Role of protein kinase C in transmembrane signaling

Yoshimi Takai, Kozo Kaibuchi, Terutaka Tsuda, Masahiko Hoshijima

研究成果: Review article査読

61 被引用数 (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.

ジャーナルJournal of Cellular Biochemistry
出版ステータスPublished - 1985

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学


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