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Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110
Evidence has accumulated that activation
of AMP kinase (AMPK) mediates the acute increase in glucose transport
induced by exercise. As the exercise-induced, insulin-independent
increase in glucose transport wears off, it is followed by an increase in muscle insulin sensitivity. The major purpose of this study was to
determine whether hypoxia and
5-aminoimidazole-4-carboxamide-1-
-D-ribofuranoside (AICAR), which also activate AMPK and stimulate glucose transport, also
induce an increase in insulin sensitivity. We found that the increase
in glucose transport in response to 30 µU/ml insulin was about
twofold greater in rat epitrochlearis muscles that had been made
hypoxic or treated with AICAR 3.5 h previously than in untreated
control muscles. This increase in insulin sensitivity was similar to
that induced by a 2-h bout of swimming or 10 min of in vitro
electrically stimulated contractions. Neither phosphatidylinositol 3-kinase activity nor protein kinase B (PKB) phosphorylation in response to 30 µU/ml insulin was enhanced by prior exercise or AICAR
treatment that increased insulin sensitivity of glucose transport.
Inhibition of protein synthesis by inclusion of cycloheximide in the
incubation medium for 3.5 h after exercise did not prevent the
increase in insulin sensitivity. Contractions, hypoxia, and treatment
with AICAR all caused a two- to three-fold increase in AMPK activity
over the resting level. These results provide evidence that the
increase in insulin sensitivity of muscle glucose transport that
follows exercise is mediated by activation of AMPK and involves a step
beyond PKB in the pathway by which insulin stimulates glucose transport.
cycloheximide; exercise; hypoxia; insulin signaling; 5-aminoimidazole-4-carboxamide-1--D-ribofuranoside
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