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J Biol Chem, Vol. 273, Issue 24, 14679-14682, June 12, 1998
From the Howard Hughes Medical Institute, Department of Medicine
and The Cox Institute, University of Pennsylvania School of Medicine,
Philadelphia, Pennsylvania 19104-6148
Insulin and muscle contraction
potently stimulate glucose uptake in mammalian skeletal muscle. Studies
in muscle and adipose tissue have shown that insulin induces its
receptor-dependent phosphorylation of insulin receptor
substrates 1 and 2, which leads to activation of
polyphosphatidylinositol (PI) 3'-kinase. In contrast, muscle
contraction stimulates glucose transport via a mechanism that is
independent of insulin, but the two pathways may converge downstream at
the level of stimulation of GLUT4 translocation. In the present study,
we have examined the role of Akt, an insulin-activated serine threonine
kinase that has previously been shown to increase glucose transport in
adipocytes. Either insulin or in vitro muscle contraction
significantly elevated glucose transport in isolated rat epitrochlearis
and soleus muscles. However, Akt kinase activity was significantly
stimulated by insulin and not contraction. Moreover, wortmannin, an
inhibitor of PI 3'-kinase, completely blocked the insulin-stimulated
increase in Akt activity and glucose transport but did not alter either
of these parameters in contracting muscles. The increases in Akt
activity were paralleled by a decrease in the electrophoretic mobility
of Akt, indicative of phosphorylation of Akt by an upstream kinase.
These changes in Akt mobility appeared to be at least partially because
of phosphorylation of Akt on serine 473. A putative downstream target
of Akt, p70 S6 kinase, showed similar changes in mobility in response
to insulin but not contraction. These data support the view that Akt is
a downstream target of PI 3'-kinase and is involved in the signaling
pathways involved in insulin but not contraction stimulation of glucose transport in skeletal muscle. These data provide further evidence that
two distinct pathways exist for the stimulation of glucose transport in
mammalian skeletal muscle.
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