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

FEBS Letters

Watson, Steve P.¹  Blake, Robert A.¹  Walker, Trevor¹  Asselin, Judith¹ 

[1] Department of Pharmacology, Mansfield Road, Oxford, OX1 3QT, UK

关键词: Feγ receptor;    Phospholipase C;    Tyrosine phosphorylation;    Human platelet;    Immune complex;    Tyrosine kinase inhibitor;    FcγRII;    Fcγ receptor II;    mAb;    monoclonal antibody;    PKC;    protein kinase C;    PLC;    phospholipase C;    PMSF;    phenylmethylsulfonyl fluoride;   

DOI  :  10.1016/0014-5793(94)80575-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We report that activation of phospholipase C (PLC) by cross-linking of the platelet low-affinity Fcγ receptor II (Fcγ 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 FcγRII cross-linking upstream of protein kinase C (PKC), Ca²⁺ and aggregation, including the FcγRII itself. The role of FcγRII phosphorylation in the regulation of PLC is discussed.

【 授权许可】

Unknown