Tokushima University / Educator and Researcher Directory --- Teramachi, Jumpei

Field of Study

○	Dentistry
○	Molecular and Cellular Biology, Oral Histology
○	Osteoimmunology

Subject of Study

○	破骨細胞の分化・活性化に関する分子生物学的研究
○
○	癌と骨病変に関する研究

Book / Paper

Book:

1.	Jumpei Teramachi and Masahiro Abe : TAK-1を標的とした骨髄腫骨破壊病変治療薬開発, NIPPONRINSHOSHA Co.,Ltd., Jul. 2016.
2.	Tatsuji Haneji and Jumpei Teramachi : Immunohistohemistry of cultured cells (in Histochemistry and Cytochemistry 2009), Nakanishi Publishing, Kyoto, 2009.

Academic Paper (Judged Full Paper):

1.	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)
2.	Masahiro Oura, Takeshi Harada, Asuka Oda, Jumpei Teramachi, Atsushi Nakayama, Ryohei Sumitani, Yusuke Inoue, Yusaku Maeda, Kimiko Sogabe, Maruhashi Tomoko, Mamiko Takahashi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Shingen Nakamura, Tomoyo Hara, Hiroki Yamagami, Kiyoe Kurahashi, Itsuro Endo, Hiroo Hasegawa, Hiroshi Fujiwara and Masahiro Abe : Therapeutic efficacy of the resorcylic acid lactone LL-Z1640-2 for adult T-cell leukaemia/lymphoma, eJHaem, Vol.4, No.3, 667-678, 2023. (Summary) Adult T-cell leukaemia/lymphoma (ATL) remains incurable. The NF-κB and interferon regulatory factor 4 (IRF4) signalling pathways are among the critical survival pathways for the progression of ATL. TGF-β-activated kinase 1 (TAK1), an IκB kinase-activating kinase, triggers the activation of NF-κB. The resorcylic acid lactone LL-Z1640-2 is a potent irreversible inhibitor of TAK1/extracellular signal-regulated kinase 2 (ERK2). We herein examined the therapeutic efficacy of LL-Z1640-2 against ATL. LL-Z1640-2 effectively suppressed the in vivo growth of ATL cells. It induced in vitro apoptosis and inhibited the nuclear translocation of p65/RelA in ATL cells. The knockdown of strongly induced ATL cell death while downregulating MYC. LL-Z1640-2 as well as the NF-κB inhibitor BAY11-7082 decreased the expression of IRF4 and MYC at the protein and mRNA levels, indicating the suppression of the NF-κB-IRF4-MYC axis. The treatment with LL-Z1640-2 also mitigated the phosphorylation of p38 MAPK along with the expression of CC chemokine receptor 4. Furthermore, the inhibition of STAT3/5 potentiated the cytotoxic activity of LL-Z1640-2 against IL-2-responsive ATL cells in the presence of IL-2. Therefore, LL-Z1640-2 appears to be an effective treatment for ATL. Further studies are needed to develop more potent compounds that retain the active motifs of LL-Z1640-2. (Link to Publication Site) ● Publication site (DOI): 10.1002/jha2.758 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37601887 ● Search Scopus @ Elsevier (PMID): 37601887 ● Search Scopus @ Elsevier (DOI): 10.1002/jha2.758 (DOI: 10.1002/jha2.758, PubMed: 37601887)
3.	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)
4.	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)
5.	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)
6.	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)
7.	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)
8.	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)
9.	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)
10.	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)
11.	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)
12.	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)
13.	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)
14.	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)
15.	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)
16.	Kaya Yoshida, Jumpei Teramachi, Kenta Uchibe, Mika Ikegame, Lihong Qiu, Di Yang and Hirohiko Okamura : Reduction of protein phosphatase 2A Ca promotes in vivo bone formation and adipocyte differentiation., Molecular and Cellular Endocrinology, Vol.470, 251-258, 2018. (Summary) Serine/threonine protein phosphatase 2A (PP2A) regulates diverse physiological processes such as cell cycle, growth, apoptosis, and signal transduction. Previously, we demonstrated that silencing of the α-isoform of PP2A catalytic subunit (PP2A Cα) in osteoblasts accelerated osteoblast differentiation, whereas its overexpression suppressed differentiation. In this study, we examined the role of PP2A Cα in in vivo bone formation by generating transgenic mice (PP2A-Tg), in which the dominant negative form of PP2A Cα was specifically expressed in osteoblasts. PP2A-Tg mice exhibited an increase in body weight, cortical bone mineral density, and cortical bone thickness. Interestingly, they also displayed higher amounts of adipose tissue in the bone marrow of tibiae. The co-culture study showed that PP2A Cα-knockdown osteoblasts stimulated adipocyte differentiation from undifferentiated mesenchymal cells via upregulation of the adipocyte marker genes, such as peroxisome proliferator-activated receptor γ (PPARγ) and CCAAT/enhancer binding protein α (C/EBPα). These results indicated that the reduction of PP2A Cα levels in osteoblasts promoted bone formation in vivo. Additionally, PP2A Cα in osteoblasts was also potentially involved in controlling adipocyte differentiation through a paracrine mechanism. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.mce.2017.11.005 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29128580 ● Summary page in Scopus @ Elsevier: 2-s2.0-85033794901 (DOI: 10.1016/j.mce.2017.11.005, PubMed: 29128580, Elsevier: Scopus)
17.	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)
18.	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)
19.	Hirohiko Okamura, Kaya Yoshida, Hiroyuki Morimoto, Jumpei Teramachi, Kazuhiko Ochiai, Tatsuji Haneji and Akihito Yamamoto : Role of Protein Phosphatase 2A in Osteoblast Differentiation and Function., Journal of Clinical Medicine, Vol.6, No.3, 2017. (Summary) The reversible phosphorylation of proteins plays hugely important roles in a variety of cellular processes, such as differentiation, proliferation, and apoptosis. These processes are strictly controlled by protein kinases (phosphorylation) and phosphatases (de-phosphorylation). Here we provide a brief history of the study of protein phosphorylation, including a summary of different types of protein kinases and phosphatases. One of the most physiologically important serine/threonine phosphatases is PP2A. This review provides a description of the phenotypes of various PP2A transgenic mice and further focuses on the known functions of PP2A in bone formation, including its role in osteoblast differentiation and function. A reduction in PP2A promotes bone formation and osteoblast differentiation through the regulation of bone-related transcription factors such as Osterix. Interestingly, downregulation of PP2A also stimulates adipocyte differentiation from undifferentiated mesenchymal cells under the appropriate adipogenic differentiation conditions. In osteoblasts, PP2A is also involved in the ability to control osteoclastogenesis as well as in the proliferation and metastasis of osteosarcoma cells. Thus, PP2A is considered to be a comprehensive factor in controlling the differentiation and function of cells derived from mesenchymal cells such as osteoblasts and adipocytes. (Keyword) osteoblast / protein dephosphorylation / protein phosphatase (Tokushima University Institutional Repository) ● Metadata: 117742 (Link to Publication Site) ● Publication site (DOI): 10.3390/jcm6030023 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28241467 ● Search Scopus @ Elsevier (PMID): 28241467 ● Search Scopus @ Elsevier (DOI): 10.3390/jcm6030023 (Tokushima University Institutional Repository: 117742, DOI: 10.3390/jcm6030023, PubMed: 28241467)
20.	Nan Ma, Di Yang, Hirohiko Okamura, Jumpei Teramachi, Tomokazu Hasegawa, Lihong Qiu and Tatsuji Haneji : Involvement of interleukin23 induced by Porphyromonas endodontalis lipopolysaccharide in osteoclastogenesis, Molecular Medicine Reports, Vol.15, No.2, 559-566, 2017. (Summary) Periapical lesions are characterized by the destruction of periapical bone, and occur as a result of local inflammatory responses to root canal infection by microorganisms including Porphyromonas endodontalis (P. endodontalis). P. endodontalis and its primary virulence factor, lipopolysaccharide (LPS), are associated with the development of periapical lesions and alveolar bone loss. Interleukin-23 (IL-23) is critical in the initiation and progression of periodontal disease via effects on peripheral bone metabolism. The present study investigated the expression of IL-23 in tissue where a periapical lesion was present, and the effect of P. endodontalis LPS on the expression of IL-23 in periodontal ligament (PDL) cells. Reverse transcription- quantitative polymerase chain reaction and immunohistochemistry revealed increased levels of IL-23 expression in tissue with periapical lesions compared with healthy PDL tissue. Treatment with P. endodontalis LPS increased the expression of IL-23 in the SH-9 human PDL cell line. BAY11-7082, a nuclear factor κB inhibitor, suppressed P. endodontalis LPS-induced IL-23 expression in SH-9 cells. Treatment of RAW264.7 cells with conditioned medium from P. endodontalis LPS-treated SH-9 cells promoted osteoclastogenesis. By contrast, RAW264.7 cells treated with conditioned medium from IL-23-knockdown SH-9 cells underwent reduced levels of osteoclastogenesis. The results of the present study indicated that the expression of IL-23 in PDL cells induced by P. endodontalis LPS treatment may be involved in the progression of periapical lesions via stimulation of the osteoclastogenesis process. (Keyword) Animals / Chromones / Humans / Immunohistochemistry / Interleukin-23 / Lipopolysaccharides / Mice / Morpholines / NF-kappa B / NFATC Transcription Factors / Nitriles / Osteoblasts / Osteogenesis / Periodontitis / Phosphatidylinositol 3-Kinases / Porphyromonas endodontalis / Proto-Oncogene Proteins c-fos / RANK Ligand / RAW 264.7 Cells / RNA Interference / RNA, Small Interfering / Sulfones (Link to Publication Site) ● Publication site (DOI): 10.3892/mmr.2016.6041 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28000855 ● Search Scopus @ Elsevier (PMID): 28000855 ● Search Scopus @ Elsevier (DOI): 10.3892/mmr.2016.6041 (DOI: 10.3892/mmr.2016.6041, PubMed: 28000855)
21.	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)
22.	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)
23.	Takeshi Harada, Hirokazu Miki, Q Cui, A Oda, Ryota Amachi, Jumpei Teramachi, A Bat-Erdene, K Sogabe, M Iwasa, Shiroh Fujii, Shingen Nakamura, Kumiko Kagawa, Sumiko Yoshida, I Endo, Ken-ichi Aihara, Shuji Ozaki, Toshio Matsumoto and Masahiro Abe : Expansion of Th1-like V9V2T cells by new-generation IMiDs, lenalidomide and pomalidomide, in combination with zoledronic acid., Leukemia, Vol.31, No.1, 258-262, 2016. (Link to Publication Site) ● Publication site (DOI): 10.1038/leu.2016.273 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27698446 ● Search Scopus @ Elsevier (PMID): 27698446 ● Search Scopus @ Elsevier (DOI): 10.1038/leu.2016.273 (DOI: 10.1038/leu.2016.273, PubMed: 27698446)
24.	Di Yang, Hirohiko Okamura, Hiroyuki Morimoto, Jumpei Teramachi and Tatsuji Haneji : Protein phosphatase 2A Cα regulates proliferation, migration, and metastasis of osteosarcoma cells., Laboratory Investigation; a Journal of Technical Methods and Pathology, Vol.96, No.10, 1050-1062, 2016. (Summary) Osteosarcoma is the most frequent primary bone tumor. Serine/threonine protein phosphatase 2A (PP2A) participates in regulating many important physiological processes, such as cell cycle, growth, apoptosis, and signal transduction. In this study, we examined the expression and function of PP2A Cα in osteosarcoma cells. PP2A Cα expression was expected to be higher in malignant osteosarcoma tissues. PP2A Cα expression level and PP2A activity was higher in malignant osteosarcoma LM8 cells compared with that in primary osteoblasts and in the osteoblast-like cell line MC3T3-E1. Okadaic acid, an inhibitor of PP2A, reduced cell viability and induced apoptosis in LM8 cells. PP2A Cα-knockdown LM8 cells (shPP2A) exhibited less striking filopodial and lamellipodial structures than that in original LM8 cells. Focal adhesion kinase phosphorylation and NF-κB activity decreased in shPP2A-treated cells. Sensitivity to serum deprivation-induced apoptosis increased in shPP2A-treated cells, accompanied by a lower expression level of anti-apoptotic BCL-2 in these cells. Reduction of PP2A Cα resulted in a decrease in the migration ability of LM8 cells in vitro. Reduction in PP2A Cα levels in vivo suppressed proliferation and metastasis in LM8 cells. PP2A Cα expression was also higher in human osteosarcoma MG63 and SaOS-2 cells than that in primary osteoblasts and MC3T3-E1 cells, and reduction in PP2A Cα levels suppressed the cell proliferation rate and migration ability of MG63 cells. These results indicate that PP2A Cα has a critical role in the proliferation and metastasis of osteosarcoma cells; therefore, its inhibition could potentially suppress the malignancy of osteosarcoma cells. (Keyword) protein dephosphorylation / osteoblast (Link to Publication Site) ● Publication site (DOI): 10.1038/labinvest.2016.82 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27617401 ● Search Scopus @ Elsevier (PMID): 27617401 ● Search Scopus @ Elsevier (DOI): 10.1038/labinvest.2016.82 (DOI: 10.1038/labinvest.2016.82, PubMed: 27617401)
25.	Jumpei Teramachi, Yuki Nagata, Khalid Mohammad, Yuji Inagaki, Yasuhisa Ohata, Theresa Guise, Laëtitia Michou, P Jacques Brown, J Jolene Windle, Noriyoshi Kurihara and David G Roodman : Measles virus nucleocapsid protein increases osteoblast differentiation in Paget's disease., The Journal of Clinical Investigation, Vol.126, No.3, 1012-1022, 2016. (Summary) Paget's disease (PD) is characterized by focal and dramatic bone resorption and formation. Treatments that target osteoclasts (OCLs) block both pagetic bone resorption and formation; therefore, PD offers key insights into mechanisms that couple bone resorption and formation. Here, we evaluated OCLs from 3 patients with PD and determined that measles virus nucleocapsid protein (MVNP) was expressed in 70% of these OCLs. Moreover, transgenic mice with OCL-specific expression of MVNP (MVNP mice) developed PD-like bone lesions that required MVNP-dependent induction of high IL-6 expression levels in OCLs. In contrast, mice harboring a knockin of p62P394L (p62-KI mice), which is the most frequent PD-associated mutation, exhibited increased bone resorption, but not formation. Evaluation of OCLs from MVNP, p62-KI, and WT mice revealed increased IGF1 expression in MVNP-expressing OCLs that resulted from the high IL-6 expression levels in these cells. IL-6, in turn, increased the expression of coupling factors, specifically ephrinB2 on OCLs and EphB4 on osteoblasts (OBs). IGF1 enhanced ephrinB2 expression on OCLs and OB differentiation. Importantly, ephrinB2 and IGF1 levels were increased in MVNP-expressing OCLs from patients with PD and MVNP-transduced human OCLs compared with levels detected in controls. Further, anti-IGF1 or anti-IGF1R blocked Runx2 and osteocalcin upregulation in OBs cocultured with MVNP-expressing OCLs. These results suggest that in PD, MVNP upregulates IL-6 and IGF1 in OCLs to increase ephrinB2-EphB4 coupling and bone formation. (Link to Publication Site) ● Publication site (DOI): 10.1172/JCI82012 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26878170 ● Summary page in Scopus @ Elsevier: 2-s2.0-84959912039 (DOI: 10.1172/JCI82012, PubMed: 26878170, Elsevier: Scopus)
26.	Di Yang, Hirohiko Okamura, Jumpei Teramachi and Tatsuji Haneji : Histone demethylase Jmjd3 regulates osteoblast apoptosis through targeting anti-apoptotic protein Bcl-2 and pro-apoptotic protein Bim., Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1863, No.4, 650-659, 2016. (Summary) Posttranslational modifications including histone methylation regulate gene transcription through directly affecting the structure of chromatin. Trimethylation of histone H3K27 (H3K27me3) contributes to gene silencing and the histone demethylase Jumonji domain-containing 3 (Jmjd3) specifically removes the methylation of H3K27me3, followed by the activation of gene expression. In the present study, we explored the roles of Jmjd3 in regulating osteoblast apoptosis. Knockdown of Jmjd3 promoted osteoblast apoptosis induced by serum deprivation with decreased mitochondrial membrane potential and increased levels of caspase-3 activation, PARP cleavage, and DNA fragmentation. B cell lymphoma-2 (Bcl-2), an anti-apoptotic protein, was down-regulated by knockdown of Jmjd3 through retaining H3K27me3 on its promoter region. Knockdown of Jmjd3 increased the pro-apoptotic activity of Bim through inhibiting ERK-dependent phosphorylation of Bim. Protein kinase D1 (PKD1), which stimulates ERK phosphorylation, decreased in the Jmjd3-knockdown cells and introduction of PKD1 relieved osteoblast apoptosis in the Jmjd3-knockdown cells through increasing ERK-regulated Bim phosphorylation. These results suggest that Jmjd3 regulates osteoblast apoptosis through targeting Bcl-2 expression and Bim phosphorylation. (Keyword) osteoblast (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbamcr.2016.01.006 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26795455 ● Summary page in Scopus @ Elsevier: 2-s2.0-84956688215 (DOI: 10.1016/j.bbamcr.2016.01.006, PubMed: 26795455, Elsevier: Scopus)
27.	Jumpei Teramachi, Yuji Inagaki, Hiroki Shinohara, Hirohiko Okamura, Di Yang, Kazuhiko Ochiai, Ryoko Baba, Hiroyuki Morimoto, Toshihiko Nagata and Tatsuji Haneji : PKR regulates LPS-induced osteoclast formation and bone destruction in vitro and in vivo., Oral Diseases, 2016. (Summary) PKR plays a pivotal role in LPS-induced bone loss in PD, and, thus, has potential as a therapeutic target for PD. This article is protected by copyright. All rights reserved. (Link to Publication Site) ● Publication site (DOI): 10.1111/odi.12592 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27718290 ● Search Scopus @ Elsevier (PMID): 27718290 ● Search Scopus @ Elsevier (DOI): 10.1111/odi.12592 (DOI: 10.1111/odi.12592, PubMed: 27718290)
28.	Di Yang, Hirohiko Okamura, Jumpei Teramachi and Tatsuji Haneji : Histone demethylase Utx regulates differentiation and mineralization in osteoblasts., Journal of Cellular Biochemistry, Vol.116, No.11, 2628-2636, 2015. (Summary) Alteration of methylation status of lysine 27 on histone H3 (H3K27) associates with dramatic changes in gene expression in response to various differentiation signals. Demethylation of H3K27 is controlled by specific histone demethylases including ubiquitously transcribed tetratricopeptide repeat X chromosome (Utx). However, the role of Utx in osteoblast differentiation remains unknown. In this study, we examined whether Utx should be involved in osteoblast differentiation. Expression of Utx increased during osteoblast differentiation in MC3T3-E1 cells and primary osteoblasts. GSK-J1, a potent inhibitor of H3K27 demethylase, increased the levels of trimethylated H3K27 (H3K27me3) and decreased the expressions of Runx2 and Osterix and ALP activity in MC3T3-E1 cells. Stable knockdown of Utx by shRNA attenuated osteoblast differentiation and decreased ALP activity, calcium content, and bone-related gene expressions. Silencing of Utx increased the level of H3K27me3 on the promoter regions of Runx2 and Osterix and decreased the promoter activities of Runx2 and Osterix. Taken together, our present results propose that Utx plays important roles in osteoblast differentiation by controlling the expressions of Runx2 and Osterix. (Keyword) osteoblast (Link to Publication Site) ● Publication site (DOI): 10.1002/jcb.25210 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25920016 ● Summary page in Scopus @ Elsevier: 2-s2.0-84941105888 (DOI: 10.1002/jcb.25210, PubMed: 25920016, Elsevier: Scopus)
29.	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)
30.	Shingen Nakamura, Hirokazu Miki, Asuka Oda, Ryota Amachi, Jumpei Teramachi, Kimiko Sogabe, Hikaru Fujino, Tomoko Maruhashi, Shiroh Fujii, Kumiko Kagawa and Masahiro Abe : Susceptibility to bendamustine considerably varies among myeloma cells, but is enhanced in acidic conditions, International Journal of Myeloma, Vol.6, No.1, 7-11, 2015.
31.	Hiroki Shinohara, Jumpei Teramachi, Hirohiko Okamura, Di Yang, Toshihiko Nagata and Tatsuji Haneji : Double stranded RNA-dependent protein kinase is necessary for TNF--induced osteoclast formation in vitro and in vivo., Journal of Cellular Biochemistry, Vol.116, No.9, 1957-1967, 2015. (Summary) Double-stranded RNA-dependent protein kinase (PKR) is involved in cell cycle progression, cell proliferation, cell differentiation, tumorgenesis, and apoptosis. We previously reported that PKR is required for differentiation and calcification in osteoblasts. TNF- plays a key role in osteoclast differentiation. However, it is unknown about the roles of PKR in the TNF--induced osteoclast differentiation. The expression of PKR in osteoclast precursor RAW264.7 cells increased during TNF--induced osteoclastogenesis. The TNF--induced osteoclast differentiation in bone marrow-derived macrophages and RAW264.7 cells was markedly suppressed by the pre-treatment of PKR inhibitor, 2-aminopurine (2AP), as well as gene silencing of PKR. The expression of gene markers in the differentiated osteoclasts including TRAP, Calcitonin receptor, cathepsin K and ATP6V0d2 was also suppressed by the 2AP treatment. Bone resorption activity of TNF--induced osteoclasts was also supressed by 2AP treatment. Inhibition of PKR supressed the TNF--induced activation of NF-B and MAPK in RAW264.7 cells. 2AP inhibited both the nuclear translocation of NF-B and its transcriptional activity in RAW264.7 cells. 2AP inhibited the TNF--induced expression of NFATc1 and c-fos, master transcription factors in osteoclastogenesis. TNF--induced nuclear translocation of NFATc1 in mature osteoclasts was clearly inhibited by the 2AP treatment. The PKR inhibitor C16 decreased the TNF--induced osteoclast formation and bone resorption in mouse calvaria. The present study indicates that PKR is necessary for the TNF--induced osteoclast differentiation in vitro and in vivo. This article is protected by copyright. All rights reserved. (Tokushima University Institutional Repository) ● Metadata: 109478 (Link to Publication Site) ● Publication site (DOI): 10.1002/jcb.25151 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25739386 ● Search Scopus @ Elsevier (PMID): 25739386 ● Search Scopus @ Elsevier (DOI): 10.1002/jcb.25151 (Tokushima University Institutional Repository: 109478, DOI: 10.1002/jcb.25151, PubMed: 25739386)
32.	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)
33.	Hirohiko Okamura, Di Yang, Kaya Yoshida, Jumpei Teramachi and Tatsuji Haneji : Reduction of PP2A C stimulates adipogenesis by regulating the Wnt/GSK-3/-catenin pathway and PPAR expression, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1843, No.11, 2376-2384, 2014. (Summary) Serine/threonine protein phosphatase 2A (PP2A) regulates several physiological processes such as the cell cycle, cell growth, apoptosis, and signal transduction. In this study, we examined the expression and role of PP2A Cα in adipocyte differentiation. PP2A Cα expression and PP2A activity decreased during adipocyte differentiation in C3H10T1/2 and 3T3-L1 cells and the expression of adipocyte marker genes such as PPARγ and adiponectin increased. To further clarify the role of PP2A Cα in adipocyte differentiation, we constructed PP2A knockdown cells by infecting C3H10T1/2 cells with a lentivirus expressing a shRNA specific for the PP2A Cα (shPP2A cells). Silencing of PP2A Cα in C3H10T1/2 cells dramatically stimulated adipocyte differentiation and lipid accumulation, which were accompanied by expression of adipocyte marker genes. Silencing of PP2A Cα suppressed Wnt10b expression and reduced the levels of the inactivated form of GSK-3β (phospho-GSK-3β), leading to the reduction of β-catenin levels in the nucleus and its transcriptional activity. Treatment with LiCl, a GSK-3β inhibitor, and inhibition of PPARγ expression suppressed the accelerated adipogenesis of shPP2A cells. Our data indicate that PP2A Cα plays an important role in the regulation of adipocyte differentiation by regulating the Wnt/GSK-3β/β-catenin pathway and PPARγ expression. (Keyword) PP2A / protein phosphatase / adipocyte (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbamcr.2014.06.008 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24949891 ● Summary page in Scopus @ Elsevier: 2-s2.0-84905178655 (DOI: 10.1016/j.bbamcr.2014.06.008, PubMed: 24949891, Elsevier: Scopus)
34.	Jumpei Teramachi, Hua Zhou, A Mark Subler, Yukiko Kitagawa, L Deborah Galson, W David Dempster, J Jolene Windle, Noriyoshi Kurihara and David G Roodman : Increased IL-6 expression in osteoclasts is necessary but not sufficient for the development of Paget's disease of bone., Journal of Bone and Mineral Research, Vol.29, No.6, 1456-1465, 2014. (Summary) Measles virus nucleocapsid protein (MVNP) expression in osteoclasts (OCLs) and mutation of the SQSTM1 (p62) gene contribute to the increased OCL activity in Paget's disease (PD). OCLs expressing MVNP display many of the features of PD OCLs. Interleukin-6 (IL-6) production is essential for the pagetic phenotype, because transgenic mice with MVNP targeted to OCLs develop pagetic OCLs and lesions, but this phenotype is absent when MVNP mice are bred to IL-6(-/-) mice. In contrast, mutant p62 expression in OCL precursors promotes receptor activator of NF-κB ligand (RANKL) hyperresponsivity and increased OCL production, but OCLs that form have normal morphology, are not hyperresponsive to 1,25-dihydroxyvitamin D3 (1,25-(OH)2 D3 ), nor produce elevated levels of IL-6. We previously generated p62(P394L) knock-in mice (p62KI) and found that although OCL numbers were increased, the mice did not develop pagetic lesions. However, mice expressing both MVNP and p62KI developed more exuberant pagetic lesions than mice expressing MVNP alone. To examine the role of elevated IL-6 in PD and determine if MVNP mediates its effects primarily through elevation of IL-6, we generated transgenic mice that overexpress IL-6 driven by the tartrate-resistant acid phosphatase (TRAP) promoter (TIL-6 mice) and produce IL-6 at levels comparable to MVNP mice. These were crossed with p62KI mice to determine whether IL-6 overexpression cooperates with mutant p62 to produce pagetic lesions. OCL precursors from p62KI/TIL-6 mice formed greater numbers of OCLs than either p62KI or TIL-6 OCL precursors in response to 1,25-(OH)2 D3 . Histomorphometric analysis of bones from p62KI/TIL-6 mice revealed increased OCL numbers per bone surface area compared to wild-type (WT) mice. However, micro-quantitative CT (µQCT) analysis did not reveal significant differences between p62KI/TIL-6 and WT mice, and no pagetic OCLs or lesions were detected in vivo. Thus, increased IL-6 expression in OCLs from p62KI mice contributes to increased responsivity to 1,25-(OH)2 D3 and increased OCL numbers, but is not sufficient to induce Paget's-like OCLs or bone lesions in vivo. (Link to Publication Site) ● Publication site (DOI): 10.1002/jbmr.2158 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24339057 ● Summary page in Scopus @ Elsevier: 2-s2.0-84901272730 (DOI: 10.1002/jbmr.2158, PubMed: 24339057, Elsevier: Scopus)
35.	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)
36.	J Guo, Di Yang, Hirohiko Okamura, Jumpei Teramachi, Kazuhiko Ochiai, L Qiu and Tatsuji Haneji : Calcium hydroxide suppresses the virulence of lipopolysaccharide from Porphyromonas endodontalis to bone cells, Journal of Dental Research, Vol.93, No.5, 508-513, 2014. (Summary) Porphyromonas endodontalis and its main virulence factor, lipopolysaccharide (LPS), are associated with the development of periapical diseases and alveolar bone loss. Calcium hydroxide is commonly used for endodontic therapy. However, the effects of calcium hydroxide on the virulence of P. endodontalis LPS and the mechanism of P. endodontalis LPS-induced bone destruction are not clear. Calcium hydroxide rescued the P. endodontalis LPS-suppressed viability of MC3T3-E1 cells and activity of nuclear factor-κB (NF-κB) in these cells, resulting in the reduced expression of interleukin-6 and tumor necrosis factor-α. In addition, calcium hydroxide inhibited P. endodontalis LPS-induced osteoclastogenesis by decreasing the activities of NF-κB, p38, and ERK1/2 and the expression of nuclear factor of activated T-cell cytoplasmic 1 in RAW264.7 cells. Calcium hydroxide also rescued the P. endodontalis LPS-induced osteoclastogenesis and bone destruction in mouse calvaria. Taken together, our present results indicate that calcium hydroxide suppressed bone destruction by attenuating the virulence of P. endodontalis LPS on bone cells. (Keyword) 3T3 Cells / Acid Phosphatase / Animals / Biological Markers / Bone Resorption / Calcium Hydroxide / Cell Line / Cell Survival / Extracellular Signal-Regulated MAP Kinases / Interleukin-6 / Isoenzymes / Lipopolysaccharides / Mice / Mitogen-Activated Protein Kinase 3 / NF-kappa B / NFATC Transcription Factors / Osteoblasts / Osteoclasts / Porphyromonas endodontalis / Root Canal Irrigants / Skull / Tumor Necrosis Factor-alpha / X-Ray Microtomography / p38 Mitogen-Activated Protein Kinases (Link to Publication Site) ● Publication site (DOI): 10.1177/0022034514526886 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24603641 ● Summary page in Scopus @ Elsevier: 2-s2.0-84898968069 (DOI: 10.1177/0022034514526886, PubMed: 24603641, Elsevier: Scopus)
37.	Tatsuji Haneji, Kanji Hirashima, Jumpei Teramachi and Hiroyuki Morimoto : Okadaic acid activates the PKR pathway and induces apoptosis through PKR stimulation in MG63 osteoblast-like cells., International Journal of Oncology, Vol.42, No.6, 1904-1910, 2013. (Summary) Double-stranded RNA-dependent protein kinase (PKR) is one of the players in the cellular antiviral responses and is involved in transcriptional stimulation through activation of NF-κB. Treatment of the human osteosarcoma cell line MG63 with the protein phosphatase inhibitor okadaic acid stimulated the expression and phosphorylation of IκBα, as judged from the results of real-time PCR and western blot analysis. We investigated the functional relationship between PKR and signal transduction of NF-κB by establishing PKR-K/R cells that produced a catalytically inactive mutant of PKR. Phosphorylation of eIF-2α, a substrate of PKR, was not stimulated by okadaic acid in the PKR-K/R cells, whereas okadaic acid induced phosphorylation of eIF-2α in MG63 cells. Phosphorylation of NF-κB in MG63 cells was stimulated by okadaic acid; however, okadaic acid did not induce phosphorylation of NF-κB in the PKR-K/R cells. Finally, okadaic acid-induced apoptosis was inhibited in the PKR-K/R cells. Our results suggest that okadaic acid-induced phosphorylation of IκBα was mediated by PKR kinase activity, thus, indicating the involvement of this kinase in the control mechanism governing the activation of NF-κB and induction of apoptosis. (Keyword) Apoptosis / Bone Neoplasms / Cell Line, Tumor / Eukaryotic Initiation Factor-2 / Humans / I-kappa B Proteins / Mutation / NF-kappa B / Okadaic Acid / Osteoblasts / Osteosarcoma / Phosphorylation / Signal Transduction / eIF-2 Kinase (Link to Publication Site) ● Publication site (DOI): 10.3892/ijo.2013.1911 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23591640 ● Summary page in Scopus @ Elsevier: 2-s2.0-84876527228 (DOI: 10.3892/ijo.2013.1911, PubMed: 23591640, Elsevier: Scopus)
38.	Jumpei Teramachi, Yuko Hiruma, Seiichi Ishizuka, Hisako Ishizuka, Jacques P Brown, Laëtitia Michou, Huiling Cao, Deborah L Galson, Mark A Subler, Hua Zhou, W David Dempster, Jolene J Windle, G. David Roodman and Noriyoshi Kurihara : Role of ATF7-TAF12 interactions in the vitamin D response hypersensitivity of osteoclast precursors in Paget's disease, Journal of Bone and Mineral Research, Vol.28, No.6, 1489-1500, 2013. (Summary) Osteoclast (OCL) precursors from many Paget's disease (PD) patients express measles virus nucleocapsid protein (MVNP) and are hypersensitive to 1,25-dihydroxyvitamin D2 (1,25-(OH)2D3; also know as calcitriol). The increased 1,25-(OH)2D3 sensitivity is mediated by transcription initiation factor TFIID subunit 12 (TAF12), a coactivator of the vitamin D receptor (VDR), which is present at much higher levels in MVNP-expressing OCL precursors than normals. These results suggest that TAF12 plays an important role in the abnormal OCL activity in PD. However, the molecular mechanisms underlying both 1,25-(OH)2D3's effects on OCL formation and the contribution of TAF12 to these effects in both normals and PD patients are unclear. Inhibition of TAF12 with a specific TAF12 antisense construct decreased OCL formation and OCL precursors' sensitivity to 1,25-(OH)2D3 in PD patient bone marrow samples. Further, OCL precursors from transgenic mice in which TAF12 expression was targeted to the OCL lineage (tartrate-resistant acid phosphatase [TRAP]-TAF12 mice), formed OCLs at very low levels of 1,25-(OH)2D3, although the OCLs failed to exhibit other hallmarks of PD OCLs, including receptor activator of NF-κB ligand (RANKL) hypersensitivity and hypermultinucleation. Chromatin immunoprecipitation (ChIP) analysis of OCL precursors using an anti-TAF12 antibody demonstrated that TAF12 binds the 24-hydroxylase (CYP24A1) promoter, which contains two functional vitamin D response elements (VDREs), in the presence of 1,25-(OH)2D3. Because TAF12 directly interacts with the cyclic adenosine monophosphate-dependent activating transcription factor 7 (ATF7) and potentiates ATF7-induced transcriptional activation of ATF7-driven genes in other cell types, we determined whether TAF12 is a functional partner of ATF7 in OCL precursors. Immunoprecipitation of lysates from either wild-type (WT) or MVNP-expressing OCL with an anti-TAF12 antibody, followed by blotting with an anti-ATF7 antibody, or vice versa, showed that TAF12 and ATF7 physically interact in OCLs. Knockdown of ATF7 in MVNP-expressing cells decreased cytochrome P450, family 24, subfamily A, polypeptide 1 (CYP24A1) induction by1,25-(OH)2D3, as well as TAF12 binding to the CYP24A1 promoter. These results show that ATF7 interacts with TAF12 and contributes to the hypersensitivity of OCL precursors to 1,25-(OH)2D3 in PD. (Keyword) Activating Transcription Factors / Animals / Calcitriol / Female / Humans / Male / Mice / Mice, Transgenic / Osteitis Deformans / Osteoclasts / RANK Ligand / Response Elements / Stem Cells / Steroid Hydroxylases / TATA-Binding Protein Associated Factors / Transcription, Genetic / Transcriptional Activation (Link to Publication Site) ● Publication site (DOI): 10.1002/jbmr.1884 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23426901 ● Search Scopus @ Elsevier (PMID): 23426901 ● Search Scopus @ Elsevier (DOI): 10.1002/jbmr.1884 (DOI: 10.1002/jbmr.1884, PubMed: 23426901)
39.	Jumpei Teramachi, Akiko Kukita, Pengfei Qu, Naohisa Wada, Yin-Ji Li, Seiji Nakamura and Toshio Kukita : Adenosine blocks aminopterin-induced suppression of osteoclast differentiation, Journal of Bone and Mineral Metabolism, Vol.31, 64-70, 2013. (Summary) To search cell surface molecules involved in the regulation of osteoclastogenesis, especially in fusion process, it is one powerful approach to obtain monoclonal antibodies bearing ability to block formation of multinucleated osteoclasts. Ideally, direct bio-assay of hybridoma supernatants is quite convenient to screen monoclonal antibodies of interest from numerous culture wells. However, addition of hybridoma supernatant containing hypoxanthine-aminopterin-thymidine (HAT), components of the selection medium, to whole bone marrow cultures strikingly suppressed osteoclastogenesis. Here we clarified aminopterin is the responsible component in HAT medium to inhibit osteoclastogenesis. Methotrexate (MTX), mono-methylated aminopterin, showed similar suppressive effect on osteoclastogenesis. When bone marrow cells were cultured in the presence of all nucleosides, aminopterin and MTX-induced suppression of osteoclastogenesis was abrogated. Among four nucleosides only adenosine canceled aminopterin-induced suppression of osteoclastogenesis. Direct bio-assay of hybridoma supernatant containing HAT selection medium is now available to screen monoclonal antibodies if adenosine-containing culture medium was utilized for evaluating osteoclastogenesis. (Keyword) Adenosine / Aminopterin / Analgesics / Animals / Cell Differentiation / Folic Acid Antagonists / Hybridomas / Male / Mice / Osteoclasts / Rats / Rats, Sprague-Dawley (Link to Publication Site) ● Publication site (DOI): 10.1007/s00774-012-0388-7 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23111587 ● Search Scopus @ Elsevier (PMID): 23111587 ● Search Scopus @ Elsevier (DOI): 10.1007/s00774-012-0388-7 (DOI: 10.1007/s00774-012-0388-7, PubMed: 23111587)
40.	Peng Yang, Kyaw-Zeyar Myint, Qin Tong, Rentian Feng, Haiping Cao, A. Abdulrahman Almehizia, Hamed Mohammed Alqarni, Lirong Wang, Patrick Bartlow, Yingdai Gao, Jürg Gertsch, Jumpei Teramachi, Noriyoshi Kurihara, G. David Roodman, Tao Cheng and Xiang-Qun Xie : Lead Discovery, Chemistry Optimization, and Biological Evaluation Studies of Novel Biamide Derivatives as CB2 Receptor Inverse Agonists and Osteoclast Inhibitors, Journal of Medicinal Chemistry, Vol.55, No.22, 9973-9987, 2012. (Summary) N,N'-((4-(Dimethylamino)phenyl)methylene)bis(2-phenylacetamide) was discovered by using 3D pharmacophore database searches and was biologically confirmed as a new class of CB(2) inverse agonists. Subsequently, 52 derivatives were designed and synthesized through lead chemistry optimization by modifying the rings A-C and the core structure in further SAR studies. Five compounds were developed and also confirmed as CB(2) inverse agonists with the highest CB(2) binding affinity (CB(2)K(i) of 22-85 nM, EC(50) of 4-28 nM) and best selectivity (CB(1)/CB(2) of 235- to 909-fold). Furthermore, osteoclastogenesis bioassay indicated that PAM compounds showed great inhibition of osteoclast formation. Especially, compound 26 showed 72% inhibition activity even at the low concentration of 0.1 μM. The cytotoxicity assay suggested that the inhibition of PAM compounds on osteoclastogenesis did not result from its cytotoxicity. Therefore, these PAM derivatives could be used as potential leads for the development of a new type of antiosteoporosis agent. (Keyword) Alkylation / Animals / Benzeneacetamides / Binding, Competitive / Bone Marrow / CHO Cells / Cell Death / Cells, Cultured / Cricetinae / Cyclic AMP / High-Throughput Screening Assays / Humans / Models, Molecular / Molecular Structure / Osteoclasts / Osteogenesis / Receptor, Cannabinoid, CB2 / Structure-Activity Relationship (Link to Publication Site) ● Publication site (DOI): 10.1021/jm301212u (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23072339 ● Search Scopus @ Elsevier (PMID): 23072339 ● Search Scopus @ Elsevier (DOI): 10.1021/jm301212u (DOI: 10.1021/jm301212u, PubMed: 23072339)
41.	Tatsuji Haneji, Jumpei Teramachi, Kanji Hirashima, Koji Kimura and Hiroyuki Morimoto : Interaction of protein phosphatase 1δ with nucleophosmin in human osteoblastic cells, Acta Histochemica et Cytochemica, Vol.45, No.1, 1-7, 2012. (Summary) Protein phosphorylation and dephosphorylation has been recognized as an essential mechanism in the regulation of cellular metabolism and function in various tissues. Serine and threonine protein phosphatases (PP) are divided into four categories: PP1, PP2A, PP2B, and PP2C. At least four isoforms of PP1 catalytic subunit in rat, PP1α, PP1γ1, PP1γ2, and PP1δ, were isolated. In the present study, we examined the localization and expression of PP1δ in human osteoblastic Saos-2 cells. Anti-PP1δ antibody recognized a protein present in the nucleolar regions in Saos-2 cells. Cellular fractionation revealed that PP1δ is a 37 kDa protein localized in the nucleolus. Nucleophosmin is a nucleolar phosphoprotein and located mainly in the nucleolus. Staining pattern of nucleophosmin in Saos-2 cells was similar to that of PP1δ. PP1δ and nucleophosmin were specifically stained as dots in the nucleus. Dual fluorescence images revealed that PP1δ and nucleophosmin were localized in the same regions in the nucleolus. Similar distribution patterns of PP1δ and nucleophosmin were observed in osteoblastic MG63 cells. The interaction of PP1δ and nucleophosmin was also shown by immunoprecipitation and Western analysis. These results indicated that PP1δ associate with nucleophosmin directly in the nucleolus and suggested that nucleophosmin is one of the candidate substrate for PP1δ. (Keyword) protein phosphatase / nucleophosmin / osteoblast (Tokushima University Institutional Repository) ● Metadata: 114979 (Link to Publication Site) ● Publication site (DOI): 10.1267/ahc.11041 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390282679837485056 ● Search Scopus @ Elsevier (DOI): 10.1267/ahc.11041 (Tokushima University Institutional Repository: 114979, DOI: 10.1267/ahc.11041, CiNii: 1390282679837485056)
42.	Akiko Kukita, Toshio Kukita, Kengo Nagata, Jumpei Teramachi, Yin-Ji Li, Hiroki Yoshida, Hiroshi Miyamoto, Steffen Gay, Frank Pessler and Takeo Shobuike : The transcription factor FBI-1/OCZF/LRF is expressed in osteoclasts and regulates RANKL-induced osteoclast formation in vitro and in vivo, Arthritis and Rheumatism, Vol.63, No.9, 2744-2754, 2011. (Summary) Since transcription factors expressed in osteoclasts are possible targets for regulation of bone destruction in bone disorders, we investigated the expression of the transcription factor FBI-1/OCZF/LRF (in humans, factor that binds to inducer of short transcripts of human immunodeficiency virus type 1; in rats, osteoclast-derived zinc finger; in mice, leukemia/lymphoma-related factor) in patients with rheumatoid arthritis (RA), and assessed its role in osteoclastogenesis in vivo. Expression of FBI-1/OCZF was investigated in subchondral osteoclasts in human RA and in rat adjuvant-induced arthritis (AIA) using immunostaining and in situ hybridization, respectively. Transgenic mice overexpressing OCZF (OCZF-Tg) under the control of the cathepsin K promoter were generated, and bone mineral density and bone histomorphometric features were determined by peripheral quantitative computed tomography, calcein double-labeling, and specific staining for osteoclasts and osteoblasts. LRF/OCZF expression and the consequence of LRF inhibition were assessed in vitro with RANKL-induced osteoclast differentiation. FBI-1/OCZF was detected in the nuclei of osteoclasts in rat AIA and human RA. RANKL increased the levels of LRF messenger RNA and nuclear-localized LRF protein in primary macrophages. In OCZF-Tg mice, bone volume was significantly decreased, the number of osteoclasts, but not osteoblasts, was increased in long bones, and osteoclast survival was promoted. Conversely, inhibition of LRF expression suppressed the formation of osteoclasts from macrophages in vitro. FBI-1/OCZF/LRF regulates osteoclast formation and apoptosis in vivo, and may become a useful marker and target in treating disorders leading to reduced bone density, including chronic arthritis. (Keyword) Animals / Arthritis, Experimental / Arthritis, Rheumatoid / Bone Density / Bone and Bones / Cell Differentiation / DNA-Binding Proteins / Female / Humans / Macrophages / Male / Mice / Mice, Transgenic / Osteoblasts / Osteoclasts / RANK Ligand / Rats / Transcription Factors (Link to Publication Site) ● Publication site (DOI): 10.1002/art.30455 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21590684 ● Search Scopus @ Elsevier (PMID): 21590684 ● Search Scopus @ Elsevier (DOI): 10.1002/art.30455 (DOI: 10.1002/art.30455, PubMed: 21590684)
43.	Jumpei Teramachi, Akiko Kukita, Yin-Ji Li, Yuki Ushijima, Hiroshi Ohkuma, Naohisa Wada, Toshiyuki Watanabe, Seiji Nakamura and Toshio Kukita : Adenosine abolishes MTX-induced suppression of osteoclastogenesis and inflammatory bone destruction in adjuvant-induced arthritis, Laboratory Investigation; a Journal of Technical Methods and Pathology, Vol.91, No.5, 719-731, 2011. (Summary) Methotrexate (MTX) is widely utilized for the treatment of patients with rheumatoid arthritis (RA); however, recent observation of the MTX-resistant patients proposed some difficulty in MTX-dependent therapeutic approach for RA. To access cellular events related to MTX resistance in RA in respect to inflammatory bone destruction, we investigated on an involvement of the potent inflammatory mediator adenosine in the regulation of osteoclastogenesis and inflammatory bone destruction. In rats with adjuvant-induced arthritis (AA rats), MTX efficiently suppressed bone destruction when it was administrated within 3 days after adjuvant injection, while it could not suppress inflammatory bone destruction if MTX was injected at the time of onset of inflammation (at day 10 after adjuvant injection). Time-course change in the level of plasma adenosine of AA rats was estimated by use of high-performance liquid chromatography and elucidated that adenosine level was markedly elevated till 10 days after adjuvant injection. In vitro bone marrow culture system for evaluating osteoclastogenesis, MTX markedly suppressed osteoclastogenesis in a stromal cell-dependent manner. This MTX-induced suppression of osteoclastogenesis was abrogated by the addition of adenosine. MTX suppressed the expression of mRNA for the receptor activator NF-κB ligand (RANKL), but it did not suppress the expression of osteoprotegerin (OPG). The addition of MTX and adenosine together markedly suppressed the level of OPG expression. Abolishment of MTX action by adenosine was significantly blocked by MRS1754, a highly selective antagonist for the A(2b) adenosine receptor (A(2b)AR), but not by caffeine, an antagonist for A1, A(2a), A3 AR (A1AR, A(2a)AR, and A3AR), which suggests that adenosine acts through A(2b)AR. Immunohistochemical studies showed abundant expression of A(2b)AR in cells localized in the bone-bone marrow boundary of the distal tibia in AA rats but not in control rats. When adenosine was injected in the ankle joints of MTX-treated AA rats, the suppressive effects of MTX on bone destruction was abolished. The current data therefore suggest that upregulation of adenosine production abolished the suppressive effect of MTX on osteoclastic bone destruction. Involvement of the adenosine-A(2b)AR system may explain MTX resistance in RA. (Keyword) Adenosine / Animals / Antirheumatic Agents / Arthritis, Experimental / Base Sequence / Bone and Bones / Chromatography, High Pressure Liquid / DNA Primers / Immunohistochemistry / Methotrexate / Osteoclasts / Osteoprotegerin / RANK Ligand / Rats / Rats, Inbred Lew / Rats, Sprague-Dawley / Reverse Transcriptase Polymerase Chain Reaction (Link to Publication Site) ● Publication site (DOI): 10.1038/labinvest.2011.9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21339747 ● Search Scopus @ Elsevier (PMID): 21339747 ● Search Scopus @ Elsevier (DOI): 10.1038/labinvest.2011.9 (DOI: 10.1038/labinvest.2011.9, PubMed: 21339747)
44.	Noriyoshi Kurihara, Yuko Hiruma, Kei Yamana, Laëtitia Michou, Côme Rousseau, Jean Morissette, Deborah L. Galson, Jumpei Teramachi, Hua Zhou, David W. Dempster, Jolene J. Windle, Jacques P. Brown and G. David Roodman : Contributions of the Measles Virus Nucleocapsid Gene and the SQSTM1/p62P392L Mutation to Paget's Disease, Cell Metabolism, Vol.13, No.1, 23-34, 2011. (Summary) Paget's disease (PD) is characterized by abnormal osteoclasts (OCL) that secrete high IL-6 levels and induce exuberant bone formation. Because measles virus nucleocapsid gene (MVNP) and the p62(P392L) mutation are implicated in PD, marrows from 12 PD patients harboring p62(P392L) and eight normals were tested for MVNP expression and pagetic OCL formation. Eight out of twelve patients expressed MVNP and formed pagetic OCL in vitro, which were inhibited by antisense-MVNP. Four out of twelve patients lacked MVNP and formed normal OCL that were hyperresponsive to RANKL but unaffected by antisense-MVNP. Similarly, mice expressing only p62(P394L) formed normal OCL, while mice expressing MVNP in OCL, with or without p62(P394L), developed pagetic OCL and expressed high IL-6 levels dependent on p38MAPK activation. IL-6 deficiency in MVNP mice abrogated pagetic OCL development in vitro. Mice coexpressing MVNP and p62(P394L) developed dramatic Paget's-like bone lesions. These results suggest that p62(P394L) and IL-6 induction by MVNP play key roles in PD. (Keyword) Adaptor Proteins, Signal Transducing / Animals / Bone Marrow Cells / Bone and Bones / Calcitriol / Cells, Cultured / Female / Gene Expression / Humans / Interleukin-6 / Measles virus / Mice / Mice, Transgenic / Middle Aged / Mutation / Nucleocapsid / Nucleocapsid Proteins / Osteitis Deformans / Osteoclasts / RANK Ligand / TATA-Binding Protein Associated Factors / p38 Mitogen-Activated Protein Kinases (Link to Publication Site) ● Publication site (DOI): 10.1016/j.cmet.2010.12.002 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21195346 ● Search Scopus @ Elsevier (PMID): 21195346 ● Search Scopus @ Elsevier (DOI): 10.1016/j.cmet.2010.12.002 (DOI: 10.1016/j.cmet.2010.12.002, PubMed: 21195346)
45.	Jumpei Teramachi, Hiroyuki Morimoto, Ryoko Baba, Yoshiaki Doi, Kanji Hirashima and Tatsuji Haneji : Double stranded RNA-dependent protein kinase is involved in osteoclast differentiation of RAW264.7 cells in vitro, Experimental Cell Research, Vol.316, No.19, 3254-3262, 2010. (Summary) Double-stranded RNA-dependent protein kinase (PKR) plays a critical role in antiviral defence of the host cells. PKR is also involved in cell cycle progression, cell proliferation, cell differentiation, tumorigenesis, and apoptosis. We previously reported that PKR is required for differentiation and calcification of osteoblasts. However, it is unknown about the role of PKR in osteoclast differentiation. A dominant-negative PKR mutant cDNA, in which the amino acid lysine at 296 was replaced with arginine, was transfected into RAW264.7 cells. We have established the cell line that stably expresses the PKR mutant gene (PKR-K/R). Phosphorylation of PKR and α-subunit of eukaryotic initiation factor 2 was not stimulated by polyinosic-polycytidylic acid in the PKR-K/R cells. RANKL stimulated the formation of TRAP-positive multinuclear cells in RAW264.7 cells. However, TRAP-positive multinuclear cells were not formed in the PKR-K/R cells even when the cells were stimulated with higher doses of RANKL. A specific inhibitor of PKR, 2-aminopurine, also suppressed the RANKL-induced osteoclast differentiation in RAW264.7 cells. The expression of macrophage fusion receptor and dendritic cell-specific transmembrane protein significantly decreased in the PKR-K/R cells by real time PCR analysis. The results of RT-PCR revealed that the mRNA expression of osteoclast markers (cathepsin K and calcitonin receptor) was suppressed in the PKR-K/R cells and RAW264.7 cells treated with 2-aminopurine. Expression of NF-κB protein was suppressed in the PKR-K/R cells and 2-aminopurine-treated RAW264.7 cells. The level of STAT1 protein expression was elevated in the PKR-K/R cells compared with that of the wild-type cells. Immunohistochemical study showed that PKR was localized in osteoclasts of metatarsal bone of newborn mouse. The finding that the PKR-positive multinuclear cells should be osteoclasts was confirmed by TRAP-staining. Our present study indicates that PKR plays important roles in the differentiation of osteoclasts. (Keyword) Animals / Cell Differentiation / Cell Fusion / Cell Line / Eukaryotic Initiation Factor-2 / Humans / Immunohistochemistry / Macrophages / Mice / Mutation / NF-kappa B / Osteoclasts / Osteogenesis / Phosphorylation / eIF-2 Kinase (Link to Publication Site) ● Publication site (DOI): 10.1016/j.yexcr.2010.08.006 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20728438 ● Search Scopus @ Elsevier (PMID): 20728438 ● Search Scopus @ Elsevier (DOI): 10.1016/j.yexcr.2010.08.006 (DOI: 10.1016/j.yexcr.2010.08.006, PubMed: 20728438)
46.	Yin-Ji Li, Akiko Kukita, Jumpei Teramachi, Kengo Nagata, Zhou Wu, Akifumi Akamine and Toshio Kukita : A possible suppressive role of galectin-3 in upregulated osteoclastogenesis accompanying adjuvant-induced arthritis in rats, Laboratory Investigation; a Journal of Technical Methods and Pathology, Vol.89, No.1, 26-37, 2009. (Summary) Galectin-3 is a beta-galactoside-binding animal lectin having pleiotropic effects on cell growth, differentiation, and apoptosis. This lectin has been shown to be involved in phagocytosis by macrophages and in inflammation. Here we investigated an involvement of galectin-3 in the regulatory process of inflammatory bone resorption in rats with adjuvant-induced arthritis (AA rats) accompanying severe bone destruction in the ankle joints. The protein level of galectin-3 in the ankle-joint extracts was markedly augmented at week 3 after adjuvant injection, at the time when severe bone destruction was observed. Immunohistochemical analysis revealed an extremely high expression of galectin-3 in macrophages and granulocytes infiltrated in the area of severe bone destruction. To estimate the role of galectin-3 in osteoclastogenesis and osteoclastic bone resorption, recombinant galectin-3 was added to in vitro culture systems. Galectin-3 markedly inhibited the formation of osteoclasts in cultures of murine osteoclast precursor cell line as well as in rat bone marrow culture systems. This inhibition was not observed by heat-inactivated galectin-3 or by galectin-7. Although recombinant galectin-3 did not affect signaling through mitogen-activated protein kinase (MAPK) or nuclear factor-kappaB (NF-kappaB), it specifically suppressed the induction of nuclear factor of activated T-cells c1 (NFATc1). Galectin-3 significantly inhibited dentine resorption by mature osteoclasts in vitro. Furthermore, in vivo studies clearly showed a significant suppression of bone destruction and osteoclast recruitment accompanying arthritis, when galectin-3 was injected into the cavity of ankle joint of AA rats. Thus, abundant galectin-3 observed in the area of severe bone destruction may act as a negative regulator for the upregulated osteoclastogenesis accompanying inflammation to prevent excess bone destruction. (Keyword) Animals / Arthritis, Experimental / Bone Marrow Cells / Bone Resorption / Carbohydrate Metabolism / Cell Differentiation / Cell Division / Cells, Cultured / Female / Galectin 3 / Injections, Intra-Articular / Male / NFATC Transcription Factors / Osteoclasts / RANK Ligand / Rats / Rats, Inbred Lew / Rats, Sprague-Dawley / Recombinant Proteins / Severity of Illness Index / Stem Cells / Tibia / Tumor Necrosis Factor-alpha (Link to Publication Site) ● Publication site (DOI): 10.1038/labinvest.2008.111 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19015643 ● Search Scopus @ Elsevier (PMID): 19015643 ● Search Scopus @ Elsevier (DOI): 10.1038/labinvest.2008.111 (DOI: 10.1038/labinvest.2008.111, PubMed: 19015643)
47.	Yong Quan Tang, Toshio Kukita, Yuki Ushijima, Akiko Kukita, Kengo Nagata, Ferry Sandra, Toshiyuki Watanabe, Kazuko Toh, Yutaka Okuma, Sadamichi Kawasaki, Linda Rasubala, Jumpei Teramachi, Ichiko Miyamoto, Zhou Wu and Tadahiko Iijima : Regulation of osteoclastogenesis by Simon extracts composed of caffeic acid and related compounds: successful suppression of bone destruction accompanied with adjuvant-induced arthritis in rats, Histochemistry and Cell Biology, Vol.125, No.3, 215-225, 2006. (Summary) Simon extracts are vitamin K(1)-rich food materials extracted from the leaves of the Simon sweet potato. Although vitamin K is known to stimulate bone formation, we postulated that Simon extracts also contain unknown biological compounds having the ability to regulate bone resorption. Here we prepared the vitamin K-free fraction from the Simon extracts and investigated the ability of this fraction on the differentiation of osteoclasts. A remarkable inhibitory effect of osteoclastogenesis was observed when osteoclast precursors were treated with this fraction in rat bone marrow culture systems as well as in a pure differentiation system using murine osteoclast precursor cell line. The vitamin K-free Simon extracts markedly suppressed severe bone destruction mediated by abundant osteoclasts associated with adjuvant-induced arthritis in rats. High performance liquid chromatography (HPLC) analysis revealed that the vitamin K-free Simon extracts contained three types of low molecular weight inhibitors for osteoclastogenesis; caffeic acid, chlorogenic acids and isochlorogenic acids. Among these substances, caffeic acid showed the most powerful inhibitory effects on osteoclastogenesis. Caffeic acid significantly suppressed expression of NFATc1, a key transcription factor for the induction of osteoclastogenesis. Our current study enlightened a high utility of the Simon extracts and their chemical components as effective regulators for bone resorption accompanied with inflammation and metabolic bone diseases. (Keyword) Animals / Arthritis, Experimental / Base Sequence / Bone Resorption / Caffeic Acids / Cathepsin K / Cathepsins / Cells, Cultured / DNA Primers / Glyceraldehyde-3-Phosphate Dehydrogenases / Ipomoea batatas / Male / Osteoclasts / Phytotherapy / Plant Extracts / Rats / Rats, Inbred Lew / Rats, Sprague-Dawley / Receptor Activator of Nuclear Factor-kappa B / Reverse Transcriptase Polymerase Chain Reaction / Vitamin K (Link to Publication Site) ● Publication site (DOI): 10.1007/s00418-005-0062-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16205940 ● Summary page in Scopus @ Elsevier: 2-s2.0-32444432178 (DOI: 10.1007/s00418-005-0062-4, PubMed: 16205940, 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.	栗原徳善 and Jumpei Teramachi : 麻疹ウイルスの感染とp62の変異はともにPaget's病における破骨細胞の活性亢進に貢献する, ライフサイエンス新着論文レビュー, Jan. 2011.

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.	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)
9.	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.
10.	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.
11.	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.
12.	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.
13.	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.
14.	Takeshi Harada, Asuka Oda, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Oura, Kimiko Sogabe, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa, Shuji Ozaki, Teru Hideshima, C. Kenneth Anderson and Masahiro Abe : Targeting myeloma metabolisms regulated by HDAC1-IRF4 axis can be a novel therapeutic strategy, 17th International Myeloma Workshop, 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.	Takeshi Harada, Asuka Oda, Yohann Grondin, Jumpei Teramachi, Ariunzaya Bat-Erdene, Masami Iwasa, Masahiro Oura, Shingen Nakamura, Kumiko Kagawa, Yasunobu Okamoto, Kimiko Sogabe, Shiroh Fujii, Hirokazu Miki, Shuji Ozaki, Teru Hideshima, Kenneth C. Anderson and Masahiro Abe : The critical role of the HDAC1-IRF4-Pim-2 axis in myeloma cell growth and survival: therapeutic impacts of targeting the HDAC1-IRF4-Pim-2 axis, 60th ASH Annual Meeting & Exposition, San Diego, Dec. 2018.
18.	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.
19.	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.
20.	Takeshi Harada, Oda Asuka, Jumpei Teramachi, Bat-Erdene Ariunzaya, Iwasa Masami, Oura Masahiro, Shingen Nakamura, Kumiko Kagawa, Okamoto Yasunobu, Kimiko Sogabe, Shiroh Fujii, Hirokazu Miki, Hideshima Teru, Anderson C. Kenneth and Masahiro Abe : Selective inhibition of class-I HDAC induces myeloma cell death through targeting IRF4-Pim-2 axis, The 9th JSH International Symposium 2018 in Kyoto, Jul. 2018. (Keyword) Multiple myeloma / Class-I HDAC / IRF4 / Pim2
21.	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.
22.	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.
23.	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.
24.	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.
25.	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.
26.	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.
27.	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.
28.	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.
29.	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.
30.	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.
31.	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.
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.	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.
36.	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.
37.	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.
38.	Hirokazu Miki, Shingen Nakamura, Hirofumi Tenshin, Ryota Amachi, Keiichiro Watanabe, Jumpei Teramachi, Shiroh Fujii, Kumiko Kagawa and Masahiro Abe : Effective impairment of myeloma progenitors by hyperthermia: augmentation with bortezomib and Pim inhibition in combination, Clinical Lymphoma, Myeloma & Leukemia, Vol.15, No.S3, e217-e218, Sep. 2015. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.clml.2015.07.470 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.clml.2015.07.470 (DOI: 10.1016/j.clml.2015.07.470)
39.	Shingen Nakamura, Hirokazu Miki, Hirofumi Tenshin, Ryota Amachi, Keiichiro Watanabe, Jumpei Teramachi, Shiroh Fujii, Kumiko Kagawa and Masahiro Abe : Alteration of Pim-2 expression by clinically available anti-myeloma agents: combinatory anti-myeloma effects with Pim inhibition, Clinical Lymphoma, Myeloma & Leukemia, Vol.15, No.S3, e243, Sep. 2015. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.clml.2015.07.517 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.clml.2015.07.517 (DOI: 10.1016/j.clml.2015.07.517)
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.	Hirohiko Okamura, Di Yang, Jumpei Teramachi and Tatsuji Haneji : PP2A Calpha regulates osteoblast differentiation and function through the expression of bone related genes., 第11回プロテインホスファターゼ国際カンファレンス, 2014年11月12-14日, 東北大学艮陵会館(仙台市, 宮城県), Nov. 2014. (Keyword) osteoblast / protein phosphatase
42.	Yukiko Kitagawa, Jumpei Teramachi, Jolene Windle, John Chirgwin, David G. Roodman and Noriyoshi Kurihara : Increased Expression of TAF12 in the Bone Microenvironment in Multiple Myeloma Enhances Tumor Cell Growth and Osteoclast Formation, 2014 ASBMR Annual Meeting, Houston, Sep. 2014.
43.	Jumpei Teramachi, Yukiko Kitagawa, Jolene Windle, Laetitia Michou, P. Jacques Brown, Noriyoshi Kurihara and David G. Roodman : MVNP Expression in Osteoblast Induces IGF1 to Increase EphrinB2/EphB4 and Osteoblast Differentiation, 2014 ASBMR Annual Meeting, Houston, Sep. 2014.
44.	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.
45.	Rebecca Silbermann, Jumpei Teramachi, Khalid Mohammad, Wei Zhao, Dan Zhou, Peng Yang, L. Julie Eiseman, Xiang-Qun Xie, David G. Roodman and Noriyoshi Kurihara : A Novel Sequestosome-1 / p622 ZZ Domain Inhibitor Blocks TNF Induced Suppression of OBL Differentiation in MM, 2014 ASBMR Annual Meeting, Houston, Sep. 2014.
46.	Jumpei Teramachi, Noriyoshi Kurihara, John M Chirgwin and G David Roodman : Myeloma Cells and Marrow Stromal Cells from Myeloma Patients Have Increased Sensitivity to 1,25-(OH)2D3., 54th American Society of Hematology, Atlanta, Dec. 2012.
47.	Jumpei Teramachi, Jolene J Windle, Khalid Mohammad, Theresa Guise, Noriyoshi Kurihara and G. David Roodman : The Expression of Measles Virus Nucleocapsid Protein Gene in Osteoclasts Induces Expression of Coupling Factors that Stimulate Bone Formation, ASBMR 2012 Annual Meeting, Minneapolis, Oct. 2012.
48.	Jumpei Teramachi, Noriyoshi Kurihara and G. David Roodman : Myeloma Cells and Marrow Stromal Cells from Myeloma Patients Express Increased Levels of TAF12 which Increases their Sensitivity to 1,25-(OH)2D3., ASBMR 2012 Annual Meeting, Minneapolis, Oct. 2012.
49.	Jumpei Teramachi, J Jolene Windle, Noriyoshi Kurihara and G. David Roodman : Increased Expression of IL-6 and the p62P392L Mutation are Sufficient to Induce Pagetic OCL in Mice, ASBMR 2012 Annual Meeting, Minneapolis, Oct. 2012.
50.	Jumpei Teramachi : Contributions of Measles Virus Nucleocapsid Gene and the SQSTM1/p62P392L Mutation to the Paget's Disease, 2012 QOL International Symposium at Niigata, Niigata, Feb. 2012.
51.	Jumpei Teramachi, Yar Kyaw Ze Myint, Rentian Feng, Xiang-Qun Xie, Jolene J Windle, G. David Roodman and Noriyoshi Kurihara : Blocking the ZZ Domain of Sequestosome 1/p62 Suppress the Enhancement of Myeloma Cell Growth and Osteoclast Formation by Marrow Stromal Cells, 53th American Society of Hematology, San Diego, Dec. 2011.
52.	Jumpei Teramachi, Yar Kyaw Ze Myint, Rentian Feng, Xiang-Qun Xie, Jolene J Windle, G. David Roodman and Noriyoshi Kurihara : Blocking the ZZ Domain of Sequestosome 1/p62 Suppress the Enhancement of Myeloma Cell Growth and Osteoclast Formation by Marrow Stromal Cells, The 11th International Conference on Cancer-Induced Bone Disease, Chicago, Nov. 2011.
53.	Tatsuji Haneji, Jumpei Teramachi and Hiroyuki Morimoto : PKR is required for osteoclast differentiation, The 10th China-Japan Joint Seminar on Histochemistry and Cytochemistry, Beijing, China, Oct. 2011. (Keyword) osteoclast / cell differentiation
54.	Jumpei Teramachi, J Jolene Windle, Noriyoshi Kurihara and David G. Roodman : Increased Levels of TAF12 with IL-6 Can Substitute for MVNP to Induce Pagetic-Osteoclasts, ASBMR 2011 Annual Meeting, San Diego, Oct. 2011.
55.	Jumpei Teramachi, Huiling Cao, Jolene J Windle, G. David Roodman and Noriyoshi Kurihara : Role of TAF12 in the Increased VDR Activity in Pagets Disease of Bone, ASBMR 2011 Annual Meeting, San Diego, Oct. 2011.
56.	Jumpei Teramachi, Yar Kyaw Ze Myint, Rentian Feng, Xiang-Qun Xie, G. David Roodman and Noriyoshi Kurihara : The Synthetic Inhibitor of ZZ Domain of Sequestosome-1/p62 Inhibits Both Stromal Cell Independent and Dependent Myeloma Cell Growth and Osteoclast Formation, ASBMR 2011 Annual Meeting, San Diego, Oct. 2011.
57.	Yoko Uehata, Jumpei Teramachi, J Jolene Windle, Noriyoshi Kurihara and David G. Roodman : The Expression of Measles Virus Nucleocapsid Protein (MVNP) Gene in Osteoclasts (OCLs) Induces Expression of Coupling Factors that Stimulate Bone Formation, ASBMR 2011 Annual Meeting, San Diego, Oct. 2011.
58.	Jumpei Teramachi, Jolene J. Windle, J. P. Brown, G. David Roodman and Noriyoshi Kurihara : The ZZ domain of sequestome-1/p62 plays an important role in stromal cell support of myeloma cell growth and osteoclast formation., 52th American Society of Hematology, Orlando, Dec. 2010.

Proceeding of Domestic Conference:

1.	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.
2.	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.
3.	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.
4.	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.
5.	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.
6.	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.
7.	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.
8.	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.
9.	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.
10.	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.
11.	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.
12.	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.
13.	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.
14.	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
15.	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
16.	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.
17.	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.
18.	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.
19.	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.
20.	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.
21.	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.
22.	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.
23.	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
24.	Kimiko Sogabe, Shingen Nakamura, Shiroh Fujii, Hirokazu Miki, 小田明日香, Takeshi Harada, Ryohei Sumitani, Masahiro Oura, Kumiko Kagawa, Hirofumi Tenshin, Jumpei Teramachi, Masaki Ri, Shinsuke Iida and Masahiro Abe : Immediate accumulation of anti-apoptotic PIM2 in myeloma cells by proteasome inhibitors, 第82回日本血液学会学術集会, Oct. 2020.
25.	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.
26.	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.
27.	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.
28.	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.
29.	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
30.	Shuichiroh Atono, Fumiya Kano, Hidetaka Arima, Noboru Hashimoto, Jumpei Teramachi, Tsutomu Iwamoto and Akihito Yamamoto : 歯髄幹細胞由来無血清培養上清を用いた脊髄損傷の治療法開発, 徳島県歯科医学大会, 37, Feb. 2020.
31.	Hidetaka Arima, Fumiya Kano, Shuichiroh Atono, Noboru Hashimoto, Jumpei Teramachi, Tsutomu Iwamoto and Akihito Yamamoto : 間葉系幹細胞由来分泌因子がSchwann細胞の活性化に与える影響, 徳島県歯科医学大会, 36, Feb. 2020.
32.	Keita Kawarabayashi, Fumiya Kano, Noboru Hashimoto, Jumpei Teramachi, Keiko Aota, Masayuki Azuma, Tsutomu Iwamoto and Akihito Yamamoto : 歯髄幹細胞由来無血清培養上清を用いた口腔乾燥症の治療法の開発, 徳島県歯科医学大会, 20, Feb. 2020.
33.	Naoko Ogasawara, Fumiya Kano, Noboru Hashimoto, YAO LIU, Hiroki Mori, Jumpei Teramachi, Tsutomu Iwamoto, Eiji Tanaka and Akihito Yamamoto : 歯髄幹細胞由来無血清培養上清を用いた変形性顎関節症の治療法開発, 徳島県歯科医学大会, 20, Feb. 2020.
34.	浜田麻衣, Atsushi Nakayama, 中山慎一朗, Jumpei Teramachi, Daisuke Tsuji, Akira Shigenaga, 安部正博, Kouji Itou, Akira Otaka and Kosuke Namba : 天然マクロライドの網羅的全合成が拓く新規多発性骨髄腫治療薬の開発研究, 2019年度第2回(第30回)日本プロセス化学会東四国フォーラムセミナー, Oct. 2019.
35.	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.
36.	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.
37.	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.
38.	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.
39.	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.
40.	YAO RIU, Noboru Hashimoto, Jumpei Teramachi, Yoshizo Matsuka, Eiji Tanaka and Akihito Yamamoto : 乳歯歯髄幹細胞培養上清によるマウス坐骨神経結紮モデルにおける神経障害性疼痛の改善．, 第40回日本炎症・再生医学会, Jul. 2019.
41.	浜田麻衣, 森崎巧也, Atsushi Nakayama, Jumpei Teramachi, Daisuke Tsuji, Akira Shigenaga, Takenori Yamamoto, Yasuo Shinohara, Akira Otaka, Kouji Itou, 安部正博 and Kosuke Namba : 天然マクロライドの全合成が拓く新規多発性骨髄腫治療薬, 創薬懇話会2019 in 秋保(仙台), Jun. 2019.
42.	Takeshi Harada, Oda Asuka, Hirofumi Tenshin, Jumpei Teramachi, Masahiro Oura, Kimiko Sogabe, Masami Iwasa, Shiroh Fujii, Hirokazu Miki, Kumiko Kagawa, Teru Hideshima, Anderson C. Kenneth and Masahiro Abe : The novel therapeutic strategy targeting the HDAC1-IRF4-PIM2 pathway in myeloma cells, The 44th Annual Meeting of the Japanese Society of Myeloma, May 2019. (Keyword) Multiple myeloma / Class-I HDAC / IRF4 / Pim-2
43.	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.
44.	Mai Hamada, Atsushi Nakayama, Akira Shigenaga, Daisuke Tsuji, Jumpei Teramachi, 安部正博, Kouji Itou, Akira Otaka and Kosuke Namba : 新規Ynone化合物の創生・評価, 日本薬学会第139年会, Mar. 2019.
45.	Jumpei Teramachi : TAK1阻害による腫瘍進展―骨破壊病変形成悪循環の断絶, 日本解剖学会第72回中国・四国支部学術集会, Oct. 2018.
46.	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.
47.	Masami Iwasa, Takeshi Harada, Bat-Erdene Ariunzaya, 小田明日香, Kimiko Sogabe, Masahiro Oura, Jumpei Teramachi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa and Masahiro Abe : HDAC阻害による骨髄腫細胞のIFN-γ-STAT1- PD-L1経路の増強効果, 第80回日本血液学会学術集会, Oct. 2018. (Keyword) Multiple myeloma
48.	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.
49.	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.
50.	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.
51.	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.
52.	Mariko Ikuo, Kei Sugisaki, Jumpei Teramachi, 田原栄俊, Masahiro Abe and Kouji Itou : 骨芽前駆細胞の骨分化経路BMP/Smadは，核内DNA結合Smadを標的とする多発性骨髄腫由来分泌小胞exosomeによって抑制される, 第91回日本生化学会大会, Sep. 2018.
53.	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.
54.	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.
55.	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.
56.	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.
57.	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.
58.	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.
59.	Masami Iwasa, Takeshi Harada, Bat-Erdene Ariunzaya, 小田明日香, 前田悠作, 高橋真美子, Masahiro Oura, Jumpei Teramachi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Kumiko Kagawa and Masahiro Abe : Amplification of the IFN- γ -STAT1- PD-L1 pathway in myeloma cells by panobinostat, The 43rd Annual Meeting of the Japanese Society of Myeloma, May 2018. (Keyword) Multiple myeloma
60.	Takeshi Harada, Oda Asuka, Jumpei Teramachi, Bat-Erdene Ariunzaya, Iwasa Masami, Maeda Yusaku, Shingen Nakamura, Oura Masahiro, Shiroh Fujii, Hirokazu Miki, Kumiko Kagawa, Hideshima Teru, Anderson C. Kenneth and Masahiro Abe : HDAC1/3 inhibition disrupts the IRF4-Pim-2 pathway to induce effective myeloma cell death, The 43rd Annual Meeting of the Japanese Society of Myeloma, May 2018. (Keyword) Multiple myeloma / Class-I HDAC / IRF4 / Pim-2
61.	Jumpei Teramachi : 骨破壊性腫瘍におけるカテプシンK阻害剤の骨形成誘導作用, 日本解剖学会第72回中国・四国支部学術集会, Oct. 2017.
62.	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.
63.	Jumpei Teramachi : 骨破壊性腫瘍におけるカテプシンK阻害剤の骨形成誘導作用, 第59回歯科基礎医学会学術大会, Sep. 2017.
64.	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.
65.	Jumpei Teramachi : 骨髄腫腫瘍進展抑制と骨形成誘導活性を有する新規薬剤の開発, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, Jul. 2017.
66.	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.
67.	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.
68.	Jumpei Teramachi : 骨形成誘導活性を有する新規骨髄腫治療薬, 第42回日本骨髄腫学会学術大会, May 2017.
69.	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.
70.	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.
71.	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.
72.	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.
73.	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.
74.	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.
75.	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.
76.	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.
77.	Jumpei Teramachi, Hirohiko Okamura and Tatsuji Haneji : TAK-1阻害による腫瘍進展の抑制と骨病変の改善効果, 第58回歯科基礎医学会学術大会, 2016年8月24-26日, 札幌コンベンションセンター(札幌市), Aug. 2016.
78.	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.
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 : 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.
80.	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.
81.	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.
82.	Jumpei Teramachi : TAK-1阻害による骨髄腫腫瘍進展の抑制と骨病変の再生効果, 第41回日本骨髄腫学会学術集会, May 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 : 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.
84.	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.
85.	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.
86.	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.
87.	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.
88.	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.
89.	Jumpei Teramachi, Hirohiko Okamura and Tatsuji Haneji : 6. Pim 阻害による骨髄腫骨吸収亢進の抑制, 第57回歯科基礎医学会学術大会, Sep. 2015.
90.	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.
91.	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.
92.	Hirofumi Tenshin, Jumpei Teramachi, 小田明日香, Ryota Amachi, Keiichiro Watanabe, Shingen Nakamura, Hirokazu Miki, Itsuro Endo, Eiji Tanaka, Toshio Matsumoto and Masahiro Abe : TRAILは破骨細胞分化・生存を促進する:TAK-1による生と死の運命制御, 第1回日本骨免疫学会, 137, Jul. 2015.
93.	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.
94.	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.
95.	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.
96.	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.
97.	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.
98.	Di Yang, Hirohiko Okamura, Jumpei Teramachi and Tatsuji Haneji : Histone demethylase Jmjd3 regulates osteoblast differentiation and apoptosis., Proceedings of the 120th Annual Meeting of The Japanese Association of Anatomists and the 92nd Annual Meeting of The Physiological Society of Japan, March 21-23, 2015, Kobe (, ), Mar. 2015. (Keyword) osteoblast
99.	Hirohiko Okamura, Di Yang, Jumpei Teramachi and Tatsuji Haneji : PP2A Calpha in osteoblasts controls osteoblast and adipocyte differentiation., Proceedings of the 120th Annual Meeting of The Japanese Association of Anatomists and the 92nd Annual Meeting of The Physiological Society of Japan, March 21-23, 2015, Kobe (, ), Mar. 2015. (Keyword) osteoblast / adipocyte
100.	Jumpei Teramachi, Hiroyuki Morimoto, Hirohiko Okamura and Tatsuji Haneji : Critical role of PKR in TNF-a-induced osteoclastogenesis, 第119回日本解剖学会総会・全国学術集会, Mar. 2015.
101.	Jumpei Teramachi : Pim2を標的とした骨髄腫骨病変の新規治療法の開発, 癌と骨病変研究会, Nov. 2014.
102.	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.
103.	Jumpei Teramachi, 篠原宏貴, Yuji Inagaki, Di Yang, Hirohiko Okamura, Toshihiko Nagata and Tatsuji Haneji : PKRによる炎症性骨破壊制御, 日本解剖学会第69回中国・四国支部学術集会プログラム, Oct. 2014.
104.	Hirohiko Okamura, Di Yang, Tatsuji Haneji and Jumpei Teramachi : PP2A C alpha is involved in adipocyte differentiation, 日本解剖学会第69回中国・四国支部学術集会プログラム, Oct. 2014. (Keyword) PP2A / protein phosphatase / adipocyte
105.	Jumpei Teramachi, Hiroyuki Morimoto, Hirohiko Okamura and Tatsuji Haneji : PKRは歯周病におけるLPSおよびTNF-αによる破骨細胞形成促進の重要な因子である．, 第56回歯科基礎医学会学術大会・総会, Sep. 2014.
106.	Hirohiko Okamura, Jumpei Teramachi and Tatsuji Haneji : The role of PP2A C in adipocyte differentiation, 第56回歯科基礎医学会学術大会・総会, Sep. 2014. (Keyword) PP2A / protein phosphatase / adipocyte
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.	Hirohiko Okamura, Jumpei Teramachi and Tatsuji Haneji : The role of protein phosphatase 2A C alpha in bone formation and osteoblast differentiation, The Annual Meeting of the Japanese Society for Bone and Mineral Research Program & Abstracts, 219, Jul. 2014. (Keyword) protein phosphatase / PP2A / osteoblast
109.	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.
110.	Jumpei Teramachi, Yuji Inagaki, Hirohiko Okamura, Toshihiko Nagata and Tatsuji Haneji : PKRは歯周病変における破骨細胞形成及び骨吸収を制御する, 第32回日本骨代謝学会学術集会, Jul. 2014.
111.	篠原宏貴, Jumpei Teramachi, Yuji Inagaki, Jun-ichi Kido, Toshihiko Nagata and Tatsuji Haneji : PKR阻害によるTNF-α誘導性骨吸収の抑制, 第140回日本歯科保存学会春季学会学術大会, Jun. 2014.
112.	篠原宏貴, Jumpei Teramachi, Yuji Inagaki, Jun-ichi Kido, Toshihiko Nagata and Tatsuji Haneji : TNF-α誘導性破骨細胞形成におけるPKRの役割, 第57回春季歯周病学会学術大会, May 2014.
113.	Jumpei Teramachi, 篠原宏貴, Yuji Inagaki, Hiroyuki Morimoto, Toshihiko Nagata and Tatsuji Haneji : The role of PKR on osteoclast formation in the microenvironment of periodontitis, 第119回日本解剖学会総会・全国学術集会, Feb. 2014.
114.	平島寛司, Jumpei Teramachi and Tatsuji Haneji : 歯周疾患部位における破骨細胞分化に対するPKRの役割, 徳島生物学会, Dec. 2013.
115.	Jumpei Teramachi, 篠原宏貴, Yuji Inagaki, Toshihiko Nagata and Tatsuji Haneji : 歯周病変における破骨細胞形成における日本鎖RNA依存性プロテインキナーゼの役割, 日本解剖学会第68回中国・四国支部学術集会, Oct. 2013.
116.	平島寛司, Jumpei Teramachi and Tatsuji Haneji : TNF-α誘導破骨細胞分化におけるPKRの役割, 日本解剖学会第68回中国・四国支部学術集会, Oct. 2013.
117.	Jumpei Teramachi, Hiroyuki Morimoto and Tatsuji Haneji : 炎症性骨破壊におけるPKRの役割, 第54回日本組織細胞化学会総会・学術集会，ワークショップ3, Sep. 2013.
118.	篠原宏貴, Jumpei Teramachi, Yuji Inagaki, Jun-ichi Kido, Toshihiko Nagata and Tatsuji Haneji : 歯周病変における破骨細胞形成に二本鎖RNA依存性プロテインキナーゼが関与する, 第56回秋季歯周病学会学術大会, Sep. 2013.
119.	Jumpei Teramachi, Hiroyuki Morimoto and Tatsuji Haneji : PKRは炎症性骨破壊において重要な役割を果たしている, 第55回歯科基礎医学会総会, Sep. 2013.
120.	Hiroyuki Morimoto, Jumpei Teramachi and Tatsuji Haneji : 破骨細胞の分化を調節する免疫関連分子とその検出法, 第55回歯科基礎医学会総会，サテライトシンポジウム2, Sep. 2013.
121.	Tatsuji Haneji, Jumpei Teramachi, Yoshiki Nakashima and Hiroyuki Morimoto : 破骨細胞の形成とPKR活性, 第117回日本解剖学会総会，2012年3月26-28日，甲府市, Mar. 2012. (Keyword) cell differentiation / osteoclast
122.	Tatsuji Haneji, Jumpei Teramachi, Yoshiki Nakashima and Hiroyuki Morimoto : PKR活性阻害と破骨細胞形成, 第53回歯科基礎医学会総会, Oct. 2011.
123.	Tatsuji Haneji and Jumpei Teramachi : 破骨細胞形成におけるPKR, 第52回日本組織細胞化学会総会・学術集会, Sep. 2011. (Keyword) osteoclast / cell differentiation
124.	Hiroyuki Morimoto, Jumpei Teramachi, Ryouko Baba, Junichi Nakamata, Yoshiaki Doi and Tatsuji Haneji : RANKL刺激による破骨細胞分化におけるPKRの役割, 日本顕微鏡学会第52回九州支部総会・学術講演会, Dec. 2010.
125.	平島寛司, Jumpei Teramachi, 木村幸司 and Tatsuji Haneji : オカダ酸誘導アポトーシスとB23の分解, 日本解剖学会第65回中国・四国支部学術集会, Oct. 2010.
126.	Hiroyuki Morimoto, Jumpei Teramachi and Tatsuji Haneji : PKR活性阻害が軟骨細胞分化に及ぼす影響, 第52回歯科基礎医学会総会, Sep. 2010.
127.	Jumpei Teramachi, Hiroyuki Morimoto and Tatsuji Haneji : PKRは破骨細胞形成を誘導する, 第52回歯科基礎医学会総会, Sep. 2010.
128.	Tatsuji Haneji, Jumpei Teramachi, 木村幸司, 平島寛司, Hiroyuki Morimoto and 土肥良秋 : 蛋白質脱リン酸化酵素PP1d とB23の細胞内局在およびアポトーシス細胞におけるB23の分解, 第51回日本組織細胞化学会総会・学術集会, Sep. 2010.
129.	松原麗, 久木田敏夫, Jumpei Teramachi, 市木佑佳, 野中和明 and 久木田明子 : 破骨細胞特異的表面抗原を認識する抗体Kat1を用いた単核破骨細胞前駆細胞の性状解析, 第28回日本骨代謝学会学術集会, Jul. 2010.
130.	Jumpei Teramachi, 久木田明子, 李銀姫, 中村誠司 and 久木田敏夫 : メソトレキセートによる炎症性骨破壊抑制のアデノシンによる解除, 第28回日本骨代謝学会学術集会, Jul. 2010.
131.	Jumpei Teramachi, 木村幸司, 晨凌, Hiroyuki Morimoto, 土肥良秋 and Tatsuji Haneji : PKRは破骨細胞形成に重要な分子である, 日本解剖学会第64回中国・四国支部学術集会, Oct. 2009.
132.	Tatsuji Haneji, Jumpei Teramachi, Hirohiko Okamura, Kaya Yoshida and Hiroyuki Morimoto : PKR変異型骨芽細胞株における蛋白質脱リン酸化酵素阻害剤によるアポトーシス誘導とIkBの発現, 第51回歯科基礎医学会総会, Sep. 2009.
133.	Tatsuji Haneji and Jumpei Teramachi : 培養細胞の免疫蛍光抗体法, 第34回組織細胞化学講習会, Jul. 2009.
134.	Jumpei Teramachi, 久木田明子, 李銀姫, 和田尚久, 永田健吾, 中村誠司 and 久木田敏夫 : アデノシンは葉酸拮抗剤による破骨細胞形成阻害を骨芽細胞を介して解除する．, 第26回日本骨代謝学会, Oct. 2008.
135.	Jumpei Teramachi, 久木田明子, 李銀姫, 和田尚久, 永田健吾, 中村誠司 and 久木田敏夫 : アデノシンは葉酸拮抗剤による破骨細胞形成阻害を解除する．, 第50回歯科基礎医学会学術大会・総会, Sep. 2008.
136.	Jumpei Teramachi, 久木田明子, 李銀姫, 和田尚久, 永田健吾, 中村誠司 and 久木田敏夫 : 葉酸拮抗剤による破骨細胞形成阻害 ∼アデノシンによる調節∼, 第8回西日本骨・関節関連疾患懇話会, Jul. 2008.
137.	菖蒲池健夫, 久木田敏夫, 永田健吾, Jumpei Teramachi, 朝霧成挙, 高柳広 and 久木田明子 : カテプシンKプロモーターによりOCZFが発現するトランスジェニックマウスの解析, 第30回日本分子生物学会年会, Dec. 2007.
138.	久木田明子, Jumpei Teramachi and 久木田敏夫 : 破骨細胞分化における転写因子の発現と細胞内局在, 第49回歯科基礎医学会学術大会・総会, Aug. 2007.
139.	菖蒲池健夫, 久木田敏夫, 永田健吾, Jumpei Teramachi, 朝霧成挙, 高柳広 and 久木田明子 : カテプシンKプロモーターによりOCZFが発現するトランスジェニックマウスの解析, 第25回日本骨代謝学会, Jul. 2007.

Et cetera, Workshop:

1.	Jumpei Teramachi : TAK1阻害はインフラマソームによる関節破壊を効果的に抑制する, 2018 Bioscience retreat in Awaji, Nov. 2018.
2.	Jumpei Teramachi and Atsushi Nakayama : 骨再生誘導作用を併せ持つ新規抗腫瘍薬の創出, 新技術説明会, Oct. 2018.
3.	Jumpei Teramachi, Hirofumi Tenshin, Itsuro Endo, Toshio Matsumoto and Masahiro Abe : 骨髄腫特異的抗腫瘍活性と骨再生をもたらす新規分子標的薬の開発, 2018 先端医学交流セミナー, Aug. 2018.
4.	Jumpei Teramachi : 骨形成誘導活性を有する新規抗骨髄腫薬の開発, 2017 Bioscience retreat in Tosa, Dec. 2017.
5.	Jumpei Teramachi, Masahiro Hiasa and Masahiro Abe : Development of novel anti-myeloma agents with potent bone anabolic actions, 14th Bone Biology Forum, Aug. 2017.
6.	Jumpei Teramachi : 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, Skeletal Science Retreat 2016, Nov. 2016.
7.	Jumpei Teramachi : 骨髄腫特異的抗腫瘍活性と骨再生をもたらず新規分子標的薬の創出, 骨髄腫セミナー2016, May 2016.
8.	Jumpei Teramachi : 骨髄腫の腫瘍進展と骨破壊病変形成におけるTAK-1の枢軸的な役割, 口腔医科学フロンティア研究会, Feb. 2016.
9.	Jumpei Teramachi, 篠原宏貴, Yuji Inagaki, Hirohiko Okamura and Toshihiko Nagata : 炎症性骨破壊におけるPKRの枢軸的役割, 第135回徳島生物学会, Dec. 2015.
10.	Hirohiko Okamura, Di Yang, Jumpei Teramachi and Tatsuji Haneji : 骨形成および骨芽細胞の分化に関する研究とその手法, 第135回徳島生物学会, Dec. 2015. (Keyword) osteoblast / protein dephosphorylation
11.	Yuji Inagaki, Jumpei Teramachi, Tatsuji Haneji and Toshihiko Nagata : 歯周炎局所の破骨細胞形成における二本鎖RNA依存性プロテインキナーゼ(PKR)の役割, 徳島骨代謝研究会, Nov. 2015.
12.	Jumpei Teramachi : 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18回癌と骨病変研究会, Nov. 2015.
13.	Jumpei Teramachi : 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, 癌と骨病変研究会, Nov. 2015.

Patent:

1.	Jumpei Teramachi, Michiyasu Nakao, Shigeki Sano, Masahiro Abe and Takeshi Harada : PIM2阻害剤, 2021- 14411 (Feb. 2021), 110000796 (Feb. 2021).
2.	Atsushi Nakayama, Jumpei Teramachi, Masahiro Abe, Kosuke Namba, Kouji Itou and Daisuke Tsuji : 新規イノン化合物及びその用途, (Oct. 2019), PCT/JP2019/042086 (Oct. 2019).
3.	Atsushi Nakayama, Jumpei Teramachi, Masahiro Abe, Kosuke Namba, Kouji Itou and Daisuke Tsuji : 新規イノン化合物及びその用途, (Oct. 2018), 2018-203219 (Oct. 2018).

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

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 )
がん細胞被認識強化をもたらす未知生体内標的分子の同定と創薬基盤の構築 (Project/Area Number: 23K06051 )
腫瘍由来新規骨形成抑制分子の機能解析と発現制御 (Project/Area Number: 22K19626 )
The oral-lung axis mediated by exosomes from oral epithelial cells in COVID-19 and the drug discovery (Project/Area Number: 22K19623 )
Molecular basis of the oral-renal linkage by periodontal disease exosomes in exacerbation of diabetes and complications of nephropathy (Project/Area Number: 23K24560 )
Development of novel anti-myeloma agents with potent bone anabolic actions and induction of anti-MM niche through bone cells (Project/Area Number: 17KK0169 )
Development of novel anti-myeloma agents with potent bone anabolic actions (Project/Area Number: 16K11504 )
Role of PP2A in bone formation and mesenchymal cell differentiation (Project/Area Number: 26462786 )
The role of TAF12 in bone marrow stromal cells on osteoclastogenesis (Project/Area Number: 25861745 )
The role of PKR on the differentiation of osteoblasts and formation of osteoclasts (Project/Area Number: 25462859 )
破骨細胞分化および活性化におけるPKRの役割とPKRを分子標的とする骨破壊制御 (Project/Area Number: 22791770 )
The role of PKR, Osterix, and Calcineurin in osteogenesis (Project/Area Number: 21592330 )
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