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Identification of a novel cytosolic poly-phosphoinositide-specific phospholipase C (PLC-86) as the major G-protein-regulated enzyme.

Authors: Thomas, GM  Geny, B  Cockcroft, S 
Citation: Thomas GM, etal., EMBO J. 1991 Sep;10(9):2507-12.
Pubmed: (View Article at PubMed) PMID:1651229

Activation of phosphoinositide-specific phospholipase C (PLC) generates two intracellular signals which play major roles in many cellular processes including secretion, proliferation and contraction. PLC activation by many receptors occurs via a guanine nucleotide regulatory protein, Gp. PLCs are found predominantly in the cytosolic fraction though some activity is membrane-associated. At least four families of iso-enzymes of PLC (alpha, beta, gamma and delta) have been identified, but there is only scant evidence to indicate that any of the mammalian cytosolic activities are involved in G-protein-regulated signalling. In this study we demonstrate that the PLC activity from rat brain cytosol can be regulated in a G-protein-dependent manner in a reconstituted system using pre-permeabilized HL60 cells. We identify two enzymes, PLC-beta and a novel 86 kDa enzyme (designated PLC-epsilon) as the G-protein-regulated enzymes. PLC-epsilon was found to be the major G-protein-regulated enzyme.


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RGD Object Information
RGD ID: 7257522
Created: 2013-08-21
Species: All species
Last Modified: 2013-08-21
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.