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为探讨心肌细胞中Janus激酶1(JAK1)在C反应蛋白(CRP)诱导的基质金属蛋白酶(MMP)-10活性上调过程中的作用,本研究以炎症细胞因子CRP诱导MMP-10上调的原代乳鼠心肌细胞为研究对象,使用JAK1的特异磷酸化抗体,用Western印迹技术检查JAK1的磷酸化水平的激活情况.应用Western印迹技术和酶谱法分别检测胞外信号调节激酶(ERK)的磷酸化水平和MMP-10的活性变化.实验分为4组:对照组,CRP组,CRP+抑制剂组和抑制剂组.结果显示,磷酸化的JAK1在CRP刺激后1/12 h即可出现,在1 h达到高峰,而总的JAK1不改变;JAK1抑制剂piceatannol可以使磷酸化的ERK水平减弱,也可以使MMP-10的活性明显降低(P<0.01).研究结果提示,JAK1是通过激活ERK,从而上调MMP-10的活性,为心力衰竭提供了一个可能的治疗靶点.
In order to investigate the role of Janus kinase 1 (JAK1) in the up-regulation of C-reactive protein (MMP) -10 activity induced by c-reactive protein (CRP) in cardiomyocytes, The cardiomyocytes of neonatal rat were used as study object to test the activation of JAK1 phosphorylation by using JAK1 specific phosphorylation antibody.Western Blotting and zymography were used to detect the phosphorylation of extracellular signal-regulated kinase (ERK) Level and MMP-10 activity.The experiment was divided into 4 groups: control group, CRP group, CRP + inhibitor group and inhibitor group.The results showed that phosphorylation of JAK1 could occur at 1/12 h after CRP stimulation, Peaked at 1 h, while the total JAK1 did not change. JAK1 inhibitor piceatannol reduced the level of phosphorylated ERK and significantly decreased the activity of MMP-10 (P <0.01) .The results suggest that JAK1 is activated by activating ERK, thereby upregulating the activity of MMP-10, provides a potential therapeutic target for heart failure.