[Characterization of platelet activation induced by CD9 McAbs]

The platelet activation induced by two anti-human platelet P24/CD9 McAbs was investigated. The results showed that the pathways of platelet aggregation induced by the two McAbs (HI117 and SJ9A4) were different and HI117 and SJ9A4 induced the phosphorylation of platelet proteins (40,000 and 20,000) when platelets were activated. However, HI117 did not cause a rise in intracellular Ca2+ concentration in activated platelets in comparison with SJ9A4 and the epitope recognized by HI117 and SJ9A4 was different and this might explain why the two CD9 McAbs played different roles in platelet activation in addition, McAbs HI117 and SJ9A4 could not promote associations of other proteins (eg: GP II b/III a) with P24/CD9 on activated human platelets. All these results indicate that the mechanisms of platelet activation induced by HI117 or SJ9A4 are different from each other. It suggests that CD9 antigen plays an importent and complex role in platelet activation.