PMID: 9555056May 23, 1998Paper

Lipid metabolism in fibroblast growth factor-stimulated L6 myoblasts: a receptor mutation (Y766F) abrogates phospholipase D and diacylglycerol kinase activities

Biochimica Et Biophysica Acta
M C van Dijk, W J van Blitterswijk

Abstract

Phosphatidylcholine (PC) hydrolysis induced by basic fibroblast growth factor (bFGF) was studied in rat L6 myoblasts expressing the wild-type FGF receptor-1 (FGFR-1) or a mutant (Y766F) that is incapable of activating phospholipase C-gamma (PLCgamma). Stimulation of FGFR-1 activated phospholipase D (PLD) rapidly and transiently, but did not induce PC-specific PLC activity. Downregulation of protein kinase C blocked bFGF-induced PLD activation but not phosphatidic acid formation by diacylglycerol (DG) kinase. Only phosphoinositide (PI)-derived DG, not PC-derived DG, appeared to be a substrate for DG kinase. Stimulation of FGFR-1(Y766F) did not activate PLD or DG kinase, both of which apparently require initial PLCgamma activation. The Y766F mutation reduced mitogen-activated protein kinase activation but not cell proliferation. We conclude that both PI turnover and PC hydrolysis are dispensable for bFGF-induced mitogenesis.

References

Jan 1, 1993·Annual Review of Biochemistry·W J FantlL T Williams
Apr 14, 1994·Biochimica Et Biophysica Acta·J H Exton
Jun 13, 1997·The Journal of Biological Chemistry·S G Rhee, Y S Bae
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Citations

Jun 8, 1999·Chemistry and Physics of Lipids·W J van Blitterswijk, B Houssa
Mar 6, 1999·The Journal of Biological Chemistry·B HoussaW J van Blitterswijk
Jul 19, 2002·Advances in Enzyme Regulation·Lisa BregoliDaniel M Raben

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