Phosphatidic acid modulates G protein regulation of phospholipase C-β1 activity in membranes

Irene Litosch

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Regulation of G protein stimulated phospholipase C-β1 (PLC-β1) activity by phosphatidic acid (PA) was determined in membranes. In cerebral cortical membranes, PLC-β1 is under dual regulation by G protein stimulatory and inhibitory mechanisms. PA stimulated basal activity and was synergistic with G protein activation in increasing PLC-β1 activity. Lysophosphatidic acid (LPA) also stimulated PLC-β activity, but was less effective then PA. PA stimulation of PLC-β1 activity was relatively independent of acyl chain length. PA decreased the Ca2+ dependence for G protein stimulation of PLC-β1 activity. PA modulated the dual G protein regulation of PLC-β1 activity, increasing stimulatory regulation and reducing inhibitory G protein regulation. The sensitivity to guanosine 5′-[γ-thio]trisphosphate (GTP-γ-S) and carbachol stimulation of PLC-β1 activity was increased by PA. These results demonstrate that PA regulates both basal activity and G protein stimulation of PLC-β1 activity. The data indicates that PA regulates the PLC-β1 signaling pathway and thus may have an important role in the modulation of cell activation.

Original languageEnglish (US)
Pages (from-to)259-263
Number of pages5
JournalCellular Signalling
Volume14
Issue number3
DOIs
StatePublished - 2002

Keywords

  • G proteins
  • Phosphatidic acid
  • Phospholipase C-β

ASJC Scopus subject areas

  • Cell Biology

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