Role of protein kinase C in transmembrane signaling

✍ Scribed by Yoshimi Takai; Kozo Kaibuchi; Terutaka Tsuda; Masahiko Hoshijima

• Publisher: John Wiley and Sons
• Year: 1985
• Tongue: English
• Weight: 756 KB
• Volume: 29
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240290209

✦ Synopsis

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 l-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 A23 187 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.