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- W134009153 abstract "The phospholipid-dependent, diacylglycerol or phorbol ester activated serine-threonine protein kinase first described by Nishizuka and colleagues is a major cellular regulatory enzyme (Nishizuka 1988). This protein kinase, protein kinase C (PKC) has been implicated in a variety of cellular processes including secretion, modulation of gene expression, proliferation and tumor promotion. PKC has also been identified as the major intracellular receptor for the tumor-promoting phorbol esters (Nishizuka 1989). The enzyme has a requirement for anionic phospholipids (i.e. phosphatidyl-L-serine) as cofactors (Takai et al. 1979), and also requires phorbol esters or the neutral lipid, sn-1,2 diacylglycerol (Kaibuchi et al. 1981) for maximal activation. sn-1,2 diacylglycerols are the naturally occurring activators of this enzyme." @default.
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- W134009153 date "1992-01-01" @default.
- W134009153 modified "2023-09-23" @default.
- W134009153 title "Structure-Function Studies on the Protein Kinase C Family Members" @default.
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- W134009153 doi "https://doi.org/10.1007/978-3-0348-7315-4_19" @default.
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