Role of protein kinase C in transmembrane signaling

Yoshimi Takai, Kozo Kaibuchi, Terutaka Tsuda, Masahiko Hoshijima

Research output: Contribution to journalReview articlepeer-review

67 Citations (Scopus)


Many extracellular signals elicit Ca2+ mobilization and diacylglycerol formation in their target cells. Diacylglycerol is derived from the receptor‐linked phosphoinositide turnover and serves as a second messenger for the activation of protein kinase C in the presence of Ca2+ and phosphatidylserine. Unique diacylglycerols such as 1‐oleoyl‐2‐acetyl‐glycerol, which activate intracellular protein kinase C when added to intact cells, have been synthesized. Tumor‐promoting phorbol esters substitute for such diacylglycerols and directly activate protein kinase C in both intact cell and cell‐free systems. Under appropriate conditions, the synthetic diacylglycerols and phorbol esters induce protein kinase C activation without Ca2+ mobilization, whereas Ca2+ ionophore A23187 induces Ca2+ mobilization without protein kinase C activation. Using these substances, we have obtained evidence that both protein kinase C and Ca2+ are involved in and play a synergistic role in exocytosis, cell division, and other cellular functions. In this article, the role of protein kinase C in transmembrane signaling is discussed.

Original languageEnglish
Pages (from-to)143-155
Number of pages13
JournalJournal of Cellular Biochemistry
Issue number2
Publication statusPublished - 1985
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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