Defect in phosphorylation of insulin receptors in cells from an insulin-resistant patient with normal insulin binding.
Defect in phosphorylation of insulin receptors in cells from an insulin-resistant patient with normal insulin binding.
复制标题
胰岛素结合正常的胰岛素抵抗患者细胞中胰岛素受体磷酸化缺陷。
作者：
G. Grunberger;Y. Zick;P. Gorden
单核血细胞取自 A 型胰岛素抵抗患者。这些细胞表现出正常的结合碘125标记胰岛素的能力。对患者细胞中溶解的胰岛素受体的分析显示，胰岛素刺激的酪氨酸激酶活性存在缺陷，这与受体本身密切相关。该酶未能磷酸化胰岛素受体，并且磷酸化外源添加底物的能力显着降低。该胰岛素抵抗患者的受体似乎在胰岛素结合位点（受体的α亚基）远端存在缺陷。该缺陷可能位于具有三磷酸腺苷结合位点的β亚基中，或者位于将胰岛素结合信号转化为激酶活性的另一个受体成分中。胰岛素受体的正常结合和有缺陷的蛋白激酶成分之间的这种解离代表了配体结合远端受体的第一个生化缺陷。
Mononuclear blood cells were obtained from a patient with type A insulin resistance. The cells showed a normal ability to bind iodine 125-labeled insulin. Analysis of solubilized insulin receptors from the patient's cells revealed a defect in insulin-stimulated tyrosine kinase activity, which is closely associated with the receptor itself. The enzyme failed to phosphorylate the insulin receptor and showed a markedly reduced ability to phosphorylate exogenously added substrates. It appears that receptors from this insulin-resistant patient have a defect distal to the insulin-binding site (the alpha subunit of the receptor). The defect could be located in the beta subunit, which has an adenosine triphosphate-binding site, or in another receptor component that transfers a signal of insulin binding into kinase activity. This dissociation between the normal binding and the defective protein kinase component of the insulin receptor represents the first biochemical defect of the receptor distal to ligand binding.
胰岛素受体的β亚基是胰岛素激活的蛋白激酶。
影响因子：
2.9
作者：
Shia,MA;Pilch,PF
通讯作者：
Pilch,PF