Regulation of myosin phosphatase through phosphorylation of the myosin- binding subunit in platelet activation

Keiji Nakai, Yoshinori Suzuki, Hisakazu Kihira, Hideo Wada, Masanori Fujioka, Masaaki Ito, Takeshi Nakano, Kozo Kaibuchi, Hiroshi Shiku, Masakatsu Nishikawa

研究成果: Article査読

49 被引用数 (Scopus)

抄録

Human platelets were found to contain myosin phosphatase consisting of a 38-kD catalytic subunit of protein phosphatase type 18, a 130-kD myosin- binding subunit (MBS) and a 20-kD subunit, all of which cross-reacted with antibodies against these subunits of smooth muscle myosin phosphatase. Anti- MBS antibody coimmunoprecipitated RhoA and Rho-kinase of human platelets. Platelets MBS is a substrate for Rho-kinase and phosphorylation of MBS decreases the activity of myosin phosphatase. Treatment of intact platelets with 9,11-epithio-11,12-methano-thromboxane A2 led to a dramatic increase in phosphorylation of MBS and a significant decrease in the activity of myosin phosphatase. These findings suggest a putative mechanism for agonist-induced regulation of myosin phosphatase activity in platelets.

本文言語English
ページ(範囲)3936-3942
ページ数7
ジャーナルBlood
90
10
DOI
出版ステータスPublished - 15-11-1997

All Science Journal Classification (ASJC) codes

  • 生化学
  • 免疫学
  • 血液学
  • 細胞生物学

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