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Articles in PresS, published online ahead of print December 17, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00436.2002
Submitted on October 7, 2002
Accepted on December 5, 2002
1 Copenhagen Muscle Research Centre, Department of Human Physiology, Institute of Exercise and Sports Sciences, Copenhagen, Denmark
2 Division of Molecular Physiology, School of Life Science, Dunde, Scotland, United Kingdom
3 St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia
* To whom correspondence should be addressed. E-mail: Jwojtaszewski{at}aki.ku.dk.
The metabolic role of 5'AMP-activated protein kinase (AMPK) in regulation of skeletal muscle metabolism in man is unresolved. We measured isoform-specific AMPK activity and 
-acetyl-CoA carboxylase (ACC) Ser221 phosphorylation and substrate balance in skeletal muscle of eight athletes at rest, during cycling exercise for 1 hour at 70% VO2peak and 1 hour into recovery. The experiment was performed twice; once in a glycogen-loaded (glycogen concentration ~900 mmol kg d.w.-1) and once in a glycogen-depleted (glycogen concentration ~160 mmol kg d.w.-1) state. At rest, plasma long chain fatty acids (FA) were twofold higher in the glycogen depleted than in the loaded state and muscle 
1AMPK (160%), 2 AMPK (145%) activities and ACC Ser221 phosphorylation (137%) were also significantly higher in the glycogen depleted state. During exercise 2 AMPK activity, ACC Ser221 phosphorylation, plasma catecholamines and leg glucose and net fatty acid uptake were significantly higher in the glycogen-depleted than the glycogen-loaded state without apparent differences in muscle high energy phosphates. Thus, exercise in the glycogen depleted state elicits an enhanced uptake of circulating fuels which might be associated with elevated muscle AMPK activation. It is concluded that muscle AMPK activity and ACC Ser221 phosphorylation at rest and during exercise are sensitive to the fuel status of the muscle. During exercise this dependency may in part be mediated by humoral factors.
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