A role of calcium-activated, phospholipid-dependent protein kinase in platelet-activating factor-induced serotonin release from rabbit platelets

Hidetaka Ieyasu, Yoshimi Takai, Kozo Kaibuchi, Makoto Sawamura, Yasutomi Nishizuka

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

Abstract

When rabbit platelets were stimulated by platelet-activating factor (PAF), phosphatidylinositol disappeared rapidly and diacylglycerol was transiently accumulated. Concurrently, an endogenous protein with a molecular weight of about 40,000 (40K protein) was heavily phosphorylated and serotonin was released. These PAF-induced reactions were associated with one another, and simultaneously inhibited by prostaglandin E1 and dibutyryl cyclic AMP. Fingerprint analysis of the phosphorylation sites in 40K protein suggested that Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) was responsible for the phosphorylation of 40K protein. PAF did not appear to activate protein kinase C directly. It is likely that PAF causes the release of serotonin in a mechanism analogous to the thrombin action through its receptor-mediated activation of this unique protein kinase system.

Original languageEnglish
Pages (from-to)1701-1708
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume108
Issue number4
DOIs
Publication statusPublished - 29-10-1982
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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