窖蛋白对粘附斑激酶信号通路的影响

EFFECT OF CAVEOLIN-1 ON FOCAL ADHESION KINASE SIGNAL TRANSDUCTION PATHWAY

目的研究窖蛋白对粘附斑激酶活性的影响,探讨窖蛋白对粘附斑激酶信号通路的作用。方法采用体外培养第3代到第6代人脐静脉内皮细胞,以腺病毒介导其高表达窖蛋白,免疫印迹法检测粘附斑激酶活性,以抗粘附斑激酶397酪氨酸残基磷酸化抗体检测粘附斑激酶磷酸化水平。结果窖蛋白与粘附斑激酶形成免疫沉淀复合体,两者可以相互识别结合。与对照组相比,高表达窖蛋白抑制粘附斑激酶397酪氨酸残基磷酸化水平在纤粘连蛋白刺激前和刺激后分别降低了33%和35%。结论窖蛋白通过抑制粘附斑激酶的起始活性来抑制粘附斑激酶信号通路。

Objective To investigate the effect of caveolin - 1 on the pbesphorylation of focal adhesion kinase （FAK）. Methods The 3 rd - 6 th generation of human umbilical venous endothelial cells （HUVEC） by in vitro culture were used. Adenovirus mediated overexpression of caveolin- 1 protein in HUVEC was performed. The activity of FAK was assayed by Westem blot. The level of FAK phosphorylation was determined by the antibody of phosphorylated tyrosine 397 residual radical in FAK. Results The caveolin- 1 protein could form immunoprecipitation complex with FAK, and overexpression of caveolin - 1 decreased the FAK tyrosine 397 phosphorylation by 33 %, 35 % respectively before and after the stimulation by fibronectin. Conclusion Caveolin - 1 inhibits the integrin - FAK signal pathway by inhibiting the phosphorylation of FAK tyrosine 397.