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- W2037434894 abstract "Phospholipase C-gamma (PLC-gamma) was rapidly phosphorylated on tyrosines and serines following PDGF and EGF treatment of quiescent 3T3 mouse fibroblasts and A431 human epidermoid cells, respectively, PDGF treatment increased PLC-gamma phosphorylation within 30 sec. This lasted for up to 1 hr, and occurred at high stoichiometry. Continuous receptor occupancy was required to maintain this phosphorylation. Three major sites of tyrosine phosphorylation were detected in PLC-gamma, two of which were phosphorylated in EGF-treated A431 cells. Under certain conditions PDGF receptor coimmunoprecipitated with PLC-gamma, suggesting that PDGF receptor can phosphorylate PLC-gamma directly. Indeed, purified PDGF or EGF receptor phosphorylated purified PLC-gamma on tyrosines identical to those phosphorylated in vivo. Tyrosine phosphorylation of PLC-gamma was not induced by bombesin, TPA, or insulin. Stimulation of PLC-gamma tyrosine phosphorylation and the reported ability of PDGF and EGF to induce phosphatidylinositol turnover in different cells were strongly correlated. We propose that tyrosine phosphorylation of PLC-gamma by PDGF and EGF receptors leads to its activation, and a consequent increase in phosphatidylinositol turnover." @default.
- W2037434894 created "2016-06-24" @default.
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- W2037434894 date "1989-06-01" @default.
- W2037434894 modified "2023-10-11" @default.
- W2037434894 title "Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro" @default.
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- W2037434894 doi "https://doi.org/10.1016/0092-8674(89)90048-2" @default.
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