Premium
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
Author(s) -
Blake Robert A.,
Asselin Judith,
Walker Trevor,
Watson Steve P.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80575-x
Subject(s) - tyrosine phosphorylation , chemistry , phospholipase c , phosphorylation , receptor tyrosine kinase , staurosporine , tyrosine kinase , biochemistry , protein kinase c , receptor , tropomyosin receptor kinase c , thromboxane receptor , tyrosine , ror1 , proto oncogene tyrosine protein kinase src , platelet derived growth factor receptor , microbiology and biotechnology , thromboxane a2 , biology , growth factor
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), Ca 2+ and aggregation, including the FcγRII itself. The role of FcγRII phosphorylation in the regulation of PLC is discussed.