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Biochem Biophys Res Commun. 1999 May 10;258(2):425-30.

Association of heterotrimeric G-proteins with bovine aortic phospholipase C gamma.

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Physiology Laboratory, University of Oxford, Parks Road, Oxford, OX1 3PT, United Kingdom.


The widely expressed phospholipase C gamma1 (PLCgamma1) isoform has been implicated in the signalling of cell growth through its ability to hydrolyse phosphatidylinositol 4,5-bisphosphate to give inositol 1,4,5-trisphosphate and 1,2-diacylglycerol. Stimulation of PLCgamma1 activity occurs upon phosphorylation of specific tyrosine residues, although it is unclear how this phosphorylation actually stimulates catalytic activity. Indeed recent reports suggest that accessory factors such as GTP-binding proteins may also be required for complete activation of PLCgamma1 in some cells. This may be of importance in vascular smooth muscle where traditionally G-protein linked PLCbeta isoforms are often absent. Here, we show that bovine aortic PLCgamma1 activity is substantially enhanced by both GTPgammaS and sodium fluoride. Similarly, immunoprecipitated PLCgamma1 is associated with an approximately 40kDa GTPgammaS-binding protein and both Galphai and Galphaq were detected in this immunoprecipitate. This data suggests that bovine aortic PLCgamma1 is both associated with, and may be activated by, heterotrimeric G-proteins.

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