RGD Reference Report - Identification of a novel cytosolic poly-phosphoinositide-specific phospholipase C (PLC-86) as the major G-protein-regulated enzyme. - Rat Genome Database

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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.
RGD ID: 7257522
Pubmed: PMID:1651229   (View Abstract at PubMed)
PMCID: PMC452947   (View Article at PubMed Central)

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.

Objects referenced in this article
Gene Plce1 phospholipase C, epsilon 1 Rattus norvegicus

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