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• W2034016143 startingPage "149" @default.
• W2034016143 abstract "We have shown previously that the stem cell factor (SCF) receptor undergoes phosphorylation on serine residues following ligand stimulation, and that this phopshorylation is dependent mainly on the activity of protein kinase C (PKC). In the present study, we have further investigated the molecular mechanisms behind SCF-stimulated activation of PKC, and found that SCF does not activate phosphati-dylinositol-specific phospholipase C. In contrast, phospholipase D (PLD) is activated in response to SCF in a dose-dependent manner. Activation of PLD was not inhibited by calphostin C, an inhibitor of PKC. On the other hand, inhibitors of phosphatidylinositol Ptdlns 3'-kinase (Ptdlns 3'-kinase), i.e. wortmannin and LY294002, inhibited SCF-induced PLD activation. Moreover, a mutant SCF receptor in which Tyr721, which is responsible for activation of Ptdlns 3'-kinase, is mutated to a phenylalanine residue was unable to mediate activation of PLD. Thus, PtdIns 3'-kinase appears to be essential for SCF-induced PLD activation. Furthermore, we demonstrate that phosphatidic acid (PtdH), generated through the action of PLD in response to SCF, is metabolized to diacylglycerol by dephosphorylation. Diacylglycerol can then activate PKC, and, moreover, after deacylation by a diacylglycerol lipase, yield arachidonic acid, an important second messenger in cell signaling." @default.
• W2034016143 created "2016-06-24" @default.
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• W2034016143 creator A5084535456 @default.
• W2034016143 date "1997-08-15" @default.
• W2034016143 modified "2023-10-17" @default.
• W2034016143 title "Involvement of Phosphatidylinositol 3'-Kinase in Stem-Cell-Factor-Induced Phospholipase D Activation and Arachidonic Acid Release" @default.
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• W2034016143 doi "https://doi.org/10.1111/j.1432-1033.1997.00149.x" @default.
• W2034016143 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9310372" @default.
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