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• W1963674744 abstract "Activation of the B cell through antigen receptor (BCR) crosslinking is known to initiate a prominent tyrosine kinase cascade and lipid second messenger production through the activation of phospholipase Cγ and phosphatidylinositol 3′ kinase. In this study, we demonstrate that protein kinase C δ (PKCδ) responds to crosslinking of the BCR by becoming activated and tyrosine phosphorylated within 30 s of stimulation. PKCδ activation was dependent primarily on phosphatidylinositol 3′ kinase, and this in turn was dependent on an upstream tyrosine phosphorylation event. Inhibition of PKCδ activation by blocking phosphatidylinositol 3′ kinase was also accompanied by a decrease in its tyrosine phosphorylation, suggesting that PKCδ must be activated in order to become tyrosine phosphorylated. Inhibition of phospholipase C activation had an insignificant effect on the activation of PKCδ, however it attenuated the tyrosine phosphorylation of PKCδ. This suggests a distinct role for phospholipase C in the regulation of PKCδ. This report describes a role for PKCδ in response to the combined signals originated by the BCR." @default.
• W1963674744 created "2016-06-24" @default.
• W1963674744 creator A5011382185 @default.
• W1963674744 creator A5025002688 @default.
• W1963674744 date "1999-10-01" @default.
• W1963674744 modified "2023-09-26" @default.
• W1963674744 title "Activation and tyrosine phosphorylation of protein kinase C δ in response to B cell antigen receptor stimulation" @default.
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• W1963674744 doi "https://doi.org/10.1016/s0161-5890(99)00128-5" @default.
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