Insulin-stimulated tyrosine phosphorylation of protein kinase C alpha: evidence for direct interaction of the insulin receptor and protein kinase C in cells.
Insulin-stimulated tyrosine phosphorylation of protein kinase C alpha: evidence for direct interaction of the insulin receptor and protein kinase C in cells.
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胰岛素刺激的蛋白激酶 C α 酪氨酸磷酸化：细胞中胰岛素受体和蛋白激酶 C 直接相互作用的证据。
DOI：
10.1006/bbrc.1994.1630
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发表时间：
1994
影响因子：
3.1
通讯作者：
Roth,RA
中科院分区：
文献类型：
--
作者：
Liu,F;Roth,RA
在过表达胰岛素受体和蛋白激酶Cα的中国仓鼠卵巢细胞中，用抗磷酸酪氨酸抗体进行免疫印迹，观察到在佛波醇酯存在下，胰岛素刺激主要80 kDa蛋白的酪氨酸磷酸化。蛋白质特异性免疫沉淀的抗体蛋白激酶C和抗磷酸酪氨酸抗体能够免疫沉淀蛋白激酶C酶活性从这些细胞。当用酪氨酸特异性磷酸酶处理该酪氨酸磷酸化蛋白激酶C时，观察到其酶活性降低35%，并且通过在反应混合物中加入酪氨酸磷酸酶抑制剂钒酸盐来阻断这种抑制。这些结果表明，在一定条件下，胰岛素可以刺激蛋白激酶C的酪氨酸磷酸化，这种磷酸化可以影响其酶活性。
Insulin, in the presence of phorbol esters, was observed to stimulate the tyrosine phosphorylation of a major 80 kDa protein by immunoblotting with anti-phosphotyrosine antibodies in Chinese hamster ovary cells overexpressing the insulin receptor and protein kinase Cα. The protein was specifically immunoprecipitated by antibodies to protein kinase C and anti-phosphotyrosine antibodies were capable of immunoprecipitating protein kinase C enzymatic activity from these cells. When this tyrosine phosphorylated protein kinase C was treated with a tyrosine-specific phosphatase, a 35% decrease in its enzymatic activity was observed and this inhibition was blocked by inclusion of a tyrosine phosphatase inhibitor, vanadate, in the reaction mixture. These results indicate that under certain conditions insulin can stimulate the tyrosine phosphorylation of protein kinase C and this phosphorylation can affect its enzymatic activity.