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J. Biol. Chem., Vol. 266, Issue 3, 1359-1362, Jan, 1991

Nerve growth factor stimulates phosphorylation of phospholipase C-gamma in PC12 cells

UH Kim, D Fink Jr, HS Kim, DJ Park, ML Contreras, G Guroff and SG Rhee
Signal Transduction Section, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.

PC12 cells contain at least three immunologically distinct phospholipase C (PLC) isozymes, PLC-beta, PLC-gamma, and PLC-delta. Treatment of PC12 cells with nerve growth factor (NGF) leads to an increase in the phosphorylation of PLC-gamma, but not of PLC-beta or PLC-delta. This increase can be seen in as little as 1 minute. The increased phosphorylation occurs on both serine and tyrosine residues, with the major increase being in the former. This result suggests the possibility that the NGF-dependent increase in phosphoinositide hydrolysis in PC12 cells is due to selective phosphorylation of PLC- gamma by serine and tyrosine protein kinases associated with the NGF receptor.
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