Cross-linking of Fc gamma receptor I (Fc gamma RI) and receptor II (Fc gamma RII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase.
作者： P.A. Kiener , B.M. Rankin , A.L. Burkhardt , G.L. Schieven , L.K. Gilliland
DOI: 10.1016/S0021-9258(20)80545-6
关键词:
摘要: Stimulation of the human monocytic cell line THP-1 by cross-linking either Fc gamma receptor I (Fc RI) or II RII) gave rise to rapid phosphorylation multiple intracellular proteins. The pattern proteins that were phosphorylated appeared be identical. Analysis these specific immunoprecipitation indicated stimulation through did indeed give same set These included: RII, phospholipase C (PLC) 1, PLC 2, Vav, GAP, and a protein co-precipitated with receptors migrated molecular weight about 70,000. Co-cross-linking an F(ab')2 anti-CD45 monoclonal antibody together antibodies inhibited all tyrosine kinases in cells revealed both stimulated activation kinase recognized Syk. Furthermore, Syk became associated RII following cross-linking. data indicate although two have different cytoplasmic tails, they are coupled signal transduction cascade is regulated CD45 involves
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