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- W1736776924 abstract "Publisher Summary Protein kinase C is a multifunctional protein kinase whose in vitro activity is dependent on phospholipid, calcium, and phorbol esters or diacylglycerols. It is also a high-affinity phorbol ester receptor that is nearly ubiquitous in mammalian cells and presumably mediates the biological effects of this class of potent tumor promoters. Diacylglycerols generated by receptor-dependent phosphoinositide degradation are endogenous activators of protein kinase C, functioning as second messengers in hormone signal transduction. This hypothesis is supported by demonstrations that a synthetic diacylglycerol––l-oleoyl-2-acetylglycerol (OAG)––induced biological responses in a variety of cell types. Structural analogs of diC 8 are prepared to provide insight into the molecular mechanism of protein kinase C activation in vitro , to identify inhibitors, and to identify nonmetabolizable activators of protein kinase C in cells. The chapter discusses the uses of diC 8 analogs." @default.
- W1736776924 created "2016-06-24" @default.
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- W1736776924 date "1987-01-01" @default.
- W1736776924 modified "2023-09-27" @default.
- W1736776924 title "Synthesis of cell-permeant diacylglycerol analogs for structure-function analysis of protein kinase C and other enzymes" @default.
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- W1736776924 doi "https://doi.org/10.1016/0076-6879(87)41079-3" @default.
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