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Science 4 April 1986: Vol. 232. no. 4746, pp. 97 - 100 DOI: 10.1126/science.3006254
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Articles
Science, Vol 232, Issue 4746, 97-100
Copyright © 1986 by American Association for the Advancement of Science
Receptor-coupled activation of phosphoinositide-specific phospholipase C by an N protein
CD Smith,
CC Cox,
and
R Snyderman
Cleavage of phosphatidylinositol 4,5-bisphosphate by phospholipase C results in the production of two important second messengers: inositol-1,4,5-trisphosphate and 1,2-diacylglycerol. Although several receptors promote this cleavage, the molecular details of phospholipase C activation have remained unresolved. In this study, occupancy of a Ca2+-mobilizing receptor, the oligopeptide chemoattractant receptor on human polymorphonuclear leukocyte plasma membranes, was found to lead to the activation of a guanine nucleotide regulatory (N) protein by guanosine 5'-triphosphate. The activated N protein then stimulated a polyphosphoinositide-specific phospholipase C by reducing the Ca2+ requirement for expression of this activity from superphysiological to normal intracellular concentrations. Therefore, the N protein-mediated activation of phospholipase C may be a key step in the pathway of cellular activation by chemoattractants and certain other hormones.
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