Activation of phospholipase C-gamma is necessary for stimulation of phospholipase D by platelet-derived growth factor.

摘要: Platelet-derived growth factor (PDGF) stimulates phosphatidylcholine hydrolysis via phospholipase D (PLD) in several tissues. To determine whether PLD activation is dependent on phosphoinositide by C (PLC), we measured the formation of phosphatidylbutanol (PtdBut), TRMP cells overexpressing wild type or various mutant PDGF receptors. Both PLC and were stimulated expressing receptors whereas they not kinase-deficient (R634) These data indicate that tyrosine phosphorylation required for both PLD. Mutation Tyr-1021 receptor to Phe caused loss stimulation On other hand, a was able bind gamma 1 but signaling proteins (including Ras GTPase-activating protein, phosphatidylinositol 3-kinase, SH2-containing phosphotyrosine phosphatase (Syp)) restored stimulatory effect Furthermore, which association with Syp individually unable mediate these signal transduction are involved PDGF. Treatment protein kinase inhibitor, Ro-31-8220, depletion cellular pretreatment 4 beta-phorbol 12-myristate 13-acetate resulted indicating PKC-dependent mechanism. In summary, results necessary provide no evidence alternative mechanisms.