Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue.

Abstract:

: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)P3 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Cross DA,Watt PW,Shaw M,van der Kaay J,Downes CP,Holder JC,Cohen P

doi

10.1016/s0014-5793(97)00240-8

subject

Has Abstract

pub_date

1997-04-07 00:00:00

pages

211-5

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014579397002408

journal_volume

406

pub_type

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