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首页> 外文期刊>Biochemistry >ACTIVATION OF CJUN NH2-TERMINAL KINASE/STRESS-ACTIVATED PROTEIN KINASE BY INSULIN
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ACTIVATION OF CJUN NH2-TERMINAL KINASE/STRESS-ACTIVATED PROTEIN KINASE BY INSULIN

机译：胰岛素激活CJUN NH2-末端激酶/应力激活的蛋白激酶

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摘要

One of insulin's many biological effects is the increased transcription of AP-1-regulated genes, cJun is the principal component of the AP-1 transcription complex, which is regulated by the newly discovered members of the MAPK superfamily referred to as cJun NH2-terminal kinases (JNKs) or stress-activated protein kinases (SAPKs). We show that insulin stimulates a dose- and time-dependent increase in JNK activity in Rat 1 fibroblasts overexpressing human insulin receptors (Rat 1 HIR cells). Using two different polyclonal anti-JNK antibodies, JNK activity was measured after immunoprecipitation from whole cell extracts by phosphorylation of GSTcJun(1-79). Peak activation occurred 15 min after insulin addition, resulting in a 2.5-fold increase in GSTcJun(1-79) phosphorylation over unstimulated controls. Maximal JNK activation correlated with the onset of AP-1 DNA binding activity. Both insulin-stimulated JNK activity and insulin-induced AP-1 transcriptional activity were found to be Ras-dependent. These data suggest that in Rat 1 cells, JNK activation may play a role in insulin-regulated AP-1 transcriptional activity leading to a mitogenic response.
机译：胰岛素的许多生物学作用之一是增加AP-1调控基因的转录，cJun是AP-1转录复合物的主要成分，该复合物受新发现的MAPK超家族成员cJun NH2-末端的调控。激酶（JNKs）或压力激活的蛋白激酶（SAPKs）。我们表明，胰岛素刺激大鼠1成纤维细胞过表达人胰岛素受体（大鼠1 HIR细胞）的JNK活性的剂量和时间依赖性增加。使用两种不同的多克隆抗JNK抗体，通过GSTcJun（1-79）的磷酸化从全细胞提取物中免疫沉淀后，测定JNK活性。胰岛素添加后15分钟出现峰值激活，导致GSTcJun（1-79）磷酸化水平比未刺激的对照组高2.5倍。最大的JNK激活与AP-1 DNA结合活性的开始有关。发现胰岛素刺激的JNK活性和胰岛素诱导的AP-1转录活性均是Ras依赖性的。这些数据表明，在大鼠1细胞中，JNK激活可能在胰岛素调节的AP-1转录活性中起作用，从而导致有丝分裂反应。

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