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J Biol Chem, Vol. 274, Issue 35, 24896-24900, August 27, 1999
From the Research Division, Joslin Diabetes Center, and the
Department of Medicine, Brigham and Women's Hospital and Harvard
Medical School, Boston, Massachusetts 02215
Glycogen synthase activity is increased in
response to insulin and exercise in skeletal muscle. Part of the
mechanism by which insulin stimulates glycogen synthesis may involve
phosphorylation and activation of Akt, serine phosphorylation and
deactivation of glycogen synthase kinase-3 (GSK-3), leading to
dephosphorylation and activation of glycogen synthase. To study Akt and
GSK-3 regulation in muscle, time course experiments on the effects of
insulin injection and treadmill running exercise were performed in
hindlimb skeletal muscle from male rats. Both insulin and exercise
increased glycogen synthase activity (%I-form) by 2-3-fold over
basal. Insulin stimulation significantly increased Akt phosphorylation
and activity, whereas exercise had no effect. The time course of the
insulin-stimulated increase in Akt was closely matched by GSK-3
Insulin and Exercise Decrease Glycogen Synthase Kinase-3
Activity by Different Mechanisms in Rat Skeletal Muscle
Ser21 phosphorylation and a 40-60% decrease in
GSK-3 and GSK-3
activity. Exercise also deactivated GSK-3 and
activity by 40-60%. However, in contrast to the effects of
insulin, there was no change in Ser21 phosphorylation in
response to exercise. Tyrosine dephosphorylation of GSK-3, another
putative mechanism for GSK-3 deactivation, did not occur with insulin
or exercise. These data suggest the following: 1) GSK-3 is
constitutively active and tyrosine phosphorylated under basal
conditions in skeletal muscle, 2) both exercise and insulin are
effective regulators of GSK-3 activity in vivo, 3) the
insulin-induced deactivation of GSK-3 occurs in response to increased
Akt activity and GSK-3 serine phosphorylation, and 4) there is an
Akt-independent mechanism for deactivation of GSK-3 in skeletal muscle.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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