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- W1630258713 endingPage "450" @default.
- W1630258713 startingPage "431" @default.
- W1630258713 abstract "This chapter provides an overview of mammalian phospholipase C. The hydrolysis of cellular phospholipids leads to the formation of various bioactive lipid mediators, acting either as extracellular signaling molecules or as intracellular second messengers. A well-known second messenger-forming system involving phospholipid hydrolysis is the stimulation of phosphoinositide-specific phospholipase C (PLC) isoforms. Eleven mammalian PLC isoforms are identified and divided into four groups: PLC-β1-4, PLC-γ1-2, PLC-δ1-4, and PLC-є1. PLC-1 is the homologue of PLC210 from Caenorhabditis elegans, probably acting as a downstream effector of Ras. Furthermore, it is evident that the PLC enzymes greatly differ in their responsiveness to receptor and non-receptor tyrosine kinases, heterotrimeric G proteins coupling to the family of serpentine receptors, small GTPases and calcium, probably due to their structural organization. Besides distinct modes of activation by membrane receptors, agonist-induced recruitment of PLC enzymes to the plasma membrane, in particular to signaling microdomain, such as caveolae and lipid rafts, represents the initial common regulatory principle." @default.
- W1630258713 created "2016-06-24" @default.
- W1630258713 creator A5006931739 @default.
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- W1630258713 creator A5036610105 @default.
- W1630258713 creator A5040820485 @default.
- W1630258713 creator A5052754373 @default.
- W1630258713 date "2003-01-01" @default.
- W1630258713 modified "2023-09-27" @default.
- W1630258713 title "Mammalian phospholipase C" @default.
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