CD162和CD62P交联对血小板ERK1/2磷酸化的影响

The interaction of CD162 and CD62P affects the phosphorylation of ERK1/2 of platelet

目的:测定ERK1/ERK2与CD162和CD62P交联时的关系,有助于了解P-选择素在白细胞与血小板粘附、血栓形成时信号转导通路。方法:将新鲜分离的血小板加入重组CD162-hIgFc融合蛋白交联,通过细胞裂解和免疫沉淀进行ERK1/ERK2磷酸化分析。结果:ERK1的磷酸化时间大概从5min开始,10min时磷酸化程度最高,然后降低;而ERK2的磷酸化时间大概从5min开始程度最高,然后降低。结论:重组CD162-hIgFc融合蛋白,与血小板上的P-选择素互相交联可导致ERK系统的激活,从而有可能诱导某些应激性蛋白的快速表达。提示可以使用ERK的特异性抗体,来拮抗白细胞与血小板的粘附、血小板的聚集以及血栓形成有一定的临床意义,

Objective To determine the change of ERK1/ERK2 after the bond of CD162and CD62P, for the purpose of understanding the signal pathway of the leukocyte and platelet adhension and thrombosis. Methods Recombinant CD162-hlgFc fusion protein was added to freshly isolated blood platelet, and the phophorylation of ERK1/ERK2 was analyzed by means of cell lysis and immunoprecipitation. Results The phosphorylation of ERK1 started from 5 minutes, and reached the peak at 10 minutes, then went down. Conclusion Recombinant CD162-hlgFc fusion protein bonded to P-selectin on the blood platelet, activated ERK signal pathway, induced some downstream stress protein expression. Blocking the ERK pathway by specific antibody could possibly block the leukocyte and platelet adhension and thrombosis.