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Am J Physiol Endocrinol Metab 280: E677-E684, 2001;
0193-1849/01 $5.00
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Vol. 280, Issue 5, E677-E684, May 2001

AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle

Nicolas Musi1,*, Tatsuya Hayashi1,*, Nobuharu Fujii1, Michael F. Hirshman1, Lee A. Witters2, and Laurie J. Goodyear1

1 Research Division, Joslin Diabetes Center and Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02215; and 2 Endocrine-Metabolism Division, Department of Medicine and Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 02755

The AMP-activated protein kinase (AMPK) has been hypothesized to mediate contraction and 5-aminoimidazole-4-carboxamide 1-beta -D-ribonucleoside (AICAR)-induced increases in glucose uptake in skeletal muscle. The purpose of the current study was to determine whether treadmill exercise and isolated muscle contractions in rat skeletal muscle increase the activity of the AMPKalpha 1 and AMPKalpha 2 catalytic subunits in a dose-dependent manner and to evaluate the effects of the putative AMPK inhibitors adenine 9-beta -D-arabinofuranoside (ara-A), 8-bromo-AMP, and iodotubercidin on AMPK activity and 3-O-methyl-D-glucose (3-MG) uptake. There were dose-dependent increases in AMPKalpha 2 activity and 3-MG uptake in rat epitrochlearis muscles with treadmill running exercise but no effect of exercise on AMPKalpha 1 activity. Tetanic contractions of isolated epitrochlearis muscles in vitro significantly increased the activity of both AMPK isoforms in a dose-dependent manner and at a similar rate compared with increases in 3-MG uptake. In isolated muscles, the putative AMPK inhibitors ara-A, 8-bromo-AMP, and iodotubercidin fully inhibited AICAR-stimulated AMPKalpha 2 activity and 3-MG uptake but had little effect on AMPKalpha 1 activity. In contrast, these compounds had absent or minimal effects on contraction-stimulated AMPKalpha 1 and -alpha 2 activity and 3-MG uptake. Although the AMPKalpha 1 and -alpha 2 isoforms are activated during tetanic muscle contractions in vitro, in fast-glycolytic fibers, the activation of AMPKalpha 2-containing complexes may be more important in regulating exercise-mediated skeletal muscle metabolism in vivo. Development of new compounds will be required to study contraction regulation of AMPK by pharmacological inhibition.

adenosine 5'-monophosphate-activated protein kinase; contraction

* N. Musi and T. Hayashi contributed equally to this study.




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