EBP homologous protein (CHOP), suggesting activation of the ATF4-CHOP pro-apoptotic pathway. These results suggest that a low dose of bortezomib induces osteogenic activity, but that, in contrast, excessive ER stress caused by bortezomib at higher doses hampers osteoblastogenesis. Therefore, dosing schedules for proteasome inhibitors warrant further study to maximize anabolic actions without compromising anti-MM activity in patients with multiple myeloma (MM). (Keyword) 3T3 Cells / Activating Transcription Factor 4 / Animals / Antineoplastic Agents / Biological Markers / Bone Marrow Cells / Boronic Acids / Calcification, Physiologic / Cells, Cultured / Endoplasmic Reticulum Stress / Gene Expression Regulation / Gene Silencing / Humans / Mice / Multiple Myeloma / Neoplasm Proteins / Osteoblasts / Osteocalcin / Osteogenesis / Proteasome Inhibitors / Pyrazines / RNA, Small Interfering / Stromal Cells (Tokushima University Institutional Repository) ● Metadata: 105938 (Link to Publication Site) ● Publication site (DOI): 10.1007/s12185-013-1367-z (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23708974 ● Summary page in Scopus @ Elsevier: 2-s2.0-84880304849 (Tokushima University Institutional Repository: 105938, DOI: 10.1007/s12185-013-1367-z, PubMed: 23708974, Elsevier: Scopus)
48.	Hirokazu Miki, Shingen Nakamura, Shuji Ozaki, A Oda, H Amou, Akishige Ikegame, Keiichiro Watanabe, Masahiro Hiasa, Q Cui, T Harada, Shiroh Fujii, A Nakano, Kumiko Kagawa, Kyoko Takeuchi, Ken-ichiro Yata, A Sakai, Masahiro Abe and Toshio Matsumoto : KRN5500, a spicamycin derivative, exerts anti-myeloma effects through impairing both myeloma cells and osteoclasts., British Journal of Haematology, Vol.155, No.3, 328-339, 2011. (Summary) The spicamycin analogue KRN5500 alters glycoprotein processing and induces damage in the endoplasmic reticulum (ER)-Golgi apparatus in cancer cells. In the present study, we explored the cytotoxic effects of KRN5500 on multiple myeloma (MM) cells and the bone marrow microenvironment with special reference to ER stress. Cell proliferation assay showed that KRN5500 induced G1 arrest and apoptosis in MM cells in a time- and dose-dependent manner. KRN5500 enhanced ER stress independently of caspase activation in MM cells. This cell death was observed even in the presence of bone marrow stroma cells or osteoclasts. Notably, KRN5500 induced cell death also in osteoclasts. In vivo effects of KRN5500 were evaluated using two xenograft models established in severe combined immunodeficient (SCID) mice by either subcutaneous injection of RPMI 8226 cells or intra-bone injection of INA-6 cells to subcutaneously implanted rabbit bones (SCID-rab model). KRN5500 significantly inhibited tumour growth in both animal models, and decreased the number of osteoclasts, which resulted in prevention of bone destruction in the SCID-rab model. These results suggest that KRN5500 exerts anti-MM effects through impairing both MM cells and osteoclasts. Therefore, this unique mechanism of KRN5500 might be a useful therapeutic option in patients with MM. (Keyword) Animals / Apoptosis / Bone Marrow Cells / Caspases / Cell Line, Tumor / Cell Proliferation / Dose-Response Relationship, Drug / Female / G1 Phase / Humans / Mice / Mice, SCID / Multiple Myeloma / Osteoclasts / Purine Nucleosides / Rabbits / Random Allocation / Stromal Cells / Tumor Microenvironment / Xenograft Model Antitumor Assays (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1365-2141.2011.08844.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21902681 ● Search Scopus @ Elsevier (PMID): 21902681 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1365-2141.2011.08844.x (DOI: 10.1111/j.1365-2141.2011.08844.x, PubMed: 21902681)
49.	Naoko Yoneda, Masahiro Hiasa, 井上雅秀, 長山智子, 吉田亮彦, 森博世, Shinji Fujihara, Shinya Horiuchi and Eiji Tanaka : インプラント固定に関する臨床統計学的研究, The Journal of Chu-Shikoku Orthodontic Society, Vol.23, No.1, 69-76, 2011.
50.	Shinya Horiuchi, Shingo Kuroda, Masahiro Hiasa, Toshiyuki Suge, Seitaro Saku, Kenichi Hamada, Takashi Matsuo, Kenzo Asaoka and Eiji Tanaka : Reinforcement of bond strength of self-etching orthodontic adhesive., The Angle Orthodontist, Vol.82, No.1, 30-35, 2011. (Summary) Abstract Objective: To determine the reinforcement of bond strength of a self-etching system by applying a pretreatment agent. Materials and Methods: Sixty extracted human premolars were used in this study. The enamel surfaces were treated with four pretreatment agents?phosphoric acid, polyacrylic acid, citric acid, and ammonium hexafluorosilicate (SiF)?and were examined under a scanning electron microscope. Afterward, orthodontic brackets were bonded with a self-etching adhesive system (n ?=? 10 for each agent), and shear bond strength was measured through a debonding process. The adhesive remnant index (ARI) was also assessed. Results: Enamel surfaces treated with polyacrylic acid seemed almost the same as intact enamel. Treatment with SiF induced slight shallow depressions compared with the intact enamel. On the other hand, enamel surfaces treated with citric acid and phosphoric acid showed severe etching patterns. All pretreatments increased the bond strength, but SiF-treated specimens revealed the greatest strength (12.201 ? 1.048?MPa), followed by polyacrylic acid (12.030 ? 2.103?MPa). The control group with no pretreatment showed the least strength (9.078 ? 1.678?MPa). All pretreatments increased ARI score compared with the control group. Conclusions: Surface conditioning before bracket adhesion could reinforce the bond strength of the self-etching adhesive system, resulting in a more reliable bonding system. (Link to Publication Site) ● Publication site (DOI): 10.2319/012011-39.1 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21751834 ● Search Scopus @ Elsevier (PMID): 21751834 ● Search Scopus @ Elsevier (DOI): 10.2319/012011-39.1 (DOI: 10.2319/012011-39.1, PubMed: 21751834)
51.	Qu Cui, Hironobu Shibata, Asuka Oda, Hiroe Amou, Ayako Nakano, Kenichiro Yata, Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Takeshi Harada, Shiroh Fujii, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Targeting myeloma-osteoclast interaction with V9V2 T cells., International Journal of Hematology, Vol.94, No.1, 63-70, 2011. (Summary) Multiple myeloma (MM) cells stimulate osteoclastogenesis, and osteoclasts (OCs) in turn enhance MM growth and drug resistance, resulting in a vicious cycle. V9V2 T cells exert potent anti-tumor effects, making T cell-based immunotherapies using these cells attractive candidates for currently incurable malignancies, such as MM. However, the impact of such treatments on the MM-OC interaction is largely unknown. We demonstrate here that V9V2 T cells expanded by zoledronic acid and IL-2 exerted potent cytotoxic effects on both MM cells and OCs, even in coculture settings, but showed no such effect on bone marrow stromal cells. V9V2 T cells marginally affected colony formation from normal hematopoietic progenitors, and furthermore migrated toward osteopontin and MIP-1, factors produced by the MM-OC interaction. These results suggest that V9V2 T cells expanded by zoledronic acid and IL-2 are able to migrate to MM bone lesions and preferentially target OCs as well as MM cells, thereby inhibiting both tumor expansion and bone destruction. (Link to Publication Site) ● Publication site (DOI): 10.1007/s12185-011-0885-9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21698356 ● Search Scopus @ Elsevier (PMID): 21698356 ● Search Scopus @ Elsevier (DOI): 10.1007/s12185-011-0885-9 (DOI: 10.1007/s12185-011-0885-9, PubMed: 21698356)
52.	Ayako Nakano, Masahiro Abe, Asuka Oda, Hiroe Amou, Masahiro Hiasa, Shingen Nakamura, Hirokazu Miki, Takeshi Harada, Shirou Fujii, Kumiko Kagawa, Kyoko Takeuchi, Takashi Watanabe, Shuji Ozaki and Toshio Matsumoto : Delayed treatment with vitamin C and N-acetyl-L: -cysteine protects Schwann cells without compromising the anti-myeloma activity of bortezomib., International Journal of Hematology, Vol.93, No.6, 727-735, 2011. (Summary) Bortezomib-induced peripheral neuropathy (BIPN) emerges as a disabling adverse effect. As rat models for BIPN have demonstrated damage in nerve Schwann cells, we screened for cytoprotective agents to devise a method of rescuing Schwann cells from the cytotoxic effects of bortezomib without compromising its anti-myeloma effects. Schwann cells underwent macroautophagy along with cytoplasmic inclusion body and vacuole formation, and appeared much less susceptible to bortezomib-induced cytotoxicity than did myeloma cells. Vitamin C or N-acetyl-L: -cysteine (NAC) achieved near-complete rescue of Schwann cells treated with bortezomib at 30 nM or less, and these agents in combination are able to cooperatively inhibit the morphological changes and the cytotoxicity in Schwann cells with higher doses of bortezomib. The delayed addition of vitamin C and/or NAC after the exposure to bortezomib alleviated the cytotoxicity in Schwann cells but not myeloma cells. These results suggest that delayed treatment with these agents may be instrumental in prophylaxis of BIPN. (Link to Publication Site) ● Publication site (DOI): 10.1007/s12185-011-0850-7 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21526377 ● Search Scopus @ Elsevier (PMID): 21526377 ● Search Scopus @ Elsevier (DOI): 10.1007/s12185-011-0850-7 (DOI: 10.1007/s12185-011-0850-7, PubMed: 21526377)
53.	J Asano, A Nakano, A Oda, H Amou, Masahiro Hiasa, Kyoko Takeuchi, H Miki, S Nakamura, T Harada, Shiroh Fujii, Kumiko Kagawa, Itsuro Endo, Ken-ichiro Yata, A Sakai, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : The serine/threonine kinase Pim-2 is a novel anti-apoptotic mediator in myeloma cells., Leukemia, 2011. (Summary) Bone marrow stromal cells (BMSCs) and osteoclasts (OCs) confer multiple myeloma (MM) cell survival through elaborating factors. We demonstrate herein that IL-6 and TNF family cytokines, TNF, BAFF and APRIL, but not IGF-1 cooperatively enhance the expression of the serine/threonine kinase Pim-2 in MM cells. BMSCs and OCs upregulate Pim-2 expression in MM cells largely via the IL-6/STAT3 and NF-B pathway, respectively. Pim-2 short interfering RNA reduces MM cell viability in cocultures with BMSCs or OCs. Thus, upregulation of Pim-2 appears to be a novel anti-apoptotic mechanism for MM cell survival. Interestingly, the mammalian target of rapamycin inhibitor rapamycin further suppresses the MM cell viability in combination with the Pim-2 silencing. The Pim inhibitor (Z)-5-(4-propoxybenzylidene) thiazolidine-2, 4-dione and the PI3K inhibitor LY294002 cooperatively enhance MM cell death. The Pim inhibitor suppresses 4E-BP1 phosphorylation along with the reduction of Mcl-1 and c-Myc. Pim-2 may therefore become a new target for MM treatment.Leukemia advance online publication, 8 April 2011; doi:10.1038/leu.2011.60. (Tokushima University Institutional Repository) ● Metadata: 106134 (Link to Publication Site) ● Publication site (DOI): 10.1038/leu.2011.60 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21475253 ● Search Scopus @ Elsevier (PMID): 21475253 ● Search Scopus @ Elsevier (DOI): 10.1038/leu.2011.60 (Tokushima University Institutional Repository: 106134, DOI: 10.1038/leu.2011.60, PubMed: 21475253)
54.	Kazuma Matsumoto, Nobuhiko Kawai, Takashi Izawa, Shinji Fujihara, Saika Nakamura, Ritsuko 徳永律子 Oura, Kazuna Takahara, Masahiro Hiasa and Eiji Tanaka : A comprehensive treatment case of severe deep bite with oligodontia, The Journal of Chu-Shikoku Orthodontic Society, Vol.22, No.1, 49-56, 2010.
55.	Kyoko Takeuchi, Masahiro Abe, Masahiro Hiasa, Asuka Oda, Hiroe Amou, Shinsuke Kido, Takeshi Harada, Osamu Tanaka, Hirokazu Miki, Shingen Nakamura, Ayako Nakano, Kumiko Kagawa, Kenichiro Yata, Shuji Ozaki and Toshio Matsumoto : Tgf-Beta inhibition restores terminal osteoblast differentiation to suppress myeloma growth., PLoS ONE, Vol.5, No.3, e9870, 2010. (Summary) BACKGROUND: Multiple myeloma (MM) expands almost exclusively in the bone marrow and generates devastating bone lesions, in which bone formation is impaired and osteoclastic bone resorption is enhanced. TGF-beta, a potent inhibitor of terminal osteoblast (OB) differentiation, is abundantly deposited in the bone matrix, and released and activated by the enhanced bone resorption in MM. The present study was therefore undertaken to clarify the role of TGF-beta and its inhibition in bone formation and tumor growth in MM. METHODOLOGY/PRINCIPAL FINDINGS: TGF-beta suppressed OB differentiation from bone marrow stromal cells and MC3T3-E1 preosteoblastic cells, and also inhibited adipogenesis from C3H10T1/2 immature mesenchymal cells, suggesting differentiation arrest by TGF-beta. Inhibitors for a TGF-beta type I receptor kinase, SB431542 and Ki26894, potently enhanced OB differentiation from bone marrow stromal cells as well as MC3T3-E1 cells. The TGF-beta inhibition was able to restore OB differentiation suppressed by MM cell conditioned medium as well as bone marrow plasma from MM patients. Interestingly, TGF-beta inhibition expedited OB differentiation in parallel with suppression of MM cell growth. The anti-MM activity was elaborated exclusively by terminally differentiated OBs, which potentiated the cytotoxic effects of melphalan and dexamethasone on MM cells. Furthermore, TGF-beta inhibition was able to suppress MM cell growth within the bone marrow while preventing bone destruction in MM-bearing animal models. CONCLUSIONS/SIGNIFICANCE: The present study demonstrates that TGF-beta inhibition releases stromal cells from their differentiation arrest by MM and facilitates the formation of terminally differentiated OBs, and that terminally differentiated OBs inhibit MM cell growth and survival and enhance the susceptibility of MM cells to anti-MM agents to overcome the drug resistance mediated by stromal cells. Therefore, TGF-beta appears to be an important therapeutic target in MM bone lesions. (Link to Publication Site) ● Publication site (DOI): 10.1371/journal.pone.0009870 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20360846 ● Search Scopus @ Elsevier (PMID): 20360846 ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0009870 (DOI: 10.1371/journal.pone.0009870, PubMed: 20360846)
56.	Masahiro Hiasa, Masahiro Abe, Ayako Nakano, Asuka Oda, Hiroe Amou, Shinsuke Kido, Kyoko Takeuchi, Kumiko Kagawa, Kenichiro Yata, Toshihiro Hashimoto, Shuji Ozaki, Kenzo Asaoka, Eiji Tanaka, Keiji Moriyama and Toshio Matsumoto : GM-CSF and IL-4 induce dendritic cell differentiation and disrupt osteoclastogenesis through M-CSF receptor shedding by up-regulation of TNF-{alpha} converting enzyme (TACE), Blood, Vol.114, No.20, 4517-4526, 2009. (Summary) Monocytes give rise to macrophages, osteoclasts (OCs), and dendritic cells (DCs). M-CSF and RANK ligand induce OC differentiation from monocytes, while GM-CSF and IL-4 trigger monocytic differentiation into DCs. These two differentiation pathways occur in a mutually exclusive manner. However, regulatory mechanisms for the polarization of monocytic differentiation are still unclear. The present study was undertaken to clarify the mechanism of triggering the deflection of OC and DC differentiation from monocytes. GM-CSF and IL-4 abolished monocytic differentiation into OCs while inducing DC differentiation even in the presence of M-CSF and RANK ligand. GM-CSF and IL-4 in combination potently up-regulate TNF-alpha converting enzyme (TACE) expression and activity in monocytes, causing ectodomain shedding of the membrane-bound M-CSF receptor, resulting in the disruption of its phosphorylation by M-CSF as well as the induction of osteoclastogenesis from monocytes by M-CSF and RANK ligand. Interestingly, TACE inhibition robustly causes the resumption of the surface expression of M-CSF receptors on monocytes, which facilitates M-CSF-mediated phosphorylation of M-CSF receptors and macrophage/OC differentiation while impairing GM-CSF and IL-4-mediated DC differentiation from monocytes. These results reveal a novel proteolytic regulation of M-CSF receptor expression in monocytes to control M-CSF signaling and monocytic differentiation into macrophage/OC-lineage cells or DCs. (Keyword) ADAM Proteins / Blotting, Western / Cell Differentiation / Dendritic Cells / Fluorescent Antibody Technique / Granulocyte-Macrophage Colony-Stimulating Factor / Humans / Interleukin-4 / Macrophages / Monocytes / Osteoclasts / RANK Ligand / Receptor, Macrophage Colony-Stimulating Factor / Reverse Transcriptase Polymerase Chain Reaction / Up-Regulation (Link to Publication Site) ● Publication site (DOI): 10.1182/blood-2009-04-215020 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19762488 ● Search Scopus @ Elsevier (PMID): 19762488 ● Search Scopus @ Elsevier (DOI): 10.1182/blood-2009-04-215020 (DOI: 10.1182/blood-2009-04-215020, PubMed: 19762488)
57.	Ken-ichi Kitazoe, Masahiro Abe, Masahiro Hiasa, Asuka Oda, Hiroe Amou, Takeshi Harada, Ayako Nakano, Kyoko Takeuchi, Toshihiro Hashimoto, Ken-ichiro Yata, Shuji Ozaki and Toshio Matsumoto : Valproic acid exerts anti-tumor as well as anti-angiogenic effects on myeloma., International Journal of Hematology, Vol.89, No.1, 45-57, 2008. (Summary) Multiple myeloma is still an incurable disease, most commonly occurring in the elderly. The myeloma-induced bone marrow microenvironment protects myeloma cells from drug-induced apoptosis. Therefore, the development of novel and tolerable therapeutic alternatives to overcome the drug resistance is an important clinical issue. Valproic acid (VPA), a safe and widely used anti-epileptic agent, is revisited as a class I- and IIa-specific histone deacetylase inhibitor. In the present study, we evaluated the effect as well as a mechanism of actions of VPA on myeloma cell growth and survival, with special reference to the myeloma-induced bone marrow microenvironment. VPA at therapeutic concentrations for epilepsy induced cell death in primary CD138-positive myeloma cells as well as myeloma cell lines, but not in CD138-negative bone marrow cells. VPA suppressed osteoclastogenesis as well as osteoclast-mediated myeloma cell growth. VPA also inhibited vascular tubule formation enhanced by co-cultures of myeloma cells and osteoclasts in concert with thalidomide. In addition, VPA induced both caspase-dependent and -independent cell death in myeloma cells, and potentiated the anti-myeloma effects of melphalan and dexamethasone. Collectively, VPA is suggested to exert multi-factorial anti-myeloma actions, and may serve as a safe adjuvant to be included in conventional chemotherapies against myeloma. (Keyword) Antineoplastic Combined Chemotherapy Protocols / Bone Marrow / cell proliferation and differentiation / Cell Survival / Coculture Techniques / Drug Synergism / Histone Deacetylase Inhibitors / Humans / Multiple Myeloma / Osteoclasts / Thalidomide / Tumor Cells, Cultured / Valproic Acid (Link to Publication Site) ● Publication site (DOI): 10.1007/s12185-008-0226-9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19093163 ● Search Scopus @ Elsevier (PMID): 19093163 ● Search Scopus @ Elsevier (DOI): 10.1007/s12185-008-0226-9 (DOI: 10.1007/s12185-008-0226-9, PubMed: 19093163)
58.	Youichi Tanaka, Masahiro Abe, Masahiro Hiasa, Asuka Oda, Hiroe Amou, Ayako Nakano, Kyoko Takeuchi, Kenichi Kitazoe, Shinsuke Kido, Daisuke Inoue, Keiji Moriyama, Toshihiro Hashimoto, Shuji Ozaki and Toshio Matsumoto : Myeloma Cell-Osteoclast Interaction Enhances Angiogenesis Together with Bone Resorption: A Role for Vascular Endothelial Cell Growth Factor and Osteopontin, Clinical Cancer Research, Vol.13, No.3, 816-823, 2007. (Summary) Similar to osteoclastogenesis, angiogenesis is enhanced in the bone marrow in myeloma in parallel with tumor progression. We showed previously that myeloma cells and osteoclasts are mutually stimulated to form a vicious cycle to lead to enhance both osteoclastogenesis and tumor growth. The present study was undertaken to clarify whether myeloma cell-osteoclast interaction enhances angiogenesis and whether there is any mutual stimulation between osteoclastogenesis and angiogenesis. Myeloma cells and monocyte-derived osteoclasts were cocultured, and angiogenic activity produced by the cocultures was assessed with in vitro vascular tubule formation assays and human umbilical vascular endothelial cell (HUVEC) migration and survival. Osteoclastogenic activity was determined with rabbit bone cell cultures on dentine slices. Myeloma cells and osteoclasts constitutively secrete proangiogenic factors, vascular endothelial growth factor (VEGF) and osteopontin, respectively. A cell-to-cell interaction between myeloma cells and osteoclasts potently enhanced vascular tubule formation. Blockade of both VEGF and osteopontin actions almost completely abrogated such vascular tubule formation as well as migration and survival of HUVECs enhanced by conditioned medium from cocultures of myeloma cells and osteoclasts. Furthermore, these factors in combination triggered the production of osteoclastogenic activity by HUVEC. Osteoclast-derived osteopontin and VEGF from myeloma cells cooperatively enhance angiogenesis and also induce osteoclastogenic activity by vascular endothelial cells. These observations suggest the presence of a close link between myeloma cells, osteoclasts, and vascular endothelial cells to form a vicious cycle between bone destruction, angiogenesis, and myeloma expansion. (Keyword) Bone Resorption / Cell Movement / Cell Survival / Coculture Techniques / Culture Media, Conditioned / Disease Progression / Endothelium, Vascular / Humans / Monocytes / Multiple Myeloma / Neovascularization, Pathologic / Osteoclasts / Osteopontin / Umbilical Veins / Vascular Endothelial Growth Factor A (Link to Publication Site) ● Publication site (DOI): 10.1158/1078-0432.CCR-06-2258 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17289872 ● Search Scopus @ Elsevier (PMID): 17289872 ● Search Scopus @ Elsevier (DOI): 10.1158/1078-0432.CCR-06-2258 (DOI: 10.1158/1078-0432.CCR-06-2258, PubMed: 17289872)
59.	Masahiro Hiasa, Yasuo Oba and Keiji Moriyama : 広汎型侵襲性歯周炎を伴う上顎前突の成人症例, The Journal of Chu-Shikoku Orthodontic Society, Vol.18, No.1, 63-70, 2006.
60.	Masahiro Abe, Shinsuke Kido, Masahiro Hiasa, Nakano Ayako, Oda Asuka, Amou Hiroe and Toshio Matsumoto : BAFF and APRIL as osteoclast-derived survival factors for myeloma cells: a rationale for TACI-Fc tratment in patients with multiple myeloma., Leukemia, Vol.20, No.7, 1313-1315, 2006. (Keyword) B-Cell Activating Factor / Cell Survival / Humans / Immunoglobulin Fc Fragments / Multiple Myeloma / Osteoclasts / Transmembrane Activator and CAML Interactor Protein / Tumor Necrosis Factor Ligand Superfamily Member 13 (Link to Publication Site) ● Publication site (DOI): 10.1038/sj.leu.2404228 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16617317 ● Search Scopus @ Elsevier (PMID): 16617317 ● Search Scopus @ Elsevier (DOI): 10.1038/sj.leu.2404228 (DOI: 10.1038/sj.leu.2404228, PubMed: 16617317)

Academic Paper (Unrefereed Paper):

1.	Hirofumi Tenshin, Keiichiro Watanabe, Emiko Nakaue, Khurel-Ochir Tsendsuren, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : Identification of key determinant for predicting feasible mandibular molars distalization, Journal of Dental Sciences, 2022. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jds.2022.05.009 (Link to Search Site for Scientific Articles) ● Summary page in Scopus @ Elsevier: 2-s2.0-85132231189 (DOI: 10.1016/j.jds.2022.05.009, Elsevier: Scopus)

Review, Commentary:

1.	Takeshi Harada, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Myeloma-Bone Interaction: A Vicious Cycle via TAK1-PIM2 Signaling, Cancers, Vol.13, No.17, 4441, Sep. 2021. (Summary) Multiple myeloma (MM) has a propensity to develop preferentially in bone and form bone-destructive lesions. MM cells enhance osteoclastogenesis and bone resorption through activation of the RANKL-NF-κB signaling pathway while suppressing bone formation by inhibiting osteoblastogenesis from bone marrow stromal cells (BMSCs) by factors elaborated in the bone marrow and bone in MM, including the soluble Wnt inhibitors DKK-1 and sclerostin, activin A, and TGF-β, resulting in systemic bone destruction with loss of bone. Osteocytes have been drawn attention as multifunctional regulators in bone metabolism. MM cells induce apoptosis in osteocytes to trigger the production of factors, including RANKL, sclerostin, and DKK-1, to further exacerbate bone destruction. Bone lesions developed in MM, in turn, provide microenvironments suited for MM cell growth/survival, including niches to foster MM cells and their precursors. Thus, MM cells alter the microenvironments through bone destruction in the bone where they reside, which in turn potentiates tumor growth and survival, thereby generating a vicious loop between tumor progression and bone destruction. The serine/threonine kinases PIM2 and TAK1, an upstream mediator of PIM2, are overexpressed in bone marrow stromal cells and osteoclasts as well in MM cells in bone lesions. Upregulation of the TAK1-PIM2 pathway plays a critical role in tumor expansion and bone destruction, posing the TAK1-PIM2 pathway as a pivotal therapeutic target in MM. (Tokushima University Institutional Repository) ● Metadata: 117425 (Link to Publication Site) ● Publication site (DOI): 10.3390/cancers13174441 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34503251 ● Search Scopus @ Elsevier (PMID): 34503251 ● Search Scopus @ Elsevier (DOI): 10.3390/cancers13174441 (Tokushima University Institutional Repository: 117425, DOI: 10.3390/cancers13174441, PubMed: 34503251)
2.	Toshiyuki Yoneda, Masahiro Hiasa and Tatsuo Okui : Pain in Bone Colonized by Cancer, Encyclopedia of Bone Biology, 390-402, Jun. 2020. (Link to Publication Site) ● Publication site (DOI): 10.1016/B978-0-12-801238-3.11252-8 (Link to Search Site for Scientific Articles) ● Summary page in Scopus @ Elsevier: 2-s2.0-85117774584 (DOI: 10.1016/B978-0-12-801238-3.11252-8, Elsevier: Scopus)
3.	Toshiyuki Yoneda, Masahiro Hiasa and Tatsuo Okui : Crosstalk Between Sensory Nerves and Cancer in Bone., Current Osteoporosis Reports, Oct. 2018. (Summary) Sensory nerves (SNs) richly innervate bone and are a component of bone microenvironment. Cancer metastasis in bone, which is under the control of the crosstalk with bone microenvironment, induces bone pain via excitation of SNs innervating bone. However, little is known whether excited SNs in turn affect bone metastasis. Cancer cells colonizing bone promote neo-neurogenesis of SNs and excite SNs via activation of the acid-sensing nociceptors by creating pathological acidosis in bone, evoking bone pain. Denervation of SNs or inhibition of SN excitation decreases bone pain and cancer progression and increases survival in preclinical models. Importantly, patients with cancers with increased SN innervation complain of cancer pain and show poor outcome. SNs establish the crosstalk with cancer cells to contribute to bone pain and cancer progression in bone. Blockade of SN excitation may have not only analgesic effects on bone pain but also anti-cancer actions on bone metastases. (Link to Publication Site) ● Publication site (DOI): 10.1007/s11914-018-0489-x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30343404 ● Search Scopus @ Elsevier (PMID): 30343404 ● Search Scopus @ Elsevier (DOI): 10.1007/s11914-018-0489-x (DOI: 10.1007/s11914-018-0489-x, PubMed: 30343404)
4.	Masahiro Hiasa : [Bone and calcium metabolism associated with malignancy. Mechanism of cancer-induced bone pain.], Clinical Calcium, Vol.28, No.11, 1495-1502, 2018. (Summary) Patients with bone colonized cancer frequently suffer from severe uncontrollable cancer-associated bone pain(CABP)during the course of illness. However, since current treatments do not satisfactorily control CABP and can elicit serious side effects, new therapeutic strategyies are needed to manage CABP. According to the recent study including ours, the cancer cell and osteoclast created-acidic extracellular microenvironment is expected to be therapeutic target for CABP. (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30374006 ● Search Scopus @ Elsevier (PMID): 30374006 (PubMed: 30374006)

Proceeding of International Conference:

1.	Takeshi Harada, Asuka Oda, Yosuke Matsushita, Ryohei Sumitani, Yusuke Inoue, Tomoyo Hara, Masahiro Oura, Kimiko Sogabe, Tomoko Maruhashi, Mamiko Takahashi, Kiyoe Kurahashi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Masahiro Hiasa, Jumpei Teramachi, Toyomasa Katagiri and Masahiro Abe : ADAR1-dsRNA metabolism in myeloma cells with 1q amplification: a novel therapeutic target, 19th International Myeloma Society Annual Meeting, Aug. 2022.
2.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Asuka Oda, Takeshi Harada, Yoshiki Higa, Kimiko Sogabe, Masahiro Oura, Ryohei Sumitani, Tomoyo Hara, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : Mechanical unloading promotes bone destruction and myeloma tumor expansion, Cancer and bone society young investigator symposium, Online, Feb. 2022.
3.	Hirofumi Tenshin, Takeshi Harada, Yusuke Inoue, Jumpei Teramachi, Masahiro Hiasa, Sou Shimizu, Emiko Nakaue, Kotaro Tanimoto, Yoshiki Higa, Masahiro Oura, Kimiko Sogabe, Tomoyo Hara, Ryohei Sumitani, Tomoko Maruhashi, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Targeting SLAMF7 to disrupt myeloma-osteoclast interaction: elotuzumabs ADCC activity with Th1-like gamma delta T cells towards osteoclasts and myeloma cells., Cancer and bone society young investigator symposium, Feb. 2022.
4.	Takeshi Harada, Yusuke Inoue, Hirofumi Tenshin, Asuka Oda, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Novel strategy of elotuzumab and zoledronic acid with Th1-like T cells against myeloma, 18th International Myeloma Workshop, Wien, Sep. 2021.
5.	Takeshi Harada, Yusuke Inoue, Hirofumi Tenshin, Asuka Oda, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Induction of elotuzumabs ADCC activity by Th1-like T cells towards osteoclasts as well as myeloma cells, EHA2021 Virtual Congress, Jun. 2021.
6.	Hirofumi Tenshin, Takeshi Harada, 井上雄介, Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Masahiro Oura, Kimiko Sogabe, Tomoyo Hara, Tomoko Maruhashi, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : The anti-SLAMF7 elotuzumab enhances ADCC activity with Th1-like γδT cells towards osteoclasts and myeloma cells., The European Calcified Tissue Society 2021 Digital Congress 2021, web, Mar. 2021.
7.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Takeshi Harada, Eiji Tanaka, Kotaro Tanimoto, Sou Shimizu, Masahiro Oura, Kimiko Sogabe, Masahiro Abe, Toshio Matsumoto and Itsuro Endo : The novel therapeutic approaches with TAK1 inhibition against the aberrant NLRP3 inflammasome activation in rheumatoid arthritis, ECTS 2020 Digital Congress, Oct. 2020.
8.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Masahiro Abe and Eiji Tanaka : Immobilization accelerates bone loss and myeloma tumor expansion., 9th IOC, Yokohama, Oct. 2020.
9.	Takeshi Harada, Asuka Oda, Hiroto Ohguchi, Yohann Grondin, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi, Masahiro Oura, Kimiko Sogabe, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Hirokazu Miki, Kumiko Kagawa, Shuji Ozaki, Teru Hideshima, Kenneth C. Anderson and Masahiro Abe : Novel therapeutic rationale for targeting HDAC1 and PIM2 in multiple myeloma, 61th ASH Annual Meeting & Exposition, Orlando, Dec. 2019. (Link to Publication Site) ● Publication site (DOI): 10.1182/blood-2019-127679 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1182/blood-2019-127679 (DOI: 10.1182/blood-2019-127679)
10.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Ashtar Mohannad, Kotaro Tanimoto, Soh Shimizu, Takeshi Harada, Masahiro Oura, Kimiko Sogabe, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : The role of NLRP3 inflammasome activation in joint inflammation and destruction in rheumatoid arthritis: novel therapeutic approaches with TAK1 inhibition., 29th Australian and New Zealand Bone and Mineral Society Annual Scientific Meeting, Oct. 2019.
11.	Mai Kanai, Itsuro Endo, Yasuko Takahashi, Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Seiji Fukumoto, Masahiro Abe and Toshio Matsumoto : Establishment of model mice of FGF23-related hypophosphatemia induced by iron solution administration, ASBMR 2019, Orlando, Sep. 2019.
12.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Ashtar Mohannad, Kotaro Tanimoto, Masami Iwasa, Bat-Erdene Ariunzaya, Takeshi Harada, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1 inhibition effectively alleviates joint inflammation as well as bone destruction in rheumatoid arthritis: Suppression of NLRP3 inflammasome-mediated inflammation and osteoclastic bone resorption, American Society for Bone and Mineral Society Annual meeting 2019, Orlando, Florida, USA,, Sep. 2019.
13.	Jumpei Teramachi, Soh Shimizu, Hirofumi Tenshin, Bat-Erdene Ariunzaya, Masahiro Hiasa, Kotaro Tanimoto, Oda Asuka, Takeshi Harada, Mohannad Ashtar, Kotaro Tanimoto, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : A progressive auto-amplification loop in TAK1 expression and activation in MM cells., ASBMR 2019,, Orlando, Florida, USA., Sep. 2019.
14.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Oda Asuka, Ashtar Mohannad, Kotaro Tanimoto, Masami Iwasa, Bat-Erdene Ariunzaya, Takeshi Harada, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1 inhibition effectively alleviates joint inflammation as well as bone destruction in rheumatoid arthritis: Suppression of NLRP3 inflammasome-mediated inflammation and osteoclastic bone resorption., ASBMR 2019,, Orlando, Florida, USA., Sep. 2019.
15.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Masahiro Abe and Eiji Tanaka : Effective suppression of inflammasome-mediated joints destruction by TAK1 inhibition, 第97回IADR学術大会, Vancouver, Jun. 2019.
16.	Mohannad Ashtar, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Oda Asuka, Iwasa Masami, Takeshi Harada, Bat-Erdene Ariunzaya, Kimiko Sogabe, Masahiro Oura, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Toshio Matsumoto, Masahiro Abe and Eiji Tanaka : Peri-implantitis and the role of Febuxostat in osteoclast differentiation., AEEDC Dubai World Orthodontic Conference, Dubai, UAE, Feb. 2019.
17.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Oda Asuka, Bat-Erdene Ariunzaya, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Disruption of a progressive vicious cycle between myeloma tumor growth and bone destruction by TAK1 inhibition, ASBMR 2018 Annual Meeting, Montreal, Sep. 2018.
18.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Oda Asuka, Ashtar Mohannad, Kotaro Tanimoto, Iwasa Masami, Bat-Erdene Ariunzaya, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Opposite effects of TRAIL on the Sp-1-c-FLIP survival pathway in myeloma cells and osteoclasts., ASBMR 2018 Annual Meeting, Montreal, Sep. 2018.
19.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Oda Asuka, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Tatsuji Haneji, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Therapeutic impact of TAK1 inhibition on myeloma tumor progression and bone destruction, 8th International Workshop on Advances in the Molecular Pharmacology and Therapeutics of Bone and other Musculoskeletal Diseases and Cancer and Bone Society 2018 Meeting, Oxford, Jun. 2018.
20.	Hirofumi Tenshin, Jumpei Teramachi, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Toshio Matsumoto, Masahiro Abe and Eiji Tanaka : Apoptosis inducer TRAIL stimulates osteoclast differentiation and survival via TAK1 activation., 1st International Conference of Biophysical Technology in Dentistry (+10th International Scientific Meeting in Dentistry),, Makassar, Indonesia., Apr. 2018.
21.	Hirofumi Tenshin, Jumpei Teramachi, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Toshio Matsumoto, Masahiro Abe and Eiji Tanaka : Apoptosis inducer TRAIL stimulates osteoclast differentiation and survival via TAK1 activation., The 4th ASEAN plus Tokushima Joint International Conference, Bali, Indonesia, Dec. 2017.
22.	Itsuro Endo, Dong Bingzi, Ohnishi Yukiyo, Kondo Takeshi, Masahiro Hiasa, Jumpei Teramachi, Toshio Matsumoto, Masahiro Abe, Seiji Fukumoto and Tatsuji Haneji : Decreased bone strength induced by persistent activation of calcium-sensing receptor, American Society for Bone and Mineral Research (ASBMR) 2017 Annual Meeting, Denver, Sep. 2017.
23.	Jumpei Teramachi, Masahiro Hiasa, Oda Asuka, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : TAK1 inhibition impairs myeloma cell-bone marrow interaction to reduce myeloma tumor growth and bone destruction, American Society for Bone and Mineral Research (ASBMR) 2017 Annual Meeting, Denver, Sep. 2017.
24.	Jumpei Teramachi, Masahiro Hiasa, Oda Asuka, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Therapeutic impact of TAK1 inhibition on myeloma tumor progression and bone destruction, International Society for Experimental Hematology 46th Annual Scientific Meeting, Frankfurt, Aug. 2017.
25.	Hirofumi Tenshin, Jumpei Teramachi, A Oda, Ryota Amachi, Masahiro Hiasa, A Baterdene, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Osteoclasts utilize TRAIL for their NF-B activation, but TAK1 inhibition resumes TRAIL-induced apoptosis in osteoclasts., Australian and New Zealand Bone and Mineral Society 2017, Brisbane, Australia., Jun. 2017.
26.	Jumpei Teramachi, Masahiro Hiasa, Oda Asuka, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Akihito Yamamoto, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Therapeutic impact of TAK1 inhibition on myeloma tumor progression and bone destruction, Cancer and Bone Society Conference 2017, Indianapolis, May 2017.
27.	Masahiro Hiasa, T Okui, J Delgado-Calle, T Bellido, GD Roodman, L Plotkin, FA White and T Yoneda : Bone pain-modifying actions of osteocytes via Connexin43-mediated communications with sensory nerves., 44th European Calcified Tissue Society Congress, May 2017.
28.	Ryota Amachi, Masahiro Hiasa, Oda Asuka, Bat-Erdene Ariunzaya, Jumpei Teramachi, Hirofumi Tenshin, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Shiroh Fujii, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : Osteoblast Creates a Non-permissive Niche for Myeloma Cells, 95th General Session & Exhibition of the IADR program book, San Francisco, Mar. 2017.
29.	Hirofumi Tenshin, Jumpei Teramachi, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Toshio Matsumoto, Masahiro Abe and Eiji Tanaka : TRAIL Stimulates Osteoclast Differentiation and Survival via TAK1 Activation., 95th General Session & Exhibition of the IADR program book, San Francisco, Mar. 2017.
30.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Kiyoe Kurahashi, Takeshi Kondo, Hirokazu Miki, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : TAK-1 inhibition disrupts Pim-2-associated and Pim-2-independent key signaling pathways to effectively suppress tumor growth and restore bone formation in myeloma, American Society for Bone and Mineral Research 2016 Annual Meeting, Atlanta, Sep. 2016.
31.	Masahiro Hiasa, T Okui, J Delgado-Calle, T Bellido, GD Roodman, L Plotkin, FA White and T Yoneda : Osteocytes Mediate Bone Pain Through Cell-Cell Communication with Sensory Neurons via Connexin 43, ASBMR 2016 Annual Meeting, Atlanta, Sep. 2016.
32.	Hirofumi Tenshin, Jumpei Teramachi, A Oda, Ryota Amachi, Bingzi Dong, Masahiro Hiasa, Keiichiro Watanabe, Ryota Amachi, S Nakamura, H Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Osteoclasts utilize an apoptosis-inducer TRAIL as a stimulator for osteoclastogenesis Critical roles of the TAK-1-Pim-2 signaling induced by RANK ligand and TRAIL., ANZBMS 2016 Annual Meeting, Gold Coast, Aug. 2016.
33.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Therapeutic impact of TAK-1 inhibition on tumor growth and bone destruction in myeloma, 21st Congress European Hematology Association, Copenhagen, Jun. 2016.
34.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Derek Hanson, Keiichiro Watanabe, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Pim inhibition suppresses osteoclastogenesis and tumor growth in myeloma, 57th ASH Annual Meeting and Exposition, Orlando, Dec. 2015.
35.	Masahiro Hiasa, Okui Tatsuo, Allette M Yohance, Ripsch S Matthew, Bellido Teresita, Roodman David G, Plotkin Lilian, White Fletcher and Yoneda Toshiyuki : Osteocytes are an Important Mediator of Bone Pain in Myeloma, ASBMR 2015 Annual Meeting, Seattle, Oct. 2015.
36.	Okui Tatsuo, Masahiro Hiasa, Nagata Yuki, White Fletcher, Roodman David G and Yoneda Toshiyuki : Reciprocal Interactions between Sensory Neurons and Tumor Cells Promote Breast Cancer Progression in Bone, Secondary Visceral Metastasis and Bone Pain, ASBMR 2015 Annual Meeting, Seattle, Oct. 2015.
37.	Hirofumi Tenshin, Jumpei Teramachi, A Oda, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, S Nakamura, H Miki, I Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TRAIL is not a proapoptotic but rather anti-apoptotic mediator for osteoclasts to stimulate their differentiation and survival, ASBMR 2015 Annual Meeting, Seattle, Oct. 2015.
38.	Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, Asuka Oda, Hirofumi Tenshin, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Shiroh Fujii, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Up-regulation of the pH sensor TRPV1 in myeloma cells and their adaption to an acidic microenvironment, ASBMR 2015 Annual Meeting, Seattle, Oct. 2015.
39.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Keiichiro Watanabe, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Pivotal role of TAK-1 in tumor growth and bone destruction in myeloma: Therapeutic impact of TAK-1 inhibition, American Society for Bone and Mineral Research 2015 Annual Meeting, Oct. 2015.
40.	Takeshi Kondo, Itsuro Endo, Ken-ichi Aihara, nishi Oh Yukiyo, Bingzi Dong, Kiyoe Kurahashi, Sumiko Yoshida, Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, Masahiro Abe, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Serum carboxy-terminal telopeptide of type I collagen, as a marker for systemic atherosclerosis, ANZBMS 2015 Annual Meeting, Hobart, Sep. 2015.
41.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Kumiko Kagawa, Hirokazu Miki, Shiroh Fujii, Keiichiro Watanabe, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Critical role of Pim-2 in NF-B-mediated suppression of osteoblastogenesis and stimulation of osteoclastogenesis: Therapeutic impact of Pim inhibition on myeloma bone disease., 2014 ASBMR Annual Meeting, Houston, Sep. 2014.
42.	Masahiro Hiasa, Nagata Yuki, Delgado-Calle Jesus, Allette M Yohance, Ripsch S Matthew, Bellido Teresita, Roodman David G., White A Fletcher and Yoneda Toshiyuki : Osteocytes directly communicate with sensory neuronal cells via cell-cell networks that are modulated under an acidic microenvironment, ASBMR 2014 Anuual Meeting, Houston, Sep. 2014.
43.	Ryota Amachi, Masahiro Abe, Masahiro Hiasa, Keiichiro Watanabe, S Fujii, T Harada, H Miki, S Nakamura, I Endo, Eiji Tanaka and Toshio Matsumoto : Acidic conditions epigenetically repress the TRAIL receptor DR4 in myeloma cells to confer their resistance to TRAIL, ASBMR 2013 Annual Meeting,, Baltimore, Oct. 2013.
44.	Keiichiro Watanabe, Masahiro Abe, H Mori, Ryota Amachi, Masahiro Hiasa, T Harada, S Fujii, S Nakamura, H Miki, K Kagawa, I Endo, Eiji Tanaka and Toshio Matsumoto : Potent induction of bone formation in myeloma bone lesions by the cathepsin K inhibitor KK1-300-01 in combination with the proteasome inhibitor bortezomib, ASBMR 2013 Annual Meeting,, Baltimore, Oct. 2013.
45.	Keiichiro Watanabe, Masahiro Abe, Ryota Amachi, Masahiro Hiasa, T Harada, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, H Mori, Itsuro Endo, Eiji Tanaka and Toshio Matsumoto : Induction of bone formation in myeloma osteolytic lesions by cathepsinK inhibition, Kyoto, Apr. 2013.
46.	Ryota Amachi, Keiichiro Watanabe, Shiroh Fujii, T Harada, Hirokazu Miki, Shingen Nakamura, A Oda, Masahiro Hiasa, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : An acidic milieu suppersses histone acetylation in myeloma cells to down-regulate the TRAIL receptor DR4 expression., Kyoto, Apr. 2013.
47.	Ryota Amachi, Masahiro Abe, Ryota Amachi, Keiichiro Watanabe, S Fujii, T Harada, H Miki, S Nakamura, A Oda, Masahiro Hiasa, Eiji Tanaka and Toshio Matsumoto : An acidic milieu suppresses DR4 editing to cause myeloma resistance to TRAIL, ASEAN plus and Tokushima Joint International Conference, Yogjakarta, Indonesia, Dec. 2012.
48.	Masahiro Abe, Masahiro Hiasa, Watanabe ken-ichiro, Nakamura Shingen, Harada Takeshi, Itsuro Endo and Toshio Matsumoto : Prevention of tumor growth and bone destruction in myeloma by Pim kinase inhibition, 12th CIBD International Meeting on Cancer Induced Bone Disease (CIBD) Lyon, Nov. 2012, Nov. 2012.
49.	Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Harada Takeshi, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Prevention of tumor growth and bone destruction in myeloma by Pim kinase inhibition, 12th Int'l Meeting on Cancer Induced Bone Disease, Lyon, Nov. 2012.
50.	Masahiro Hiasa, Ryota Amachi, Keiichiro Watanabe, Harada Takeshi, Fujii Shirou, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Pim-2 suppresses BMP-2 signaling as a common inhibitory mediator of osteoblastogenesis in myeloma, ASBMR 2012 Anuual Meeting, Minneapolis, Oct. 2012.
51.	Keiichiro Watanabe, Masahiro Abe, Ryota Amachi, Masahiro Hiasa, T Harada, S Fujii, S Nakamura, H Miki, K Kagawa, H Mori, I Endo, Eiji Tanaka and Toshio Matsumoto : Restoration of bone formation in myeloma osteolytic lesions by the cathepsin K inhibitor KK1-300-01, 34th ASBMR meeting, Minneapolis, MN, USA., Oct. 2012.
52.	Masahiro Hiasa, Masahiro Abe and Toshio Matsumoto : RelB attenuates the activation of the classical NF-kB pathway to facilitate osteoblastogenesis, Sep. 2012.
53.	Masahiro Hiasa, Masahiro Abe, Rieko Arakaki, Akiko Yamada, Kenzo Asaoka, Toshio Matsumoto, Yoshio Hayashi and Naozumi Ishimaru : RelB attenuates the activation of the classical NF-κB pathway to facilitate osteoblastogenesis, ANZBMS Annual Scientific Meeting, Perth, Sep. 2012.
54.	Keiichiro Watanabe, Masahiro Abe, Hiroyo Mori, Ryota Amachi, Masahiro Hiasa, T Harada, S Fujii, S Nakamura, H Miki, K Kagawa, I Endo, Eiji Tanaka and Toshio Matsumoto : The cathepsin K inhibitor KK1-300-01 prevents bone destruction and resumes bone formation in myeloma osteolytic lesions, Australian & New Zealand Bone & Mineral Society 22th Annual Scientific Meeting with 1st Asia-Pacific Bone and Mineral Research meeting, Perth, Australia., Sep. 2012.
55.	Kazuma Matsumoto, Naozumi Ishimaru, Takashi Izawa, Masahiro Hiasa, Yoshio Hayashi and Eiji Tanaka : Hyperfunctions of osteoclasts in a rheumatoid arthritis model, ASBMR 2011 Annual Meeting, San Diego, Sep. 2011.
56.	Keiichiro Watanabe, Masahiro Abe, M Kawatani, Masahiro Hiasa, A Kawano, T Jinno, T Harada, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki, Eiji Tanaka, H Osada and Toshio Matsumoto : Aggravation of myeloma growth and drug resistance by an acidic created in myeloma-osteoclast interaction., ASBMR 2011 Annual Meeting, San Diego, Sep. 2011.
57.	Masahiro Hiasa, nakano ayako, Keiichiro Watanabe, C Qu, T Harada, Shiroh Fujii, Hirokazu Miki, Shingen Nakamura, Kumiko Kagawa, Kyoko Takeuchi, Eiji Tanaka, Kenzo Asaoka, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Prevention of tumor growth and bone destruction in myeloma by Pim kinase inhibition., ASBMR 2011 Annual Meeting, San Diego, Sep. 2011.
58.	Masahiro Hiasa, nakano ayako, Keiichiro Watanabe, C Qu, T Harada, Shiroh Fujii, Hirokazu Miki, Shingen Nakamura, Kumiko Kagawa, Kyoko Takeuchi, Eiji Tanaka, Kenzo Asaoka, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Dual effects of Pim inhibition on myeloma: induction of bone formation and tumor suppression., IOF-ANZBMS 2011 Annual Meeting, Gold Coast, Sep. 2011.
59.	Keiichiro Watanabe, Masahiro Abe, Cui Qu, Kawatani Makoto, Masahiro Hiasa, Nakano Ayako, Jinno Tadashi, Harada Takeshi, Shiroh Fujii, Shingen Nakamura, Miki Hirokazu, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki, Eiji Tanaka, Osada Hiroyuki and Toshio Matsumoto : An Acidic Mileu Created In Myeloma-Osteoclast Interaction Enhances Tumor Growth, but Triggers Anti-Myeloma Activity of Reveromycin A, a Novel Anti-Resorptive Agent, 52th American Society of Hematology, Orlando, Dec. 2010.
60.	Cui Qu, Masahiro Abe, Miki Hirokazu, Shingen Nakamura, Keiichiro Watanabe, Akishige Ikegame, Masahiro Hiasa, Nakano Ayako, Harada Takeshi, Shiroh Fujii, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki and Toshio Matsumoto : Lenalidomide In Combination with Zoledronic Acid Restores the Activation and Anti-Myeloma Effects of γδT Cells Attenuated by the Bone Marrow Microenvironment, 52th American Society of Hematology, Orlando, Dec. 2010.
61.	Keiichiro Watanabe, Masahiro Abe, Cui Qu, Kawatani Makoto, Masahiro Hiasa, Nakano Ayako, Jinno Tadashi, Harada Takeshi, Shiroh Fujii, Shingen Nakamura, Miki Hirokazu, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki, Eiji Tanaka, Osada Hiroyuki and Toshio Matsumoto : A Novel Anti-resorptive Agent, Reveromycin A, Ameliorates Bone Destruction and Tumor Growth in Myeloma, ASBMR 2010 Annual Meeting, Toronto, Oct. 2010.
62.	Masahiro Hiasa, Masahiro Abe, nakano ayako, oda aska, amo hiroe, Keiichiro Watanabe, Shingen Nakamura, miki hirokazu, Kyoko Takeuchi, Kumiko Kagawa, Shuji Ozaki, Eiji Tanaka, Kenzo Asaoka and Toshio Matsumoto : Bone Marrow Stromal Cells Suppress TACE-mediated M-CSFR and RANK Shedding to Facilitate Osteoclastogenesis and Suppress DC Differentiation from Monocytes., ASBMR 2010 Annual Meeting, Toronto, Oct. 2010.
63.	Masahiro Abe, Masahiro Hiasa, Nakano A, Shingen Nakamura, Miki H, Qu C, Keiichiro Watanabe, Harada T, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki and Toshio Matsumoto : TIMP-3 up-regulation facilitates osteoclastogenesis and suppresses DC differentiation from monocytes in the bone marrow microenvironment in myeloma, 10th International Conference Cancer-induced Bone Disease, Sep. 2010. (Keyword) Sheffield (United Kingdom)
64.	Keiichiro Watanabe, Masahiro Abe, Cui Qu, Kawatani Makoto, Masahiro Hiasa, Nakano Ayako, Jinno Tadashi, Harada Takeshi, Shiroh Fujii, Shingen Nakamura, Miki Hirokazu, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki, Eiji Tanaka, Osada Hiroyuki and Toshio Matsumoto : The novel anti-resorptive agent reveromycin A ameliorates bone destruction and tumor growth in myeloma, 10th International Conference Cancer-induced Bone Disease, Sheffield (United Kingdom), Sep. 2010.
65.	Masahiro Hiasa, Masahiro Abe, Eiji Tanaka, Kenzo Asaoka and Toshio Matsumoto : Stroma inhibit DC differentiation through the suppression of M-CSFR shedding, 88th IADR, Barcelona, Jul. 2010.
66.	Masahiro Hiasa, Masahiro Abe, I Endo, A Nakano, Shuji Ozaki, Eiji Tanaka, Kenzo Asaoka and Toshio Matsumoto : Myeloma-bone marrow stromal cell interaction enhances osteoclastogenesis and suppresses dendritic cell differentiation from monocytes, 14th International Congress of Endocrinology, Kyoto, Mar. 2010.
67.	Masahiro Hiasa, Masahiro Abe, A Nakano, Kyoko Takeuchi, K Watanabe, Kumiko Kagawa, Ken-ichiro Yata, Kenzo Asaoka, Eiji Tanaka and Toshio Matsumoto : Bone marrow stromal cells inhibit dendritic cell differentiation and facilitate osteoclastogenesis in myeloma through the suppression of M-CSF receptor shedding in monocytes, 第26回内藤コンファレンス, Nov. 2009.
68.	S Nakamura, Masahiro Abe, Cui Qui, A Nakano, Oda A., Amou H., Ikegame A., Harada T., Masahiro Hiasa, H Miki, Kumiko Kagawa, Kyoko Takeuchi, Ken-ichiro Yata, Shuji Ozaki and Toshio Matsumoto : Facilitation of Osteoblast Differentiation by ATF-4 Accumulation through Proteasome Inhibition., ASH Annual Meeting, Nov. 2009.
69.	A Nakano, Asano J., Masahiro Abe, Masahiro Hiasa, S Nakamura, H Miki, Kumiko Kagawa, Kyoko Takeuchi, Ken-ichiro Yata, Itsuro Endo, Shuji Ozaki and Toshio Matsumoto : Up-regulation of Pim-2 in myeloma cells by an interaction with bone marrow microenvironment enhances myeloma cell survival via stimulating Bad phosphorylation, ASBMR Annual Meeting, Denver, Sep. 2009.
70.	Masahiro Abe, A Oda, Shinsuke Kido, A Nakano, Masahiro Hiasa, H Amou, S Nakamura, Kyoko Takeuchi, H Miki, Kumiko Kagawa, Ken-ichiro Yata, Shuji Ozaki, Itsuro Endo and Toshio Matsumoto : Bortezomib, a proteasome inhibitor with anti-myeloma activity, stimulates osteoblast differentiation by enhancing ATF4 accumulation in osteoblastic cells., ASBMR Annual Meeting, Denver, Sep. 2009.
71.	Ken-ichiro Yata, Masahiro Abe, Oda A., Amou H., takeuchi K., Masahiro Hiasa, Nakano A., Miki H., Nakamura S., Tanaka O., Kumiko Kagawa, Shuji Ozaki and Toshio Matsumoto : Anti-myeloma effects of γδ T cells are hampered by bone marrow stromal cells but resumed by stromal cell-derived osteoblasts, Annual Meeting of the American Society of Hematology, San Francisco, Dec. 2008.
72.	Masahiro Abe, Masahiro Hiasa, Oda A., Amou H., takeuchi K., Tanaka O., Nakamura S., Miki H., Kumiko Kagawa, Ken-ichiro Yata, Shuji Ozaki, Kido S. and Toshio Matsumoto : Bone marrow stromal cells up-regulate M-CSF receptor in monocytes to disrupt dendritic cell differentiation while facilitating osteoclastogenesis in myeloma, ASBMR, Montreal, Sep. 2008.
73.	Takeuchi K., Masahiro Abe, Oda A., Amou H., Masahiro Hiasa, Tanaka O., Nakamura S., Miki H., Kumiko Kagawa, Ken-ichiro Yata, Hashimoto T., Shuji Ozaki, Kido S. and Toshio Matsumoto : TGF-β Suppresses Adipocytic Differentiation and Enhances Accumulation of Stromal Cells in Myeloma Bone Lesions, ASBMR, Montreal, Sep. 2008.
74.	Masahiro Abe, Masahiro Hiasa, Kido S., Oda A., Amou H., takeuchi K., Ken-ichiro Yata, Shuji Ozaki and Toshio Matsumoto : TACE up-regulation in monocytes by GM-CSF and IL-4 disrupts myeloma cell-induced osteoclastogenesis while inducing dendritic cell differentiation, International Meeting on Cancer Induced Bone Disease, Scotland, Jun. 2008.

Proceeding of Domestic Conference:

1.	Masahiro Hiasa, Shinya Horiuchi, Keiichiro Watanabe and Eiji Tanaka : 歯科矯正用アンカースクリューの初期安定性に対する皮質骨厚の影響, 第3回歯科矯正用アンカースクリュー研究会学術大会, Nov. 2023.
2.	Emiko Nakaue, Jumpei Teramachi, Masahiro Hiasa, Sou Shimizu, Yoshiki Higa, TANAKA Mariko, KIMU Suha, NAKAGAWA Motosumi, Eiji Tanaka and Masahiro Abe : プロテアソーム阻害薬による骨髄腫骨病変部における骨形成のメカニズム, 第82回日本矯正歯科学会学術大会抄録集, 192, Nov. 2023.
3.	Yoshiki Higa, Masahiro Hiasa, NAKAGAWA Motosumi, KIMU Suha, TANAKA Mariko, Emiko Nakaue, Sou Shimizu, Hirofumi Tenshin, Eiji Tanaka and Masahiro Abe : KEAP1-NRF2軸を介した脂肪細胞分化と骨芽細胞分化の制御機構, 第82回日本矯正歯科学会学術大会抄録集, 194, Nov. 2023.
4.	Shinya Horiuchi, Emiko Nakaue, Keiichiro Watanabe, Masahiro Hiasa and Eiji Tanaka : 顎間関係を判断するAIにおける判定根拠に関する検討, 第82回日本矯正歯科学会学術大会抄録集, 208, Nov. 2023.
5.	KINJO Soichiro, 塩屋園玲子, Kaoru Yoshinaga, Emiko Nakaue, Keiichiro Watanabe, Masahiro Hiasa and Eiji Tanaka : 上顎骨前方部延長術を行った口唇口蓋裂患者2症例の術後評価, The Journal of Chu-Shikoku Orthodontic Society, Vol.35, No.1, 114-115, Aug. 2023. (Keyword) 顎の奇形(外科的療法) / 歯科矯正治療 / statistics / 病院歯科診療部門 / 顎矯正手術 / ヒト; 男; 女; 歯学
6.	花輪茂己, Masahiro Hiasa, Akihiko Iwasa, Keiichiro Watanabe, Hirofumi Tenshin, Nao Kinouchi, Shinya Horiuchi and Eiji Tanaka : 上顎左側第二小臼歯先天性欠如を伴う片側性唇顎口蓋裂患者に対して下顎左側第二小臼歯を移植した一症例, The Journal of Chu-Shikoku Orthodontic Society, Vol.35, No.1, 67-75, Aug. 2023. (Summary) 口唇裂・口蓋裂患者では永久歯が先天性欠如する割合が高く,とくに複数歯が先天性欠如する症例の場合,マルチブラケット装置を用いた治療の際に咬合の確立に苦慮することは少なくない.今回,上顎左側側切歯および第二小臼歯の先天性欠如を伴う左側唇顎口蓋裂患者に対して,便宜抜去した下顎左側第二小臼歯を上顎左側第二小臼歯欠如部に移植し全顎的な矯正治療を行うことで良好な治療結果が得られたので報告する.初診時年齢0歳20日の女児で,左側唇顎口蓋裂を主訴に当院形成外科から紹介され来院した.12歳時,下顎歯列におけるarch length discrepancyの改善のために抜去した下顎左側第二小臼歯を上顎左側第二小臼歯欠如部へ移植した.12歳10ヵ月時,移植歯の歯根形成と根尖孔閉鎖が認められ,顎骨の成長がほぼ終了したため,二期治療としてマルチブラケット装置を用いて咬合の確立を図った.動的治療期間は5年0ヵ月で,1歯対2歯の緊密な咬合関係が獲得された.現在,保定後2年3ヵ月経過して安定した咬合を維持している.本症例では,便宜抜去した歯を移植することで,補綴処置を回避し,天然歯による緊密な咬合を獲得することができた.移植後2年経過した時点で歯根吸収は認めず,安定した経過をたどっている.しかしながら今後も長期的な観察が必要と考えられる.口唇裂・口蓋裂患者の歯の先天性欠如部位に対する治療法の一つとして歯の移植が有用であることが示唆された.(著者抄録) (Keyword) パノラマX線撮影法 X線診断自家移植下顎骨歯根吸収(合併症,X線診断,外科的療法) 上顎疾患(合併症,外科的療法,診断) 小臼歯(移植) 頭部計測法歯(移植) 無歯症(合併症,外科的療法,診断) 歯科矯正維持装置歯科矯正用ブラケット *唇顎口蓋裂(合併症,外科的療法,診断) ヒト新生児女歯学
7.	田中茉里子, Shinya Horiuchi, Masahiro Hiasa, Keiichiro Watanabe, Akihiko Iwasa and Eiji Tanaka : 術後に顎関節に疼痛を訴えた下顎骨左方偏位を伴う骨格性上顎前突症例, The Journal of Chu-Shikoku Orthodontic Society, Vol.35, No.1, 77-86, Aug. 2023. (Summary) 顎偏位を伴う骨格性上顎前突患者に対し,咬合平面の傾斜と下顎骨左方偏位および後退の改善を目的として上下顎同時移動術を施行し,術後に顎関節の変調をきたした症例を経験したので報告する.初診時25歳9ヵ月の女性で,顔面の非対称と上顎前突を主訴に来院した.顔面正中に対して上顎歯列正中は一致し,下顎歯列正中は6.0mm左方に偏位していた.咬合平面は2.0°左上がりに傾斜し,左側下顎枝は右側に比べ短かった.Overjetは8.5mm,overbiteは2.5mmであった.咬合平面の傾斜,下顎の左方偏位と後退を改善するため,上顎Le Fort I型骨切り術および下顎枝矢状骨切り術を施行した.顎骨の移動量については上顎右側臼歯部で5.5mmの圧下および左側臼歯部で1.5mmの圧下を計画した.下顎は右側臼歯部で4.0mmの後方移動および左側臼歯部で5.0mmの前方移動を計画した.術後,左側顎関節の疼痛を訴えたため,II級ゴムと上下顎同時移動術に用いたセカンドスプリントから移行した下顎前方整位型スプリントを使用したところ,関節部の疼痛は軽減した.段階的にII級ゴムとスプリントの装着時間を短くした結果,下顎の後退が観察され,overjetが増加傾向を示したため,歯科矯正用アンカースクリューを固定源として使用した上顎歯列の遠心移動を行った.術後2年8ヵ月経過時に,良好な咬合が獲得され下顎位も安定したため保定へと移行した.現在保定後5年4ヵ月経過して,緊密な咬合状態が保たれている.下顎の前方移動を伴う外科的矯正治療は,顎関節に不調をきたすことも多く,術後長期にわたる経過観察と,治療変化に対応し得る余地を残した治療計画を勘案する必要性が示唆された.(著者抄録) (Keyword) パノラマX線撮影法 X線診断下顎骨顎関節疾患(病因,診断,治療) 顎の奇形(合併症,外科的療法,診断) 顎前突症(合併症,外科的療法,診断) 歯科矯正ワイヤー MRI 術後痛(診断,治療) 頭部計測法 *関節痛(病因,診断,治療) オクルーザルスプリント LeFort骨切り術歯科矯正用ブラケット下顎枝矢状分割術歯科矯正用固定源埋込みエッジワイズ法矯正的遠心移動ヘッドギアヒト成人(19∼44) 女歯学
8.	NAKAGAWA Motosumi, Masahiro Hiasa, HANAWA Shigeki, KIMU Suha, Yoshiki Higa, Yuta Matsuki, Shinya Horiuchi and Eiji Tanaka : 上顎骨前方部延長術を行った口唇口蓋裂患者2症例の術後評価, The Journal of Chu-Shikoku Orthodontic Society, Vol.35, No.1, 112-113, Aug. 2023. (Keyword) 口蓋裂(外科的療法,診断) 口唇裂(外科的療法,診断) 骨延長法上顎骨治療成績ヒト歯学
9.	Kim SooHa, Jumpei Teramachi, Masahiro Hiasa, Hirofumi Tenshin, Emiko Nakaue, TANAKA Mariko, NAKAGAWA Motosumi, Itsuro Endo, Takeshi Harada, Eiji Tanaka and Masahiro Abe : Molecular mechanisms for generation of non-permissive niche for myeloma cells by activated osteoblasts., The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 173, Jul. 2023.
10.	WADA Ryohei, Keiichiro Watanabe, Kaoru Yoshinaga, KIMU Suha, HANAWA Shigeki, TANAKA Mariko, Yuki Sakamoto, Aki Shimada, Eiji Kondou, Takamasa Kitamura, Hiroyuki Yamasaki, Kazuhide Mineda, Masahiro Hiasa, Shinya Horiuchi, Tomonori Iwasaki, Ichiro Hashimoto and Eiji Tanaka : 徳島大学病院における過去10年間の口唇裂・口蓋裂患者に関する臨床統計調査, Journal fo Japanese Cleft Palate Association, Vol.48, No.2, 200, May 2023. (Keyword) 口蓋裂 / statistics / 大学病院 / ヒト; 男; 女; 歯学
11.	Eiji Kondou, Yuki Sakamoto, Aki Shimada, Kaoru Yoshinaga, Takamasa Kitamura, 山崎裕行, Kazuhide Mineda, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi, Tomonori Iwasaki, Ichiro Hashimoto and Eiji Tanaka : 徳島大学病院における口蓋裂児の滲出性中耳炎と鼓膜チューブ留置術の検討, 第47回日本口蓋裂学会, May 2023.
12.	坂本幸, Eiji Kondou, Aki Shimada, Kaoru Yoshinaga, Takamasa Kitamura, 山崎裕行, Kazuhide Mineda, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi, Tomonori Iwasaki, Ichiro Hashimoto and Eiji Tanaka : 徳島大学病院における口蓋裂児の新生児聴覚スクリーニング結果と滲出性中耳炎罹患率, Journal fo Japanese Cleft Palate Association, Vol.48, No.2, 153, Apr. 2023. (Keyword) 口蓋裂(合併症) 新生児スクリーニング中耳炎-滲出性(診断,合併症) 発生率大学病院聴覚検査ヒト乳児(1∼23ヶ月) 幼児(2∼5) 男女歯学
13.	Eiji Kondou, 坂本幸, Aki Shimada, Kaoru Yoshinaga, Takamasa Kitamura, 山崎裕行, Kazuhide Mineda, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi, Tomonori Iwasaki, Ichiro Hashimoto and Eiji Tanaka : 徳島大学病院における口蓋裂児の滲出性中耳炎と鼓膜チューブ留置術の検討, Journal fo Japanese Cleft Palate Association, Vol.48, No.2, 154, Apr. 2023. (Keyword) 口蓋裂(合併症) 中耳炎-滲出性(外科的療法,合併症) *中耳換気大学病院結果再現性ヒト乳児(1∼23ヶ月) 幼児(2∼5) 小児(6∼12) 青年期(13∼18) 男女歯学
14.	Takeshi Harada, Ryohei Sumitani, Asuka Oda, Yusuke Inoue, Masahiro Oura, Kimiko Sogabe, Tomoko Maruhashi, Mamiko Takahashi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Shuji Ozaki, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : The therapeutic potential targeting ADAR1-dsRNA metabolism in myeloma cells with 1q amplification, The 84th Annual Meeting of the Japanese Society of Hematology, Oct. 2022.
15.	Yoshiki Higa, Masahiro Hiasa, KIMU Suha, TANAKA Mariko, Emiko Nakaue, Sou Shimizu, Kotaro Tanimoto, Hirofumi Tenshin, Eiji Tanaka and Masahiro Abe : キサンチンオキシダーゼ阻害薬febuxostatはKEAP1-NRF2軸を介し脂肪細胞分化と骨芽細胞分化を制御する, 第81回日本矯正歯科学会学術大会, Oct. 2022.
16.	Sou Shimizu, Jumpei Teramachi, Masahiro Hiasa, Hirofumi Tenshin, Yoshiki Higa, Emiko Nakaue, Masahiro Abe and Eiji Tanaka : 骨髄腫細胞の生存・増殖におけるTAK1-CIP2A経路の重要な役割, 第81回日本矯正歯科学会学術大会, Oct. 2022.
17.	Akihiko Iwasa, Yoshiki Higa, Emiko Nakaue, Kaoru Yoshinaga, Sou Shimizu, Yuta Matsuki, Kotaro Tanimoto, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : 特発性下顎頭吸収を呈する矯正患者の下顎頭の形態学的特徴, 第81回日本矯正歯科学会学術大会, Oct. 2022.
18.	Emiko Nakaue, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi, Takeshi Harada, Yusuke Inoue, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : プロテアソーム阻害薬による骨髄腫骨病変部選択的骨形成誘導活性の検討, 第40回日本骨代謝学会学術集会, 141, Jul. 2022.
19.	Yoshiki Higa, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Takeshi Harada, 小田明日香, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : キサンチンオキシダーゼ(XO)阻害薬febuxostatによる脂肪細胞分化と骨芽細胞分化の制御機構, 第40回日本骨代謝学会学術集会, Jul. 2022.
20.	TANAKA Mariko, Masahiro Hiasa, Kotaro Tanimoto, Hirofumi Tenshin, Sou Shimizu, Yoshiki Higa, Emiko Nakaue, KIMU Suha, Jumpei Teramachi, Takeshi Harada, Shingen Nakamura, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 不動は骨髄腫骨病変部DPP-4発現増加と骨髄腫の腫瘍進展・髄外播種を加速させる, 第40回日本骨代謝学会学術集会, Jul. 2022.
21.	Takeshi Harada, Hirofumi Tenshin, Yusuke Inoue, Ryohei Sumitani, Emiko Nakaue, Jumpei Teramachi, Masahiro Hiasa, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Production of SLAMF7 by osteoclasts and development of novel treatment targeting SLAMF7 against myeloma bone disease, 第40回日本骨代謝学会学術集会, Jul. 2022.
22.	Emiko Nakaue, Keiichiro Watanabe, Hirofumi Tenshin, Kaoru Yoshinaga, Yuta Matsuki, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : Identification of key determinant for predicting feasible mandibular molars distalization, The Journal of Chu-Shikoku Orthodontic Society, Jul. 2022.
23.	TANAKA Mariko, Shinya Horiuchi, Masahiro Hiasa, Keiichiro Watanabe, Akihiko Iwasa, Natsumi Takamaru, Hirokazu Nagai, Youji Miyamoto and Eiji Tanaka : 術後に顎関節に変調をきたした顎偏位を伴う骨格性上顎前突症例, 第32回日本顎変形症学会総会・学術大会, Vol.32, No.2, 171, Jun. 2022.
24.	HANAWA Shigeki, Masahiro Hiasa, Akihiko Iwasa, Keiichiro Watanabe, Hirofumi Tenshin, Nao Kinouchi, Shinya Horiuchi and Eiji Tanaka : 上顎左側第二小臼歯先天欠損を伴う片側性唇顎口蓋裂患者に対して下顎左側第二小臼歯を移植した一症例, Journal fo Japanese Cleft Palate Association, Vol.47, No.2, 146, May 2022.
25.	KIMU Suha, Keiichiro Watanabe, Kaoru Yoshinaga, Hirofumi Tenshin, Emiko Nakaue, Yoshiki Higa, 坂本幸, 近藤英司, Aki Shimada, Kazuhide Mineda, Soushi Ishida, Aya Miyazaki, Takamasa Kitamura, Masahiro Hiasa, Shinya Horiuchi, Tomonori Iwasaki, Ichiro Hashimoto and Eiji Tanaka : 徳島大学病院における口唇口蓋裂センター設立前後での患者動向の変化金秀河(徳島大学大学院口腔科学教育部口腔顎顔面矯正学分野), 渡邉佳一郎, 吉永薫, 天眞寛文, 中上絵美子, 比嘉佳基, 坂本幸, 近藤英司, 島田亜紀, 峯田一秀, 石田創士, 宮嵜彩, 北村尚正, 日浅雅博, 堀内信也, 岩崎智憲, 橋本一郎, 田中栄二日本口蓋裂学会雑誌(0386-5185)47巻2号 Page135(2022.04), Journal fo Japanese Cleft Palate Association, Vol.47, No.2, 135, May 2022.
26.	Hirofumi Tenshin, Takeshi Harada, 井上雄介, 菊池次郎, 小田明日香, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, 丸橋朋子, 高橋真美子, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Masahiro Hiasa, Jumpei Teramachi, 鈴木敦, 角川学士, 峯畑健一, 古川雄祐 and Masahiro Abe : Osteoclasts robustly express SLAMF7 and secrete soluble SLAMF7, The 47th Annual Meeting of the Japanese Society of Myeloma, May 2022.
27.	井上雄介, Takeshi Harada, Hirofumi Tenshin, 小田明日香, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, 丸橋朋子, 高橋真美子, Shiroh Fujii, Hirokazu Miki, Shingen Nakamura, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Leverage of Th1-like γδT cells into antibody-mediated immunotherapy against myeloma, The 47th Annual Meeting of the Japanese Society of Myeloma, May 2022.
28.	Takeshi Harada, Ryohei Sumitani, Asuka Oda, Inoue Yusuke, Masahiro Oura, Kimiko Sogabe, Tomoko Maruhashi, Takahashi Mamiko, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Therapeutic impact of targeting RNA editing enzyme ADAR1 on myeloma cells with 1q amplification, 第47回日本骨髄腫学会学術集会, May 2022.
29.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, 小田明日香, Sou Shimizu, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, 丸橋朋子, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Takeshi Harada and Masahiro Abe : TAK1 阻害は骨髄腫の細胞間相互作用による骨破壊と薬剤耐性を改善する, 第47回日本骨髄腫学会学術集会, May 2022.
30.	Yoshiki Higa, Masahiro Hiasa, Hirofumi Tenshin, Kotaro Tanimoto, Sou Shimizu, Jumpei Teramachi, Takeshi Harada, 小田明日香, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : Critical role of the xanthine oxidase-ROS axis in perturbation of bone marrow milieu in myeloma, International Journal of Myeloma, Vol.12, No.3, 149, May 2022.
31.	Emiko Nakaue, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Takeshi Harada, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Ryohei Sumitani, 丸橋朋子, Masahiro Oura, Kimiko Sogabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka and Masahiro Abe : The impact of pulsatile proteasome inhibitor on bone metabolism, International Journal of Myeloma, Vol.12, No.3, 152, May 2022. (Keyword) 骨髄腫-多発性(薬物療法,病理学) / 骨組織リモデリング / パルス療法(薬物療法) / Proteasome Inhibitors(治療的利用,薬理学) / Homo sapiens
32.	Hirofumi Tenshin, Takeshi Harada, 井上雄介, 菊池次郎, 小田明日香, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, 丸橋朋子, 高橋真美子, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Masahiro Hiasa, Jumpei Teramachi, 鈴木敦, 角川学士, 峯畑健一, 古川雄祐 and Masahiro Abe : 破骨細胞はSLAMF7を強発現し可溶性SLAMF7を産生する(Osteoclasts robustly express SLAMF7 and secrete soluble SLAMF7), International Journal of Myeloma, Vol.12, No.3, 150, May 2022. (Keyword) 骨髄腫-多発性(遺伝学,病理学) 破骨細胞 Signaling Lymphocytic Activation Molecule Family(血液) SLAMF7 Protein(血液) ヒト
33.	Keiichiro Watanabe, Hirofumi Tenshin, Kaoru Yoshinaga, Emiko Nakaue, 坂本幸, Eiji Kondou, Aki Shimada, Kazuhide Mineda, Soushi Ishida, Masahiro Hiasa, Shinya Horiuchi, Tomonori Iwasaki, Ichiro Hashimoto and Eiji Tanaka : Pre-epiglottic baton plateによる保存的治療で重度気道閉塞の改善がみられたPierre Robin Sequenceの1例, Journal fo Japanese Cleft Palate Association, Vol.47, No.2, 116, Apr. 2022. (Keyword) Pierre Robin症候群(合併症) 気道閉塞(合併症,診断,予後) 呼吸障害(病因,予後) *保存的療法哺乳障害(病因,予後) ヒト新生児男歯学
34.	Sou Shimizu, Jumpei Teramachi, Takeshi Harada, 小田明日香, Hirofumi Tenshin, Masahiro Hiasa, Kotaro Tanimoto, Yoshiki Higa, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : The critical roles of the TAK1-CIP2A axis in MM cell growth and survival and osteoclastogensis, 第83回日本血液学会学術集会, BPA-3-3, Sep. 2021.
35.	Kimiko Sogabe, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, 小田明日香, 井上雄介, Ryohei Sumitani, 丸橋朋子, Masahiro Oura, Shiroh Fujii, Kumiko Kagawa, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Resumption of myeloma cell sensitivity to proteasome inhibitors by PIM and Akt inhibition, The 83rd Annual Meeting of the Japanese Society of Hematology, Sep. 2021.
36.	Yoshiki Higa, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Takeshi Harada, 小田明日香, 大浦雅弘, Kimiko Sogabe, Itsuro Endo, Toshio Matsumoto, Masahiro Abe and Eiji Tanaka : Critical roles of the XO-ROS axis in the pathology of bone loss in myeloma, 第83回日本血液学会学術集会, BPA-3-4, Sep. 2021.
37.	Hirofumi Tenshin, 寺町順平日浅雅博小田明日香原田武志, Masahiro Hiasa, 小田明日香, Takeshi Harada, Masahiro Oura, Kimiko Sogabe, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Eiji Tanaka, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : NLRP3 inflammasome aggravates osteoclastic bone destruction in myeloma, 日本血液学会学術集会83回 Page 83回 Page OS2-4B-4(2021.09), Sep. 2021.
38.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Takeshi Harada, 小田明日香, Masahiro Oura, Kimiko Sogabe, Itsuro Endo, Toshio Matsumoto, Eiji Tanaka and Masahiro Abe : Extraosseous dissemination of myeloma by mechanical unloading, 日本血液学会学術集会83回 Page 83回 Page OS2-11C-3(2021.09), Sep. 2021.
39.	Takeshi Harada, Yusuke Inoue, Hirofumi Tenshin, Asuka Oda, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Expansion of γδT cells by CELMoDs and enhancement of their anti-myeloma effects by elotuzumab, The 83rd Annual Meeting of Japanese Society of Hematology, Sep. 2021.
40.	Kimiko Sogabe, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, 小田明日香, 井上雄介, Ryohei Sumitani, 丸橋朋子, Masahiro Oura, Shiroh Fujii, Kumiko Kagawa, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : PIMとAkt阻害による骨髄腫細胞のプロテアソーム阻害薬感受性の増強(Sensitization of myeloma cells to proteasome inhibitors by PIM and Akt inhibition), 日本血液学会学術集会, OS2-11D-3, Sep. 2021.
41.	Yuzo Hirai, Keiichiro Watanabe, Emiko Nakaue, Muneyuki Yoshimura, Hirofumi Tenshin, Masahiro Hiasa and Eiji Tanaka : 歯科矯正用アンカースクリューおよび周囲骨の応力分布に及ぼす植立深さの影響:有限要素法による解析, The Journal of Chu-Shikoku Orthodontic Society, Vol.33, No.1, 80, Jul. 2021.
42.	Takeshi Harada, Yusuke Inoue, Hirofumi Tenshin, Asuka Oda, Ryohei Sumitani, Masahiro Oura, Kimiko Sogabe, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Development of combinatory treatment of Th1-like γδT cells with elotuzumab against osteoclasts as well as myeloma cells, 第46回日本骨髄腫学会学術集会, May 2021.
43.	Kimiko Sogabe, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, 小田明日香, 井上雄介, Ryohei Sumitani, Masahiro Oura, Shiroh Fujii, Kumiko Kagawa, Hirofumi Tenshin, Masahiro Hiasa, Jumpei Teramachi, 李政樹, 飯田真介 and Masahiro Abe : 骨髄腫細胞のプロテアソーム阻害薬の耐性機序におけるPIM2とAkt活性およびNRF2蓄積の役割(Mechanisms for the resistance to proteasome inhibitors in myeloma cells: the role of PIM2 and Akt kinase activation and NRF2 accumulation), International Journal of Myeloma, Vol.11, No.2, 85, May 2021. (Keyword) 癌原遺伝子タンパク質骨髄腫-多発性(遺伝学,実験的) Protein-Serine-Threonine Kinases 抗腫瘍剤耐性 c-akt癌原遺伝子タンパク質 NF-E2-Related Factor 2 Proteasome Inhibitors(薬理学) *PIM2 Protein
44.	Keiichiro Watanabe, Hirofumi Tenshin, Kazuhide Mineda, Soushi Ishida, Kaoru Yoshinaga, Emiko Nakaue, Yoshiki Higa, Aya Miyazaki, Takamasa Kitamura, 坂本幸, Eiji Kondou, Aki Shimada, Masahiro Hiasa, Shinya Horiuchi, Ichiro Hashimoto and Eiji Tanaka : 当院における口腔内スキャナーを活用した哺乳床早期装着のための取り組み, Journal fo Japanese Cleft Palate Association, Vol.46, No.2, 123, Apr. 2021. (Keyword) 口蓋裂口唇裂歯科用機器母乳栄養ヒト乳児(1∼23ヶ月) 歯学
45.	Sou Shimizu, Jumpei Teramachi, Takeshi Harada, 小田明日香, Hirofumi Tenshin, Masahiro Hiasa, Kotaro Tanimoto, Yoshiki Higa, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 骨髄腫細胞のPP2A阻害因子CIP2A発現誘導を介するTAK1活性化増強機構, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 149, Oct. 2020.
46.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Mohannad Ashtar, Sou Shimizu, Yoshiki Higa, Jumpei Teramachi, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 不動は骨吸収と骨髄腫進展を促進させる, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 149, Oct. 2020.
47.	Hirofumi Tenshin, Mohannad Ashtar, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Sou Shimizu, Yoshiki Higa, Takeshi Harada, Masahiro Oura, Kimiko Sogabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 抗腫瘍薬が誘導するROSは破骨細胞分化を促進する:Xanthine oxidase阻害剤febuxostatの治療効果．, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 148, Oct. 2020.
48.	Takeshi Harada, Yusuke Inoue, Hirofumi Tenshin, Asuka Oda, Masahiro Oura, Kimiko Sogabe, Ryohei Sumitani, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Masahiro Hiasa, Jumpei Teramachi and Masahiro Abe : Versatile anti-myeloma effects by elotuzumab: impact on γδT cells and osteoclasts, The 82nd Annual Meeting of Japanese Soceity of Hematology, Oct. 2020.
49.	Hirofumi Tenshin, アシテルモハナッド, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Sou Shimizu, 比嘉佳基, Takeshi Harada, Masahiro Oura, Kimiko Sogabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 抗腫瘍薬が誘導するROSは破骨細胞分化を促進する Xanthine oxidase阻害剤febuxostatの治療効果, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 148, Oct. 2020. (Keyword) Xanthine Oxidase(拮抗物質・阻害物質) / reactive oxygen species / 抗腫瘍剤(毒性・副作用) / 骨吸収(化学的誘発,薬物療法,実験的) / cell differentiation / osteoclast / 破骨細胞分化因子 / Febuxostat(治療的利用) / RAW264.7細胞 / マウス / animal
50.	Hiroki Mori, Tsutomu Iwamoto, Saki Saitoh, Kimiko Ueda Yamaguchi, Kazumi Takaishi, Yoshiko Yamamura, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : 本院における口唇口蓋裂児への治療の取り組み, 徳島県歯科医学大会, 28, Feb. 2020.
51.	Fumiko Takahashi, Masahiro Hiasa, Shinya Horiuchi, Eiichi Honda and Eiji Tanaka : 歯科矯正学的に骨性癒着歯と診断された歯の歯科用CBCT画像を用いた鑑別診断, 第78回日本矯正歯科学会学術大会: 日本矯正歯科学会大会プログラム・抄録集 78回 Page207.(2019), 207, Nov. 2019.
52.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Mohannad Ashtar, Bat-Erdene Ariunzaya, Masami Iwasa, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1阻害は関節リウマチにおけるNLRP3インフラマソーム誘導性の炎症および骨破壊を抑制する, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 190, Oct. 2019.
53.	Kotaro Tanimoto, Masahiro Hiasa, Akihiko Iwasa, Hirofumi Tenshin, Jumpei Teramachi, Mohannad Ashtar, Masami Iwasa, 小田明日香, 曾我部公子, Masahiro Oura, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 不動性骨吸収の亢進は骨髄内の骨髄腫進展を促進させる．, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Oct. 2019.
54.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Mohannad Ashtar, Ariunzaya Bat-Erdene, Masami Iwasa, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1阻害は関節リウマチにおけるNLRP3インフラマソーム誘導性の炎症および骨破壊を抑制する．, 第37回日本骨代謝学会学術集会, Oct. 2019.
55.	谷本幸太朗, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Mohannad Ashtar, Masami Iwasa, 小田明日香, Kimiko Sogabe, Masahiro Oura, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 不動性骨吸収の亢進は骨髄内の骨髄腫進展を促進させる, 第37回日本骨代謝学会学術集会, Oct. 2019.
56.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Kotaro Tanimoto, Soh Shimizu, Ashtar Mohannad, Takeshi Harada, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : NLRP3 inflammasome-mediated inflammation and osteoclastic bone resorption in rheumatoid arthritis : the therapeutic roles of TAK1 inhibition, 16th Meeting of Bone Biology Forum, Aug. 2019.
57.	Masaki Sawada, Akihiko Iwasa, Muneyuki Yoshimura, Aki Ichihara, Silvia Naomi Mitsui Akagi, 塩屋園玲子, Masahiro Hiasa, Akihiro Yasue and Eiji Tanaka : シルエットを用いた側貌に対する審美的評価, 第62回中・四国矯正歯科学会大会, Vol.31, No.1, Jul. 2019.
58.	Sou Shimizu, Shinya Horiuchi, Hirofumi Tenshin, Akihiko Iwasa, Keiichiro Watanabe, Masahiro Hiasa, Tsutomu Iwamoto and Eiji Tanaka : 徳島大学病院矯正歯科における口唇裂・口蓋裂患者の合併先天異常に関する実態調査．, Journal fo Japanese Cleft Palate Association, May 2019.
59.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa and Masahiro Abe : TAK1阻害は腫瘍と微小環境との相互作用を遮断し腫瘍進展・骨破壊病変形成を抑制する, 第124回日本解剖学会総会・全国学術集会, Mar. 2019.
60.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Oda Asuka, Bat-Erdene Ariunzaya, Takeshi Harada, Iwasa Masami, Shiroh Fujii, Kimiko Sogabe, Shingen Nakamura, Hirokazu Miki, Masahiro Oura, Kumiko Kagawa, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Mechanisms of TAK1 over-activation in myeloma cells and TAK1-mediated myeloma growth and bone destruction, 第80回日本血液学会学術集会, Oct. 2018.
61.	Ashtar Mohannad, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Oda Asuka, Iwasa Masami, Takeshi Harada, Ariunzaya Erdene Bat, Kimiko Sogabe, Oura Masahiro, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Roles of ROS in induction of bone disease and cancer treatment-induced bone loss in myeloma., The 80th Annual Meeting of the Japanese Society of Hematology, Oct. 2018.
62.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Mohannad Ashtar, Ariunzaya Bat-Erdene, Iwasa Masami, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Kimiko Sogabe, Oura Masahiro, Shiroh Fujii, Kumiko Kagawa, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Inverse regulation of c-FLIP-mediated survival in myeloma cells and osteoclasts by TRAIL., The 80th Annual Meeting of the Japanese Society of Hematology, Oct. 2018.
63.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, Oda Asuka, Mohannad Ashtar, Ariunzaya Bat-Erdene, Iwasa Masami, Kimiko Sogabe, Oura Masahiro, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Impact of denervation-induced paralysis and mechanical unloading on tumor expansion in myeloma., The 80th Annual Meeting of the Japanese Society of Hematology, Oct. 2018.
64.	Masahiro Hiasa, Jumpei Teramachi, Hirofumi Tenshin, Kotaro Tanimoto, Ariunzaya Bat-Erdene, Mohannad Ashtar, Masami Iwasa, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Kimiko Sogabe, Oura Masahiro, Shiroh Fujii, Kumiko Kagawa, Oda Asuka, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : The effects of cathepsin K inhibition on osteocytes: its role in bone restoration in MM bone disease., The 80th Annual Meeting of the Japanese Society of Hematology, Oct. 2018.
65.	Itsuro Endo, 大西幸代, Kiyoe Kurahashi, Jumpei Teramachi, Masahiro Hiasa, Hirofumi Tenshin, Seiji Fukumoto, Masahiro Abe and Toshio Matsumoto : カルシウム感知受容体活性型変異マウスにおける骨強度の低下, 第36回日本骨粗鬆症学会各術集会, Jul. 2018.
66.	Jumpei Teramachi, Hirofumi Tenshin, Masahiro Hiasa, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : TAK1 inhibition impairs myeloma cell-bone marrow interaction to reduce myeloma growth and bone destruction, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Jul. 2018.
67.	Masahiro Hiasa, Jumpei Teramachi, Hirofumi Tenshin, Kotaro Tanimoto, Mohannad Ashtar, Ariunzaya Bat-Erdene, Masami Iwasa, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : カテプシンK阻害による多発性骨髄腫骨病変部の骨量回復プロセスにおける骨細胞の役割．, 第36回日本骨代謝学会学術集会, Jul. 2018.
68.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, Kotaro Tanimoto, Mohannad Ashtar, Ariunzaya Bat-Erdene, Masami Iwasa, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1阻害はTRAILによる破骨細胞活性化作用を遮断させると同時にTRAILの抗骨髄腫作用を増強する, 第36回日本骨代謝学会学術集会, Jul. 2018.
69.	Fumiko Takahashi, Masahiro Hiasa, Shinya Horiuchi, Eiichi Honda and Eiji Tanaka : パノラマX線画像による外科的亜脱臼後予後良好な骨性癒着大臼歯の鑑別診断, 第61回中・四国矯正歯科学会大会, Vol.30, No.1, Jul. 2018.
70.	Hirofumi Tenshin, Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Kotaro Tanimoto, Mohannad Ashtar, Ariunzaya Bat-Erdene, Masami Iwasa, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1による破骨細胞に対するTRAILの生存・細胞死シグナル制御機構．, 第4回日本骨免疫学会, Jun. 2018.
71.	Kotaro Tanimoto, Masahiro Hiasa, Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Mohannad Ashtar, Ariunzaya Bat-Erdene, Masami Iwasa, Kimiko Sogabe, 大浦雅弘, Takeshi Harada, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 神経切断による麻痺と免荷の骨髄腫の進展への影響．, 第4回日本骨免疫学会, Jun. 2018.
72.	Jumpei Teramachi, Masahiro Hiasa, Oda Asuka, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Masami Iwasa, Masahiro Oura, Yusaku Maeda, Shiroh Fujii, Kumiko Kagawa, Hirokazu Miki, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Disruption of myeloma cell-bone marrow interaction by TAK-1 inhibition, 第80回日本血液学会学術集会, Oct. 2017.
73.	Akihiko Iwasa, Haruna Konishi, Kana Fujimoto, Naoko Ogasawara, Keiichiro Watanabe, Masahiro Hiasa, Shinya Horiuchi and Eiji Tanaka : 徳島大学病院矯正歯科患者における永久歯埋伏に関する臨床統計学的調査, 第76回日本矯正歯科学会学術大会, Oct. 2017.
74.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Ariunzaya Baterdene, Masami Iwasa, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TRAILは破骨細胞を活性化させるが，TAK1阻害により骨髄腫細胞とともに破骨細胞にもTRAILのアポトーシス誘導活性が惹起できる, The 35th Annual Meeting of the Japanese Society for Bone and Mineral Research (oral talk), Jul. 2017.
75.	Kana Fujimoto, Haruna Konishi, Akihiko Iwasa, Aki Ichihara, Manami Shirai, Keiichiro Watanabe, Masahiro Hiasa, Hiroyo Mori, Shinya Horiuchi and Eiji Tanaka : 歯科矯正患者における埋伏永久歯に関する実態調査, 第60回中・四国矯正歯科学会大会, Jul. 2017.
76.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Baterdene Ariunzaya, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1阻害はTRAILの抗骨髄腫作用を増強するともに骨吸収促進活性を抑制活性に変換する．, 第42回日本骨髄腫学会, May 2017.
77.	天知良太, Shingen Nakamura, Masahiro Hiasa, 小田明日香, バットエルデネアリウンザヤ, Jumpei Teramachi, Hirofumi Tenshin, Keiichiro Watanabe, Hirokazu Miki, Kumiko Kagawa, Shiroh Fujii, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 骨形成誘導による骨髄腫細胞のエネルギー代謝の抑制, 第42回日本骨髄腫学会学術集会, May 2017.
78.	Jumpei Teramachi, Masahiro Hiasa, Hirofumi Tenshin, Hirohiko Okamura, Masahiro Abe and Tatsuji Haneji : 骨髄腫腫瘍進展と骨破壊病変形成におけるTAK-1の枢軸的役割, 第122回日本解剖学会総会・全国学術集会, Mar. 2017.
79.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 30. 天真寛文, 寺町順平, 小田明日香, 天知良太, , ,破骨細胞系細胞はアポトーシス誘引因子TRAILを生存促進・破骨細胞形成誘導因子として利用する:TAK1-Pim-2経路の役割, 第19回日本癌と骨病変研究会, Nov. 2016.
80.	Masahiro Hiasa, Ryota Amachi, Hirofumi Tenshin, Shinya Horiuchi, Masahiro Abe, Naozumi Ishimaru and Eiji Tanaka : RelBは古典的NF-κB経路の活性化を阻害し骨癒合不全と偽関節形成を予防する, 日本矯正歯科学会大会プログラム・抄録集., 192., Nov. 2016.
81.	Jumpei Teramachi, Masahiro Hiasa, Hirohiko Okamura, Masahiro Abe and Tatsuji Haneji : 骨髄腫の腫瘍進展と骨破壊病変形成におけるTAK1の枢軸的な役割, 日本解剖学会第71回中国・四国支部学術集会, Oct. 2016.
82.	Jumpei Teramachi, Hiroshi Mori, Yasuo Ochi, Ryota Amachi, Asuka Oda, Masahiro Hiasa, Takeshi Harada, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Potent induction of bone formation by anti-resorptive cathepsin K inhibitor in myeloma., The 77th Annual Meeting of the Japanese Society of Hematology, Oct. 2016.
83.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TAK1 inhibition subverts TRAIL-mediated osteoclastogenesis., 第77回日本血液学会学術集会,, Oct. 2016.
84.	Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, 小田明日香, Hirofumi Tenshin, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Shiroh Fujii, 遠藤逸郎, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Mechanism of the TRPV1 up-regulatation in myeloma cells and adaptation to an acidic microenvironment., 第77回日本血液学会学術集会,, Oct. 2016.
85.	Keiichiro Watanabe, Jumpei Teramachi, Ryota Amachi, 小田明日香, Hirofumi Tenshin, 岩浅正美, Masahiro Hiasa, Shingen Nakamura, 遠藤逸郎, 川谷誠, 長田裕之, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Amelotin gene expression is temporarily being upregulated at the initiation of apoptosis induced by TGFb1 in mouse gingival epithelial cells, 第77回日本血液学会学術集会,, Oct. 2016.
86.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Shingen Nakamura, Kiyoe Kurahashi, Takeshi Kondo, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : TAK-1 inhibition disrupts Pim-2-associated and Pim-2-independent key signaling pathways to effectively suppress tumor growth and restore bone formation in myeloma, 第78回日本血液学会学術集会, Oct. 2016.
87.	Hiroko Sato, Noboru Kajimoto, Masahiro Hiasa, Shinya Horiuchi, Kenichi Hamada and Eiji Tanaka : イオン液体を混和したレジンセメントの特性-矯正用レジンセメントにおける検討-, 日本歯科理工学会近畿中四国地方会夏期セミナー, Aug. 2016.
88.	Keiichiro Watanabe, Jumpei Teramachi, Ryota Amachi, 小田明日香, Hirofumi Tenshin, Masahiro Hiasa, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, 川谷誠, 長田裕之, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : リベロマイシンAによる酸性環境での骨髄腫細胞の治療抵抗性の克服, 日本骨代謝学会学術集会プログラム抄録集 (1349-0761)34回 Page183(2016.07), 183, Jul. 2016.
89.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 破骨細胞はTAK1の発現誘導を介しアポトーシスを抑制しTRAILにより成熟活性化される, 日本骨代謝学会学術集会プログラム抄録集 (1349-0761)34回 Page183(2016.07), 183, Jul. 2016.
90.	Masahiro Hiasa, T Okui and T Yoneda : 骨細胞はコネキシン43を介して痛覚神経を興奮させ骨痛を増悪す, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Jul. 2016.
91.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Hirofumi Tenshin, Ryota Amachi, 原田武志, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : 骨髄腫腫瘍進展と骨破壊病変形成におけるTAK1-Pim-2経路の役割, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Jul. 2016.
92.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, 原田武志, Hirofumi Tenshin, Shingen Nakamura, Ryota Amachi, Shiroh Fujii, Keiichiro Watanabe, Kumiko Kagawa, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Pim-2は骨髄腫における破骨細胞形成促進の必須媒介因子である, 第41回日本骨髄腫学会学術集会, May 2016.
93.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TRAILは破骨細胞に細胞死を誘導せず，破骨細胞分化・生存を促進する., 第41回日本骨髄腫学会, May 2016.
94.	Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, A Oda, Hirofumi Tenshin, Keiichiro Watanabe, Shingen Nakamura, H Miki, Kumiko Kagawa, Shiroh Fujii, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Mechanism of the TRPV1 up-regulatation in myeloma cells and adaptation to an acidic microenvironment, 第77回日本血液学会学術集会, Oct. 2015.
95.	Keiichiro Watanabe, Jumpei Teramachi, H Mori, Y Ochi, Ryota Amachi, A Oda, Masahiro Hiasa, T Harada, Shiroh Fujii, Shingen Nakamura, H Miki, Kumiko Kagawa, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : Potent induction of bone formation by anti-resorptive cathepsin K inhibitor in myeloma, 第77回日本血液学会学術集会, Oct. 2015.
96.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Keiichiro Watanabe, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Potent suppression of osteoclastogenesis in myeloma by Pim inhibition, 第77回日本血液学会学術集会, Oct. 2015.
97.	Jumpei Teramachi, Masahiro Hiasa, Asuka Oda, Hirofumi Tenshin, Ryota Amachi, Takeshi Harada, Keiichiro Watanabe, Shiroh Fujii, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Tumor reduction and bone restoration in myeloma by TAK-1 inhibition, 第77回日本血液学会学術集会, Oct. 2015.
98.	Jumpei Teramachi, Masahiro Hiasa, Hirohiko Okamura, Masahiro Abe and Tatsuji Haneji : Pim-2を標的とした骨髄腫細胞による骨破壊の抑制, 日本解剖学会第70回中国・四国支部学術集会, Oct. 2015.
99.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Hirofumi Tenshin, Ryota Amachi, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : Pim阻害による骨髄種骨病変の治療:破骨細胞形成の抑制, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Jul. 2015.
100.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Hirofumi Tenshin, Ryota Amachi, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Tatsuji Haneji, Toshio Matsumoto and Masahiro Abe : 骨髄腫腫瘍進展と骨破壊病変形成における TAK-1の枢軸的役割, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Jul. 2015.
101.	Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, 小田明日香, Hirofumi Tenshin, Keiichiro Watanabe, Shingen Nakamura, Kumiko Kagawa, Hirokazu Miki, Shiroh Fujii, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 酸環境での骨髄腫細胞のDR4発現抑制:酸によるエピジェネティックな遺伝子発現制御, 第1回日本骨免疫学会, 108, Jul. 2015.
102.	Ryota Amachi, Masahiro Hiasa, Jumpei Teramachi, 小田明日香, Keiichiro Watanabe, Hirofumi Tenshin, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Takeshi Kondo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 酸性環境での骨髄腫細胞のTRPV1の発現亢進と酸環境への適応, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 165, Jul. 2015.
103.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : アポトーシス誘導因子TRAILによる破骨細胞分化・生存の促進, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 164, Jul. 2015.
104.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, 原田武志, Ryota Amachi, Hirofumi Tenshin, Hirokazu Miki, Shingen Nakamura, Shiroh Fujii, Kumiko Kagawa, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Pim阻害による骨髄腫骨吸収亢進の抑制, 第40回日本骨髄腫学会学術集会, May 2015.
105.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, 原田武志, Ryota Amachi, Hirofumi Tenshin, Hirokazu Miki, Shingen Nakamura, Shiroh Fujii, Kumiko Kagawa, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : TAK-1は骨髄腫腫瘍進展と骨破壊病変形成の枢軸的な媒介因子である, 第40回日本骨髄腫学会学術集会, May 2015.
106.	Jumpei Teramachi, Masahiro Hiasa, 原田武志, Ryota Amachi, Kumiko Kagawa, Hirokazu Miki, Shingen Nakamura, Shiroh Fujii, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Therapeutic impact of Pim inhibition on myeloma bone disease: blockade of NF-B-mediated suppression of osteoblastogenesis and stimulation of osteoclastogenesis, 日本血液学会, Oct. 2014.
107.	Ryota Amachi, Masahiro Hiasa, Keiichiro Watanabe, Jumpei Teramachi, 小田明日香, Keiichiro Watanabe, Shingen Nakamura, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : 酸が惹起する骨髄腫細胞の酸感受と生存シグナルの悪循環, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 225, Jul. 2014.
108.	Jumpei Teramachi, Masahiro Hiasa, 小田明日香, Ryota Amachi, Shingen Nakamura, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : Pim-2キナーゼはTNF-αによる骨芽細胞分化抑制および破骨細胞形成促進の必須媒介因子である:Pim阻害薬の骨髄腫骨病変改善効果, 第32回日本骨代謝学会学術集会, Jul. 2014.
109.	Keiichiro Watanabe, Masahiro Abe, H Mori, K Udaka, M Iwasa, D Hanson, Ryota Amachi, Masahiro Hiasa, T Harada, Shiroh Fujii, Shingen Nakamura, H Miki, Kumiko Kagawa, Itsuro Endo, Eiji Tanaka and Toshio Matsumoto : Bone restoration and tumor suppression in myeloma by cathepsin K inhibition with Bortezomib, 第75回日本血液学会学術集会, Oct. 2013.
110.	Ryota Amachi, Keiichiro Watanabe, Masahiro Hiasa, Masahiro Abe, Toshio Matsumoto and Eiji Tanaka : 酸性環境が骨髄腫細胞の破骨細胞活性に及ぼす影響, 第72回日本矯正歯科学会大会プログラム・抄録集, Oct. 2013.
111.	Ryota Amachi, Keiichiro Watanabe, Shiroh Fujii, T Harada, H Miki, S Nakamura, A Oda, Masahiro Hiasa, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : An acdic milieu confers the resistance to TRAIL in myeloma cells through the PI3K-Akt-mediated epigenetic down-regulation of the TRAIL receptor DR4, International Bone and Mineral Society 2013, May 2013.
112.	Keiichiro Watanabe, Masahiro Abe, H Mori, Ryota Amachi, Masahiro Hiasa, T Harada, Shiroh Fujii, S Nakamura, H Miki, K Kagawa, I Endo, Eiji Tanaka and Toshio Matsumoto : Induction of cathepsin K induce bone formation in myeloma osteolytic lesions, International Bone and Mineral Society 2013, May 2013.
113.	Ryota Amachi, Keiichiro Watanabe, Shiroh Fujii, T Harada, H Miki, S Nakamura, A Oda, Masahiro Hiasa, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : An acdic milieu suppresses histone acetylation in myeloma cells to down-regulate the TRAIL receptor DR4 expression, 14th International Myeloma Workshop, Apr. 2013.
114.	Keiichiro Watanabe, Masahiro Abe, Ryota Amachi, Masahiro Hiasa, T Harada, Shiroh Fujii, S Nakamura, H Miki, K Kagawa, I Endo, Eiji Tanaka and Toshio Matsumoto : Induction of bone formation in myeloma osteolytic lesions by cathepsin K inhibition, 14th International Myeloma Workshop, Apr. 2013.
115.	Shiroh Fujii, Masahiro Abe, Ryota Amachi, Keiichiro Watanabe, Masahiro Hiasa, 竹内恭子, 岩佐昌美, 原田武志, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa and Toshio Matsumoto : Pim inhibition preferentially induces anti-myeloma activity in an acidic milien, 第74回日本血液学会学術集会, Oct. 2012.
116.	Masahiro Hiasa, Masahiro Abe, Kumiko Kagawa, Hirokazu Miki, Shingen Nakamura, Harada Takeshi, Fujii Shirou, Keiichiro Watanabe, Ryota Amachi, Kenzo Asaoka and Toshio Matsumoto : Pim-2 acts as a common downstream mediator to suppress bone formation in myeloma., 第74回に本血液学会, Oct. 2012.
117.	Ryota Amachi, Masahiro Abe, Keiichiro Watanabe, Masahiro Hiasa, Eiji Tanaka and Toshio Matsumoto : An acidic milieu suppresses DR4 editing and induces p22 c-FLIP to cause myeloma resistance to TRAIL, 第74回日本血液学会学術集会, Oct. 2012.
118.	Shinya Horiuchi, Ryota Amachi, Namhee Kim, Emi Kawakami, Kazuma Matsumoto, Rie Matsuda, Masahiro Hiasa, Shingo Kuroda and Eiji Tanaka : Preventive effect of orthodontic adhesive with S-PRG filler on enamel demineralization, 第71回日本矯正歯科学会大会プログラム・抄録集, 187, Sep. 2012.
119.	Keiichiro Watanabe, Masahiro Abe, Ryota Amachi, Masahiro Hiasa, Shingen Nakamura, 遠藤逸郎, 森裕史, Eiji Tanaka and Toshio Matsumoto : カテプシンK 阻害剤KK1-300-01 は骨髄腫骨病変部の骨破壊を抑制し骨形成を惹起する, 第30回日本骨代謝学会学術大会, 217, Jul. 2012.
120.	Masahiro Hiasa, Masahiro Abe, Rieko Arakaki, Akiko Yamada, Kenzo Asaoka, Toshio Matsumoto, Yoshio Hayashi and Naozumi Ishimaru : RelB antagonizes the classical NF-κB pathway and its suppression of osteoblastogenesis, 第30回日本骨代謝学会, Jul. 2012.
121.	Ryota Amachi, Masahiro Abe, Keiichiro Watanabe, Shingen Nakamura, Masahiro Hiasa, Eiji Tanaka and Toshio Matsumoto : 酸性環境は骨髄腫細胞にDR4 の発現抑制とcFLIP の活性化を惹起しTRAIL に対する抵抗性を獲得させる, 第30回日本骨代謝学会学術集会, 259, Jul. 2012.
122.	Kazuma Matsumoto, Nobuhiko Kawai, Shinya Horiuchi, Kazuna Takahara, Emi Kawakami, Masahiro Hiasa, Shingo Kuroda and Eiji Tanaka : long-term observation of a patient with achondroplasia who acquired acceptable occlusion by orthodontic treatment, 第55回中・四国矯正歯科学会大会, 29, Jul. 2012.
123.	Kazuma Matsumoto, Rieko Arakaki, Akiko Yamada, Masahiro Hiasa, Ritsuko 徳永律子 Oura, 岩浅亮彦, Eiji Tanaka, Yoshio Hayashi and Naozumi Ishimaru : Hyperfunctions of osteoclasts in pathogenesis of rheumatoid arthritis in MRL/lpr mice., 第40回日本免疫学会学術集会, Nov. 2011.
124.	Masahiro Hiasa, Rieko Arakaki, Akiko Yamada, Ritsuko 徳永律子 Oura, Masahiro Abe, Toshio Matsumoto, Yoshio Hayashi, Naozumi Ishimaru and Kenzo Asaoka : A novel role of NF-B relB in bone remodeling., 第40回日本免疫学会学術集会, Nov. 2011.
125.	Ritsuko 徳永律子 Oura, Rieko Arakaki, Masahiro Hiasa, Akiko Yamada, Eiji Tanaka, Yoshio Hayashi and Naozumi Ishimaru : In vivo T cell apoptosis via interaction with CD11b+ macrophages in Fas-deficient host., Proceedings of the Japanese Society for Immunology, Vol.40, 111, Nov. 2011.
126.	Keiichiro Watanabe, Masahiro Abe, Q Cui, Masahiro Hiasa, M Kawatani, T Harada, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, A Nakano, K Kagawa, K Takeuchi, H Osada, Eiji Tanaka and Toshio Matsumoto : Targeting an acidic microenvironment by reveromycin A to overcome drug resistance to myeloma cells and ameliorate bone disease., 第36回日本骨髄腫研究会総会, Nov. 2011.
127.	Kazuma Matsumoto, Naozumi Ishimaru, Takashi Izawa, Masahiro Hiasa, Ritsuko 徳永律子 Oura, Akihiko Iwasa, Yoshio Hayashi and Eiji Tanaka : 関節リウマチモデルマウスにおける破骨細胞の機能亢進, 日本矯正歯科学会大会プログラム・抄録集, 218, Oct. 2011. (Keyword) 関節リウマチ(実験的); 疾患モデル(動物); 破骨細胞 / マウス; 動物; 歯学
128.	Shinya Horiuchi, Shingo Kuroda, Masahiro Hiasa, Ryota Amachi, Keiichiro Watanabe, Emi Kawakami, Nobuhiko Kawai and Eiji Tanaka : S-PRGフィラー含有矯正歯科用接着剤の歯質脱灰抑制効果に関する検討, 日本矯正歯科学会大会プログラム・抄録集, 312, Oct. 2011. (Keyword) 歯科矯正装置; 歯科矯正治療; 歯牙接着法; 接着剤; フッ素; 歯牙脱灰(予防) / フィラー / ヒト; 歯学
129.	Masahiro Hiasa, Masahiro Abe, 中野綾子, Kyoko Takeuchi, Kumiko Kagawa, Shingen Nakamura, Hirokazu Miki, Eiji Tanaka, Kenzo Asaoka, Ken-ichiro Yata and Toshio Matsumoto : Pimキナーゼ阻害による腫瘍進展と骨破壊の抑制, 第73回日本血液学会, Oct. 2011.
130.	Masahiro Hiasa, A Nakano, Keiichiro Watanabe, C Qu, T Harada, S Fujii, H Miki, S Nakamura, K Kagawa, K Takeuchi, Eiji Tanaka, Kenzo Asaoka, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Prevention of tumor growth and bone destruction in myeloma by Pim kinase inhibition, Bone Biology Forum, 19-21st Aug, 2011, Shizuoka., Aug. 2011.
131.	Masahiro Hiasa, Masahiro Abe, 中野綾子, Keiichiro Watanabe, Shingen Nakamura, Eiji Tanaka, Kenzo Asaoka and Toshio Matsumoto : Pimキナーゼの阻害は骨芽細胞分化を促進し，骨髄腫骨病変の形成と腫瘍進展を抑制する, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 178, Jul. 2011.
132.	Keiichiro Watanabe, Masahiro Abe, 川谷誠, Masahiro Hiasa, Shingen Nakamura, Eiji Tanaka, 長田裕之 and Toshio Matsumoto : リベロマイシンAによる酸性環境がもたらす骨髄腫薬剤耐性の克服と骨病変形成の抑制, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 208, Jul. 2011.
133.	Kazuma Matsumoto, Naozumi Ishimaru, Takashi Izawa, Masahiro Hiasa, Eiji Tanaka and Yoshio Hayashi : 関節リウマチモデルマウスにおける破骨細胞の機能解析, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 256, Jul. 2011.
134.	Masahiro Hiasa, Masahiro Abe, 中野綾子, Keiichiro Watanabe, Shingen Nakamura, Eiji Tanaka, Kenzo Asaoka and Toshio Matsumoto : Pimキナーゼの阻害は骨芽細胞分化を促進し，骨髄腫骨病変の形成と腫瘍進展を抑制する, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 178, 2011. (Keyword) 癌原遺伝子蛋白質(拮抗物質・阻害物質); 骨芽細胞; 骨疾患(病因,実験的); 骨髄腫(合併症,実験的); 細胞分化; Protein-Serine-Threonine Kinases(拮抗物質・阻害物質) / Mouse Pim2 Protein(拮抗物質・阻害物質) / マウス; 動物
135.	Keiichiro Watanabe, Masahiro Abe, 川谷誠, Masahiro Hiasa, Shingen Nakamura, Eiji Tanaka, 長田裕之 and Toshio Matsumoto : リベロマイシンAによる酸性環境がもたらす骨髄腫薬剤耐性の克服と骨病変形成の抑制, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 208, 2011. (Keyword) Pyrans; Spiro Compounds; 骨疾患; 骨髄腫; 抗腫瘍剤耐性 / Reveromycin A
136.	Kazuma Matsumoto, Naozumi Ishimaru, Takashi Izawa, Masahiro Hiasa, Eiji Tanaka and Yoshio Hayashi : 関節リウマチモデルマウスにおける破骨細胞の機能解析, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 256, 2011. (Keyword) 関節リウマチ(実験的); 疾患モデル(動物); 破骨細胞 / マウス; 動物; 歯学
137.	Keiichiro Watanabe, Masahiro Abe, Cui Qu, Kawatani Makoto, Masahiro Hiasa, Nakano Ayako, Jinno Tadashi, Harada Takeshi, Shiroh Fujii, Shingen Nakamura, Miki Hirokazu, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki, Eiji Tanaka, Osada Hiroyuki and Toshio Matsumoto : Reveromycin A prevents bone destruction and suppresses tumor growth in myeloma, 第72回日本血液学会, Dec. 2010.
138.	Ritsuko 徳永律子 Oura, Naozumi Ishimaru, Masahiro Hiasa, Kazuma Matsumoto, Yoshio Hayashi and Eiji Tanaka : Fasを介した末梢T細胞維持機構の破綻による関節リウマチ発症機序の解明, 第69回日本矯正歯科学会, Sep. 2010.
139.	Kumiko Kagawa, Jinno Tasashi, Harada Kakeshi, Cui Qu, Keiichiro Watanabe, Masahiro Hiasa, Oda Asuka, Amo Hiroe, Akishige Ikegame, Miki Hirokazu, Shiroh Fujii, Nakano Ayako, Kyoko Takeuchi, Shuji Ozaki, Masahiro Abe and Toshio Matsumoto : Sensitization of hematopietic malignant cells to TRAIL with bortezomib and a TACE inhibitor, 第72回日本血液学会, Sep. 2010.
140.	Shingen Nakamura, Masahiro Abe, Cui Qu, Keiichiro Watanabe, Akishige Ikegame, Masahiro Hiasa, Miki Hirokazu, Nakano Ayako, Oda Asuka, Amo Hiroe, Jinno Tasashi, Harada Takeshi, Shiroh Fujii, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki and Toshio Matsumoto : Bortezomib-induced osteoblast differentiation is hampered by excessive ER stress, 第72回日本血液学会, Sep. 2010.
141.	Masahiro Hiasa, Masahiro Abe, 中野綾子, 小田明日香, 天羽宏枝, Kyoko Takeuchi, Kumiko Kagawa, Shingen Nakamura, 三木浩和, Ken-ichiro Yata, Keiichiro Watanabe, Shuji Ozaki, Kenzo Asaoka, Eiji Tanaka and Toshio Matsumoto : Bone marrow stromal cells supress TACE activity in monocytes to induce osteoclastogenesis, 第72回日本血液学会, Sep. 2010.
142.	Cui Qu, Masahiro Abe, Miki Hirokazu, Shingen Nakamura, Keiichiro Watanabe, Akishige Ikegame, Masahiro Hiasa, Nakano Ayako, Jinnno Tadashi, Harada Takeshi, Shiroh Fujii, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki and Toshio Matsumoto : Bone marrow stromal cells attenuate gama delta T, 第72回日本血液学会, Sep. 2010.
143.	Masahiro Hiasa, Masahiro Abe, Toshio Matsumoto and Kenzo Asaoka : 骨髄間質細胞は単球のTACE活性を抑制し樹状細胞分化を抑制し破骨細胞分化を誘導する, 第3回ナノ・バイオメディカル学会大会, Sep. 2010.
144.	Shinya Horiuchi, Masahiro Hiasa, Nao Kinouchi, Akihiro Yasue, Kenichi Hamada, Kenzo Asaoka and Eiji Tanaka : リン酸亜鉛カルシウムを添加した亜鉛徐放性アパタイトセメントの開発, 日本矯正歯科学会大会プログラム・抄録集, 208, Sep. 2010.
145.	Masahiro Hiasa, Masahiro Abe, 中野綾子, 小田明日香, 天羽宏枝, Kyoko Takeuchi, Kumiko Kagawa, Shingen Nakamura, 三木浩和, Ken-ichiro Yata, Keiichiro Watanabe, Shuji Ozaki, Kenzo Asaoka, Eiji Tanaka and Toshio Matsumoto : 骨髄間質細胞は，単球のTACE活性を抑制し樹状細胞分化を抑制し破骨細胞文化を誘導する, 第28回日本骨代謝学会, Jul. 2010.
146.	Keiichiro Watanabe, Masahiro Abe, Kawatani Makoto, Masahiro Hiasa, Shingen Nakamura, Eiji Tanaka, 長田裕之 and Toshio Matsumoto : リベロマイシンAは骨髄腫骨破壊病変の形成と腫瘍進展を抑制する, 第28回日本骨代謝学会, Jul. 2010.
147.	Shingen Nakamura, Masahiro Abe, Cui Qu, Keiichiro Watanabe, Akishige Ikegame, Masahiro Hiasa, 三木浩和, 中野綾子, 小田明日香, 天羽宏枝, 神野雅, 原田武志, Shiroh Fujii, Kumiko Kagawa, Kyoko Takeuchi, Shuji Ozaki and Toshio Matsumoto : ボルテゾミブによる骨芽細胞分化の促進は過剰な小胞体ストレスによって抑制される, 第28回日本骨代謝学会, Jul. 2010.
148.	Naoko Yoneda, Masahiro Hiasa, 井上雅秀, 長山智子, 吉田亮彦, 森博世, Shinji Fujihara, Shinya Horiuchi and Eiji Tanaka : Clinico-statistical study of micro-implant anchorage, 第53回中・四国矯正歯科学会学術大会, Jul. 2010.
149.	Masahiro Hiasa : GM-CSFとIL-4は単球のM-CSF受容体の切断を介し破骨細胞分化を抑制し樹状細胞分化を誘導する, 第6回麒麟塾, Jun. 2010.
150.	Masahiro Hiasa : TNF-α converting enzyme (TACE)による破骨細胞・樹状細胞分化の制御, 第8回口腔医科学フロンティア, Mar. 2010.
151.	Masahiro Hiasa and Kenzo Asaoka : ニッケルチタン合金の腐食とその生体為害性, 第2回 Nano Biomedicine, Feb. 2010.
152.	Shinya Horiuchi, Masahiro Hiasa, Hiroko Mori, Kenichi Hamada, Kenzo Asaoka and Eiji Tanaka : ボンディング前処理剤がセルフエッチングプライマーを用いるダイレクトボンディングに与える影響について, 第68回日本矯正歯科学会学術大会, Nov. 2009.
153.	Kazuma Matsumoto, Takashi Izawa, Ritsuko 徳永律子 Oura, Masahiro Hiasa and Eiji Tanaka : Oligodontiaを伴う著しい過蓋咬合に対する包括的治療例, 第52回中・四国矯正歯科学会学術大会, Jul. 2009.
154.	Masahiro Hiasa, Masahiro Abe, 竹内恭子, Ken-ichiro Yata, Kumiko Kagawa, 三木浩和, Shuji Ozaki, Kenzo Asaoka and Toshio Matsumoto : 骨髄間質細胞は単球のM-CSFR発現を増強し単球由来樹状細胞分化を抑制し骨髄腫細胞による破骨細胞分化を促進する, 日本骨代謝学会・学術総会, Oct. 2008.
155.	竹内恭子, Masahiro Abe, Masahiro Hiasa, 田中修, 中村信元, 三木浩和, Kumiko Kagawa, Ken-ichiro Yata, Shuji Ozaki and Toshio Matsumoto : 骨髄腫骨病変部由来TGF-βは，脂肪細胞分化を抑制し骨髄内に間質細胞を誘導する, 日本骨代謝学会・学術総会, Oct. 2008.
156.	竹内恭子, Masahiro Abe, Masahiro Hiasa, 田中修, 中村信元, 三木浩和, Kumiko Kagawa, Ken-ichiro Yata, Shuji Ozaki and Toshio Matsumoto : TGF-βによる間質細胞からの脂肪細胞分化の抑制, 日本血液学会, Oct. 2008.
157.	Ken-ichiro Yata, Masahiro Abe, Masahiro Hiasa, 竹内恭子, 田中修, 中村信元, 三木浩和, Kumiko Kagawa, Shuji Ozaki and Toshio Matsumoto : 骨髄腫細胞と間質細胞の共存は単球M-CSFR発現増強を介し単球分化を破骨細胞側に偏らせる, 日本血液学会, Oct. 2008.
158.	Shinya Horiuchi, Masahiro Hiasa, Emi Kawakami, Shinji Fujihara, Kenzo Asaoka and Eiji Tanaka : Development of a new biomaterial applying the apatite transformed from water setting zinc phosphate cement, 第67回日本矯正歯科学会学術大会, Sep. 2008.
159.	Masahiro Hiasa, Masahiro Abe, Kenzo Asaoka and Toshio Matsumoto : inhibition of osteoclastgenesis by ectodomain shedding of M-CSF receptor, 17, Aug. 2008.
160.	Masahiro Hiasa and Kenzo Asaoka : TI合金の腐食と免疫応答, 歯科チタン学会, Feb. 2008.
161.	Masahiro Hiasa, Masahiro Abe, Toshihiro Hashimoto, Shuji Ozaki, Daisuke Inoue, Shinsuke Kido, Keiji Moriyama and Toshio Matsumoto : GM-CSFとIL-4は単球のM-CSF破骨細胞分化を抑制し樹状細胞分化を誘導する, Journal of Japanese Society of Bone Morphometry, Vol.16, No.3, 66, Dec. 2006. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1573668925326077696 (CiNii: 1573668925326077696)
162.	田中洋一, Masahiro Abe, Masahiro Hiasa, Toshihiro Hashimoto, Shinsuke Kido, Daisuke Inoue, Shuji Ozaki, Keiji Moriyama and Toshio Matsumoto : 骨髄腫細胞，破骨細胞と血管内皮細胞の細胞間相互作用:腫瘍進展，骨破壊と血管新生の促進, 第23回日本骨代謝学会学術集会, Jul. 2005.
163.	Masahiro Hiasa, Yasuo Oba and Keiji Moriyama : 歯周疾患を伴う上顎前突の成人2症例, 第48回中·四国矯正歯科学会大会, Jul. 2005.

Et cetera, Workshop:

1.	Eiji Tanaka and Masahiro Hiasa : 歯科矯正用アンカースクリューを用いた安心安全なMTMの実際と注意点, 香川県保険医協会・歯科セミナー, Oct. 2022.
2.	Jumpei Teramachi, Masahiro Hiasa and Masahiro Abe : Development of novel anti-myeloma agents with potent bone anabolic actions, 14th Bone Biology Forum, Aug. 2017.
3.	Masahiro Hiasa, T Okui, Masahiro Abe and T Yoneda : Targeting the myeloma-induced acidic microenvironment decreases bone pain, 第78回日本血液学会学術集会, Oct. 2016.
4.	Masahiro Hiasa, T Okui and T Yoneda : Vacuolar proton pump on multiple myeloma cells contribute to the induction of bone pain, Bone Biology Forum, Aug. 2016.
5.	Ryota Amachi, Masahiro Abe, Keiichiro Watanabe, Kumiko Kagawa, Shiroh Fujii, 原田武志, Hirokazu Miki, Keiichiro Watanabe, 小野明日香, Masahiro Hiasa, Eiji Tanaka and Toshio Matsumoto : 骨髄腫の酸性環境はTRAIL受容体発現をエピジェネティックに抑制し，TRAIL抵抗性をもたらす, 第20回徳島骨代謝研究会, Nov. 2013.
6.	Keiichiro Watanabe, Ryota Amachi, Masahiro Hiasa, Shingen Nakamura, Itsuro Endo, Hiroshi Mori, Eiji Tanaka and Toshio Matsumoto : The cathepsinK inhibitor ONO-KK1-300-01 (ONO-KK1) prevents bone destruction and restores bone formation in myeloma bone lesions, Bone Seminar, Aug. 2012.
7.	Ryota Amachi, Masahiro Abe, Keiichiro Watanabe, Kumiko Kagawa, 藤井志郎, 原田武志, Hirokazu Miki, Shingen Nakamura, 小田明日香, Masahiro Hiasa, Eiji Tanaka and Toshio Matsumoto : 酸環境は骨髄腫細胞のTRAILに対する抵抗性を増強する, 第3回骨バイオサイエンス研究会, Jul. 2012.
8.	Masahiro Hiasa, Masahiro Abe, 中野綾子, Keiichiro Watanabe, Kyoko Takeuchi, Kumiko Kagawa, Hirokazu Miki, Shingen Nakamura, Shiroh Fujii, 原田武志, Shuji Ozaki, Eiji Tanaka, Kenzo Asaoka and Toshio Matsumoto : Pimキナーゼの阻害による骨髄腫の進展抑制, 癌と骨病変研究会, Nov. 2011.
9.	Keiichiro Watanabe, Masahiro Abe, 崔衢, 川谷誠, Masahiro Hiasa, 長田裕之, Eiji Tanaka and Toshio Matsumoto : A novel anti-resorptive agent, reveromycin A, ameliorates bone destruction and tumor growth in myeloma, 第2回骨バイオサイエンス研究会, Jul. 2011.
10.	Masahiro Hiasa, Masahiro Abe, 中野綾子, 小田明日香, 天羽宏枝, Kyoko Takeuchi, Kumiko Kagawa, Shingen Nakamura, 三木浩和, Ken-ichiro Yata, Keiichiro Watanabe, Shuji Ozaki, Kenzo Asaoka, Eiji Tanaka and Toshio Matsumoto : 骨髄間質細胞は，単球のTACE活性を抑制し樹状細胞分化を抑制し破骨細胞文化を誘導する, 第17回徳島骨代謝研究会, Nov. 2010.
11.	Ken-ichiro Yata, Masahiro Abe, 竹内恭子, Masahiro Hiasa, 中野綾子, 三木浩和, 田中修, 中村信元, Kumiko Kagawa, Shuji Ozaki and Toshio Matsumoto : 骨髄間質細胞はγδT細胞による抗骨髄腫効果を減弱させる, 日本骨髄腫研究会総会, Nov. 2008.
12.	Masahiro Hiasa and Kenzo Asaoka : TI合金の腐食と免疫応答, 平成20年度厚生労働省科学研究費補助金化学物質リスク研究事業「ナノ微粒子の体内動態可視化法の開発」平成20年度第2回班会議, Feb. 2008.

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

骨細胞が関与する骨痛メカニズムの解明 (Project/Area Number: 24K22250 )
骨形成環境による腫瘍排他的ニッチの分子機序の解明：新たながん治療戦略の可能性 (Project/Area Number: 24K02643 )
骨細胞保護によるがんの骨転移新規治療戦略の開発 (Project/Area Number: 23K27791 )
Elucidation of molecular mechanisms of cancer progression by mechanical unloading (Project/Area Number: 19K22719 )
Fabrication of direct bonding material for easily debonding on demand (Project/Area Number: 18K09855 )
Elucidation of the pathogenesis of bone diseases mediated by osteocyte-sensory nerve networks (Project/Area Number: 17H05104 )
骨破壊性悪性腫瘍のもたらす骨髄酸性環境を標的とした骨痛緩和法の開発 (Project/Area Number: 16H07018 )
Exploration for novel fluoride compound inforce the anticariogenisitic effect of glass-ionomer (Project/Area Number: 25463181 )
骨形成誘導と骨破壊性腫瘍の進展抑制を併せ持つ新たな分子標的薬の開発 (Project/Area Number: 25463087 )
Mechanism of bone and cartilage deterioration in rheumatoid arthritis via RANKL/Fas signaling (Project/Area Number: 23659966 )
Development of immunotherapy against the bone destructive tumor (Project/Area Number: 23659946 )
Fabrications of zinc-releasing biocement combining zinc calcium phosphate to calcium phosphate cement (Project/Area Number: 22592287 )
Clarification of the function of TIMP3 in fracture healing and development of new fracture healing drug (Project/Area Number: 21792077 )
Novel therapy to prevent scar formation in wound healing via TGF-β/Smad3 signaling pathway (Project/Area Number: 21592597 )
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Associate Professor : Hiasa, Masahiro

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