Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue
Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue
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DOI：
10.1016/s0014-5793(97)00240-8
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发表时间：
1997-04-07
期刊：
影响因子：
3.5
通讯作者：
Cohen, P
中科院分区：
文献类型：
--
作者：
Cross, DAE;Watt, PW;Cohen, P
在骨骼肌和脂肪细胞中，胰岛素刺激蛋白激酶B α（PK B α）超过10倍，并使糖原合成酶激酶3（GSK 3）活性降低50+/-10%。雷帕霉素不能阻止PKB的激活，抑制GSK 3或刺激糖原合成酶长达5分钟。因此，雷帕霉素不敏感的途径介导胰岛素对主要胰岛素反应组织中糖原合成酶的急性作用，EGF对脂肪细胞中磷脂酰肌醇（3，4，5）P-3 PKB α和GSK 3的微小且非常短暂的作用，与胰岛素的强烈且持续的作用相比，这解释了为什么EGF不刺激脂肪细胞中的葡萄糖摄取或糖原合成。(C)1997年欧洲生物化学学会联合会。
Insulin stimulated protein kinase B alpha (PKB alpha) more than 10-fold and decreased glycogen synthase kinase-3 (GSK3) activity by 50+/-10% in skeletal muscle and adipocytes. Rapamycin did not prevent the activation of PKB, inhibition of GSK3 or stimulation of glycogen synthase up to 5 min. Thus rapamycin-insensitive pathways mediate the acute effect of insulin on glycogen synthase in the major insulin-responsive tissues, The small and very transient effects of EGF on phosphatidylinositol (3,4,5)P-3 PKB alpha and GSK3 in adipocytes, compared to the strong and sustained effects of insulin, explains why EGF does not stimulate glucose uptake or glycogen synthesis in adipocytes. (C) 1997 Federation of European Biochemical Societies.