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Role of protein kinase C in transmembrane signaling
Author(s) -
Takai Yoshimi,
Kaibuchi Kozo,
Tsuda Terutaka,
Hoshijima Masahiko
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240290209
Subject(s) - diacylglycerol kinase , protein kinase c , microbiology and biotechnology , protein kinase a , ask1 , prkcq , second messenger system , mitogen activated protein kinase kinase , biochemistry , map2k7 , signal transduction , biology , kinase , chemistry , cyclin dependent kinase 2
Many extracellular signals elicit Ca 2+ 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 Ca 2+ 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 Ca 2+ mobilization, whereas Ca 2+ ionophore A23187 induces Ca 2+ mobilization without protein kinase C activation. Using these substances, we have obtained evidence that both protein kinase C and Ca 2+ 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.