Peng L, Li J Z, Wu H Z, Wang M J
Institute of hematology, Peking Union Medical College, Chinese Academy of Medical Science, Tianjin, China.
Thromb Res. 1997 Jul 1;87(1):65-73. doi: 10.1016/s0049-3848(97)00105-9.
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.
研究了两种抗人血小板P24/CD9单克隆抗体诱导的血小板活化。结果表明：两种单克隆抗体（HI117和SJ9A4）诱导血小板聚集的途径不同；HI117和SJ9A4在血小板活化时诱导血小板蛋白（40KD和20KD）磷酸化；但与SJ9A4相比，HI117不会导致活化血小板内Ca2+浓度升高；HI117和SJ9A4识别的表位不同，这可能是这两种CD9单克隆抗体在血小板活化中发挥不同作用的真正原因。此外，单克隆抗体HI117和SJ9A4不能促进活化人血小板上其他蛋白质（如：GPIIb/IIIa）与P24/CD9的结合。所有这些结果表明，HI117或SJ9A4诱导血小板活化的机制彼此不同。这表明CD9抗原在血小板活化中起重要而复杂的作用。
