Yamamoto Hideyuki

写真a

Title

Professor(Moving Out or Retirement)

Researcher Number(JSPS Kakenhi)

60191433

Laboratory Address

207 Uehara,Nishihara,Okinawa

Mail Address

E-mail address

Laboratory Phone number

+81-98-895-1112

Laboratory Fax number

+81-98-895-1114

Homepage URL

http://biochem.med.u-ryukyu.ac.jp/

Current Affiliation Organization 【 display / non-display

  • Duty   University of the Ryukyus   Graduate School of Medicine   Professor  

Academic degree 【 display / non-display

  • Kumamoto University -  Doctor of Medical Science

External Career 【 display / non-display

  • 2006.04
     
     

    University of the Ryukyus, Graduate School of Medicine, Professor  

Research Interests 【 display / non-display

  • Bioochemistry

  • Neurochemistry

  • Neuropharmacology

  • 神経薬理学

Research Areas 【 display / non-display

  • Life Science / Neuroscience-general

  • Life Science / Medical biochemistry

Thesis 【 display / non-display

  • The role of Ca, calmodulin-dependent phosphorylation in the regulation of microtubule formation

    1985.03

Published Papers 【 display / non-display

  • Roles of Pyk2 in signal transduction after gonadotropin-releasing hormone receptor stimulation.

    Okitsu-Sakurayama S, Higa-Nakamine S, Torihara H, Higashiyama S, Yamamoto H

    Journal of cellular physiology ( Journal of Cellular Physiology )    2020.09 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

  • Regulation of epidermal growth factor receptor expression and morphology of lung epithelial cells by interleukin-1β.

    Nakayama I, Higa-Nakamine S, Uehara A, Sugahara K, Kakinohana M, Yamamoto H

    Journal of biochemistry ( Journal of biochemistry )  168 ( 2 ) 113 - 123   2020.08 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

  • Fyn-mediated phosphorylation of Pyk2 promotes its activation and dissociation downstream of gonadotropin-releasing hormone receptor.

    Higa-Nakamine S, Okitsu-Sakurayama S, Kina S, Yamamoto H

    The FEBS journal ( FEBS Journal )  287 ( 16 ) 3551 - 3564   2020.08 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

  • Increased expression of EGR1 and KLF4 by polysulfide via activation of the ERK1/2 and ERK5 pathways in cultured intestinal epithelial cells.

    Arakaki K, Uehara A, Higa-Nakamine S, Kakinohana M, Yamamoto H

    Biomedical research (Tokyo, Japan) ( バイオメディカルリサーチプレス )  41 ( 3 ) 119 - 129   2020 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

     View Summary

    <p>Sodium trisulfide (Na<sub>2</sub>S<sub>3</sub>) releases hydrogen polysulfide (H<sub>2</sub>S<sub>n</sub>) and is useful for the investigation of the effects of H<sub>2</sub>S<sub>n</sub> on the cell functions. In the present study, we first examined the effects of Na<sub>2</sub>S<sub>3</sub> on the gene expression of IEC-6 cells, a rat intestinal epithelial cell line. Microarray analysis and reverse transcription-polymerase chain reaction analysis revealed that Na<sub>2</sub>S<sub>3</sub> increased the gene expression of early growth response 1 (EGR1) and Kruppel-like transcription factor 4 (KLF4). It was interesting that U0126, an inhibitor of the activation of extracellular signal-regulated kinase 1 (ERK1), ERK2, and ERK5, inhibited the Na<sub>2</sub>S<sub>3</sub>-induced gene expression of EGR1 and KLF4. Na<sub>2</sub>S<sub>3</sub> activated ERK1 and ERK2 (ERK1/2) within 15 min. In addition to ERK1/2, Na<sub>2</sub>S<sub>3</sub> activated ERK5. We noticed that the electrophoretic mobility of ERK5 was decreased after Na<sub>2</sub>S<sub>3</sub> treatment. Phos-tag analysis and <i>in vitro</i> dephosphorylation of the cell extracts indicated that the gel-shift of ERK5 was due to its phosphorylation. The gel-shift of ERK5 was inhibited completely by both U0126 and ERK5-IN-1, a specific inhibitor of ERK5. From these results, we concluded that the gel-shift of ERK5 was induced through autophosphorylation by activated ERK5 after Na<sub>2</sub>S<sub>3</sub> treatment. The present study suggested that H<sub>2</sub>S<sub>n</sub> affected various functions of intestinal epithelial cells through the activation of the ERK1/2 and ERK5 pathways.</p>

  • Activation of Pyk2 by CaM kinase II in cultured hypothalamic neurons and gonadotroph cells.

    Okitsu-Sakurayama S, Higa-Nakamine S, Torihara H, Takahashi H, Higashiyama S, Yamamoto H

    Journal of cellular physiology ( Journal of Cellular Physiology )  234 ( 5 ) 6865 - 6875   2019.05 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

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