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 language | English (US) |
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Pages (from-to) | 259-263 |
Number of pages | 5 |
Journal | Cellular Signalling |
Volume | 14 |
Issue number | 3 |
DOIs | |
State | Published - 2002 |
Keywords
- G proteins
- Phosphatidic acid
- Phospholipase C-β
ASJC Scopus subject areas
- Cell Biology