Receptor-coupled activation of phosphoinositide-specific phospholipase C by an N protein.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Smith, CD; Cox, CC; Snyderman, R

Published Date

  • April 4, 1986

Published In

Volume / Issue

  • 232 / 4746

Start / End Page

  • 97 - 100

PubMed ID

  • 3006254

Pubmed Central ID

  • 3006254

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.3006254

Language

  • eng

Conference Location

  • United States