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目的 :探讨整合素α bβ3与血小板信号分子聚焦粘附激酶 PP12 5 F AK磷酸化的关系。方法 :采用免疫沉淀、SDS- PAGE和 Western blots等方法 ,观察在凝血酶刺激时 3种不同条件 (1正常人血小板 ;2用抗α bβ3单克隆抗体阻断正常血小板 ;3α bβ3缺陷的血小板无力症患者血小板 )下血小板 PP12 5 FAK磷酸化反应。结果 :正常人血小板 PP12 5 F AK发生磷酸化反应 ;α bβ3单抗阻断正常血小板其 PP12 5 FAK磷酸化明显减弱 ,但仍可见微弱磷酸化反应 ;血小板无力症患者血小板 PP12 5 F AK未见磷酸化反应。结论 :PP12 5 F AK磷酸化依赖于血小板活化和 α bβ3结构及功能的完整。整合素 α bβ3介导了血小板外 -内信号传导 ,α bβ3缺陷可影响这种信号传导 ,抗 α bβ3单抗不能完全阻断 PP12 5 F AK磷酸化
Objective: To investigate the relationship between integrin α bβ3 and platelet signaling molecule focal adhesion kinase (PP12 5 F AK) phosphorylation. Methods: Immunoprecipitation, SDS-PAGE and Western blots were used to observe the effects of thrombin on platelets stimulated by 3 different conditions (1 normal platelet; 2 anti-α bβ3 monoclonal antibody block normal platelets; 3α bβ3 deficient platelet weakness Symptoms of platelet) platelet PP12 5 FAK phosphorylation. Results: The phosphorylation of platelet PP12 5 F AK was detected in normal subjects. The phosphorylation of PP12 5 FAK in normal platelets blocked by α bβ3 monoclonal antibody was obviously weakened, but the faint phosphorylation was still observed. Platelet PP12 5 F AK Phosphorylation reaction. CONCLUSION: Phosphorylation of PP12 5 F AK is dependent on platelet activation and integrity of α bβ3 structure and function. Integrin α bβ3 mediates platelet-endo-signal transduction and α bβ3 deficiency can affect this signaling, whereas anti-α bβ3 mAb does not completely block PP12 5 F AK phosphorylation