Synergistic functions of protein phosphorylation and calcium mobilization in platelet activation

K. Kaibuchi, Y. Takai, M. Sawamura, M. Hoshijima, T. Fujikura, Y. Nishizuka

研究成果: ジャーナルへの寄稿学術論文査読

480 被引用数 (Scopus)

抄録

When human platelets were stimulated by synthetic diacylglycerol such as 1-oleoyl-2-acetyl-glycerol, which was a potent activator in vitro of Ca2+ -activated, phospholipid-dependent protein kinase (protein kinase a protein having M(r) ~ 40,000 (40-kilodalton protein) was rapidly phosphorylated, just as it was by natural extracellular messengers such as thrombin. Fingerprint analysis appeared to indicate that protein kinase C was indeed responsible for this 40-kilodalton protein phosphorylation in intact platelets. Under these conditions, neither inositol phospholipid breakdown nor endogenous diacylglycerol formation was observed, indicating that the synthetic diacylglycerol intercalated into the membrane and directly activated protein kinase C without interaction with cell surface receptors. During this process, the diacylglycerol was converted in situ to the corresponding phosphatidate, 1-oleoyl-2-acetyl-glyceryl-3-phosphoric acid. Experiments with the synthetic diacylglycerol and Ca2+ ionophore A23187 suggested that the protein phosphorylation catalyzed by protein kinase C was a prerequisite requirement for the release of serotonin, and that the receptor-linked protein phosphorylation and Ca2+ mobilization acted synergistically to elicit the full physiological cellular response.

本文言語英語
ページ(範囲)6701-6704
ページ数4
ジャーナルJournal of Biological Chemistry
258
11
出版ステータス出版済み - 1983
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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