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Volume 270, Number 25, Issue of June 23, pp. 15119-15124, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Anti-CD9 Monoclonal Antibody Activates p72 in Human Platelets

Yukio Ozaki , Kaneo Satoh , Kenji Kuroda , Ruomei Qi , Yutaka Yatomi , Shigeru Yanagi , Kiyonao Sada , Hirohei Yamamura , Mutsumasa Yanabu , Shosaku Nomura , Shoji Kume

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`) fragments of NNKY 1-19 did not, suggesting that the stimulation of FcII 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 I (PGI). The activity of p72 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 p72-associated tyrosine kinase activity that peaked at 10 s and subsided to the original level 2 min after stimulation. Coinciding with this time course, p60 transiently associated with p72. In platelets preexposed to GRGDS peptides or PGI, NNKY 1-19 also increased the p72-associated tyrosine kinase activity and led to the association of p60 with p72. However, in contrast to the control without any inhibitor, the elevated tyrosine kinase activity and the associated state of the two tyrosine kinases persisted as long as 5 min after stimulation. F(ab`) fragments of NNKY 1-19 induced changes similar to those observed with the effects of GRGDS peptides or PGI treatment on intact IgG NNKY 1-19 stimulation. F(ab`) fragments of another CD9 MoAb, PMA2, had effects on p72essentially similar to those of NNKY 1-19. These findings suggest that the binding of anti-CD9 MoAb to CD9 on the platelet membrane per se induces an increase in the p72-associated tyrosine kinase activity but that FcII receptor-mediated signal(s) is required for the full activation of platelets and the appearance of tyrosine-phosphorylated proteins. The elevated intracellular cAMP level induced by PGI acts at a step distal to the activation of p72 and inhibited the signal transduction pathway leading to protein tyrosine phosphorylation and aggregation. p72activation occurs in the absence of aggregation, but aggregation appears to reduce the elevated p72 activity induced by anti-CD9 MoAb.

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