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Identification of a novel cytosolic poly‐phosphoinositide‐specific phospholipase C (PLC‐86) as the major G‐protein‐regulated enzyme.
Author(s) -
Thomas G.M.,
Geny B.,
Cockcroft S.
Publication year - 1991
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1991.tb07790.x
Subject(s) - biology , cytosol , phospholipase c , enzyme , biochemistry , phospholipase , identification (biology) , phosphoinositide phospholipase c , microbiology and biotechnology , botany
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.