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FEBS Lett. 1994 Mar 28;342(1):15-8.

Fc gamma receptor II stimulated formation of inositol phosphates in human platelets is blocked by tyrosine kinase inhibitors and associated with tyrosine phosphorylation of the receptor.

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Department of Biochemistry, University of Dundee, Scotland.


We report that activation of phospholipase C (PLC) by cross-linking of the platelet low-affinity Fc gamma receptor II (Fc gamma RII) is inhibited by two structurally distinct tyrosine kinase inhibitors, staurosporine and ST271. This contrasts with PLC activation induced by thrombin and U46619, a thromboxane mimetic, whose receptors have seven transmembrane domains characteristic of G-protein coupled receptors. Several proteins undergo phosphorylation on tyrosine on Fc gamma RII cross-linking upstream of protein kinase C (PKC), Ca2+ and aggregation, including the Fc gamma RII itself. The role of Fc gamma RII phosphorylation in the regulation of PLC is discussed.

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