Comparison of the modes of action of Ca2+ ionophore A23187 and thrombin in protein kinase C activation in human platelets

Kimihiko Sano, Hajime Nakamura, Tamotsu Matsuo, Yasuhiro Kawahara, Hisashi Fukuzaki, Kozo Kaibuchi, Yoshimi Takai

研究成果: Article査読

10 被引用数 (Scopus)


In human platelets, the Ca2+ ionophore A23187 stimulated the phosphorylation of a 40 kDa protein and myosin light chain (MLC) to the same extents as those induced by thrombin, but the doses of A23187 for 40 kDa protein phosphorylation were higher than those for MLC phosphorylation, although the doses of thrombin for both reactions were nearly the same. Moreover, A23187 produced much less diacylglycerol than thrombin. However, the sites of the 40 kDa protein phosphorylated by the action of A23187 and thrombin were identical, and the 40 kDa protein phosphorylation induced by A23187 and thrombin was inhibited by tetracaine, an inhibitor for protein kinase C. Neither A23187 nor thrombin induced the production of a catalytic fragment of protein kinase C which might be generated by limited proteolysis with Ca2+-dependent protease. These results indicate that A23187 induces protein kinase C activation which phosphorylates the 40 kDa protein, but higher doses of A23187 are required for the activation of this enzyme than for the activation of MLC kinase.

ジャーナルFEBS Letters
出版ステータスPublished - 11-11-1985

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学


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