ISHII Satoshi



Graduate School of Medicine  Doctorial Course in Medicine  Bioregulatory Medicine  Department of Immunology

Laboratory Address

1-1-1 Hondo, Akita-City, Akita 010-8543, Japan

Laboratory Phone number


Laboratory Fax number


Mail Address

E-mail address

Research Fields, Keywords

G-protein-coupled receptor , Bioactive lipid

Graduating School 【 display / non-display

  • 1984.04

    Tokyo Institute of Technology   Faculty of Science   Graduated

Graduate School 【 display / non-display

  • 1988.04

    Tokyo Institute of Technology  Graduate School, Division of Integrated Science and Engineering  Master's Course  Completed

Campus Career 【 display / non-display

  • 2010.02

    Akita University   Graduate School of Medicine   Doctorial Course in Medicine   Bioregulatory Medicine   Professor  

Research Field (grants-in-aid-for-scientific-research classification) 【 display / non-display

  • General medical chemistry


Published Papers 【 display / non-display

  • Lysophosphatidic acid-induced YAP/TAZ activation promotes developmental angiogenesis by repressing Notch ligand Dll4

    Yasuda D.

    Journal of Clinical Investigation ( Journal of Clinical Investigation )  129 ( 10 ) 4332 - 4349   2019.10  [Refereed]

    Domestic Co-author


  • Molecular mechanism of lysophosphatidic acid-induced hypertensive response

    Kano K.

    Scientific Reports ( Scientific Reports )  9 ( 1 )   2019.02  [Refereed]

    Domestic Co-author


  • The Gα12/13-coupled receptor LPA4 limits proper adipose tissue expansion and remodeling in diet-induced obesity

    Yanagida K.

    JCI insight ( JCI insight )  3 ( 24 ) e97293   2018.12  [Refereed]

    Domestic Co-author

    DOI PubMed

  • LPA5 signaling is involved in multiple sclerosis-mediated neuropathic pain in the cuprizone mouse model

    Tsukahara R.

    Journal of Pharmacological Sciences ( Journal of Pharmacological Sciences )  136 ( 2 ) 93 - 96   2018.02  [Refereed]

    Domestic Co-author

    Lysophosphatidic acid (LPA) and LPA1 receptor signaling play a crucial role in the initiation of peripheral nerve injury-induced neuropathic pain through the alternation of pain-related genes/proteins expression and demyelination. However, LPA and its signaling in the brain are still poorly understood. In the present study, we revealed that the LPA5 receptor expression in corpus callosum elevated after the initiation of demyelination, and the hyperalgesia through Aδ-fibers following cuprizone-induced demyelination was mediated by LPA5 signaling. These data suggest that LPA5 signaling may play a key role in the mechanisms underlying neuropathic pain following demyelination in the brain.

    DOI PubMed

  • Identification of optineurin as an interleukin-1 receptor-associated kinase 1-binding protein and its role in regulation of MyD88-dependent signalling

    Tanishima M.

    Journal of Biological Chemistry ( Journal of Biological Chemistry )  292 ( 42 ) 17250 - 17257   2017.10  [Refereed]

    Domestic Co-author

    Upon stimulation of toll-like receptors with various microbial ligands, induction of a variety of inflammatory genes is elicited by activation of a myeloid differentiation primary-response protein 88 (MyD88)-dependent signaling pathway. Interleukin-1 (IL-1) receptor-associated kinase 1 (IRAK1) plays an essential role in this pathway by activating nuclear factor kappa B (NF-kappa B) and mitogen-activated kinases (MAPKs). Here, we identified optineurin (OPTN) as an IRAK1-binding protein by yeast two-hybrid screening using IRAK1 as bait. A C-terminal fragment of OPTN harboring a ubiquitin-binding domain was co-immunoprecipitated with IRAK1. In reporter analyses, overexpression of OPTN inhibited IL-1 beta-, IRAK1-, and LPS-induced NF-kappa B activation. Consistently, OPTN deficiency resulted in increased NF-kappa B activation in response to IL-1 beta/LPS stimulation. To address the mechanisms underlying the inhibitory effect of OPTN on NF-kappa B signaling, we focused on tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6), which is an adaptor protein of IRAK1 and upon polyubiquitination plays a crucial role during NF-kappa Bactivation. Overexpression of OPTN prevented TRAF6 polyubiquitination. Furthermore, OPTN H486R mutant, which is unable to recruit the deubiquitinase CYLD, failed to inhibit IRAK1-induced NF-kappa Bactivation. These results suggest that the IRAK1-binding protein OPTN negatively regulates IL-1 beta/LPS-induced NF-kappa Bactivation by preventing polyubiquitination of TRAF6.

    DOI PubMed

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Grant-in-Aid for Scientific Research 【 display / non-display

  • Grant-in-Aid for Scientific Research(B)

    Project Year: 2019.04  -  2022.03