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Copenhagen Muscle Research Centre, Department of Human Physiology, Institute of Exercise and Sports Sciences, University of Copenhagen, Copenhagen 2100, Denmark
After a single
bout of exercise, insulin action is increased in the muscles that were
active during exercise. The increased insulin action has been shown to
involve glucose transport, glycogen synthesis, and glycogen synthase
(GS) activation as well as amino acid transport. A major mechanism
involved in increased insulin stimulation of glucose uptake after
exercise seems to be the exercise-associated decrease in muscle
glycogen content. Muscle glycogen content also plays a pivotal role for
the activity of GS and for the ability of insulin to increase GS
activity. Insulin signaling in human skeletal muscle is activated by
physiological insulin concentrations, but the increase in insulin
action after exercise does not seem to be related to increased
insulin signaling [insulin receptor tyrosine kinase activity,
insulin receptor substrate-1 (IRS-1) tyrosine phosphorylation (RS1),
IRS-1-associated phosphatidylinositol 3-kinase activity, Akt
phosphorylation (Ser473), glycogen synthase kinase 3 (GSK3)
phosphorylation (Ser21), and GSK3
activity], as
measured in muscle lysates. Furthermore, insulin signaling is also
largely unaffected by exercise itself. This, however, does not preclude
that exercise influences insulin signaling through changes in the
spatial arrangement of the signaling compounds or by affecting
unidentified signaling intermediates. Finally, 5'-AMP-activated protein
kinase has recently entered the stage as a promising player in
explaining at least a part of the mechanism by which exercise enhances
insulin action.
glycogen synthase; muscle glucose transport; insulin sensitivity; glycogen
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