Insulin activates protein kinase B, inhibits glycogen synthase kinase‐3 and activates glycogen synthase by rapamycin‐insensitive pathways in skeletal muscle and adipose tissue
Open Access
- 7 April 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 406 (1-2) , 211-215
- https://doi.org/10.1016/s0014-5793(97)00240-8
Abstract
Insulin stimulated protein kinase Bα (PKBα) 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)P3 PKBα 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 adipocytesKeywords
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