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The platelet activation induced by two anti-human platelet P24/CD9 McAbs was investigated. The results showed that: the pathway of platelet aggregation induced by the two McAbs (HI117 and SJ9A4) is not the same; HI117 and SJ9A4 induced the phosphorylation of platelet proteins (40KD and 20KD) when platelets were activated; but HI117 didn't cause a rise in intracellular Ca2+ concentration in activated platelets compared with SJ9A4; the epitope recognized by HI117 and SJ9A4 is different and this is probably the real reason why the two CD9 McAbs play different roles in platelet activation. Additionally McAbs HI117 and SJ9A4 could not promote associates of other proteins (e.g.: GPIIb/IIIa) with P24/CD9 on activated human platelets. All these results indicate that the mechanism of platelet activation induced by HI117 or SJ9A4 is different form each other. It suggests that CD9 antigen play an important and complex role in platelet activation.
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