Anti-CD9 monoclonal antibody activates p72syk in human platelets.

The Journal of Biological Chemistry
Y OzakiS Nomura

Abstract

NNKY 1-19, anti-CD9 monoclonal antibody (MoAb), induced protein tyrosine phosphorylation of 125-, 97-, 75-, 64-, and 40-kDa proteins in human platelets, whereas F(ab')2 fragments of NNKY 1-19 did not, suggesting that the stimulation of Fc gamma II receptors is required for the induction of protein tyrosine phosphorylation. Tyrosine-phosphorylated proteins of 97 and 125 kDa were associated with aggregation, while NNKY 1-19-induced protein tyrosine phosphorylation was completely inhibited by prostaglandin I2 (PGI2). The activity of p72syk was assessed in immunoprecipitation kinase assays to determine at which step the signal transduction pathway leading to protein tyrosine phosphorylation was suspended. NNKY 1-19 induced a rapid and transient increase in the p72syk-associated tyrosine kinase activity that peaked at 10 s and subsided to the original level 2 min after stimulation. Coinciding with this time course, p60c-src transiently associated with p72syk. In platelets preexposed to GRGDS peptides or PGI2, NNKY 1-19 also increased the p72syk-associated tyrosine kinase activity and led to the association of p60c-src with p72syk. However, in contrast to the control without any inhibitor, the elevated tyrosine kinase activity and th...Continue Reading

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Citations

Jul 1, 1996·Molecular Immunology·M G Tomlinson, M D Wright
Nov 13, 2004·The Journal of Nutritional Biochemistry·N W Schoene, C A Guidry
May 26, 2012·Cancer Cell·Rosa LapalombellaJohn C Byrd
Mar 15, 2005·Platelets·Gregory W Moseley
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Feb 17, 2000·Arteriosclerosis, Thrombosis, and Vascular Biology·C Klein-SoyerF Lanza
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Jul 1, 2004·Journal of Cell Science·Yoko MurayamaYasuhisa Shinomura
Jan 1, 1997·Journal of Virology·S LöfflerJ Schneider-Schaulies

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