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Am J Physiol Endocrinol Metab 279: E1202-E1206, 2000;
0193-1849/00 $5.00
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Vol. 279, Issue 5, E1202-E1206, November 2000

RAPID COMMUNICATION
AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation

Zhi-Ping Chen1,*, Glenn K. McConell2,*, Belinda J. Michell1, Rodney J. Snow3, Benedict J. Canny2, and Bruce E. Kemp1

1 St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Victoria 3065; 2 Department of Physiology, Monash University, Clayton, Victoria 3800; and 3 School of Health Sciences, Deakin University, Burwood, Victoria 3025, Australia

AMP-activated protein kinase (AMPK) is a metabolic stress-sensing protein kinase responsible for coordinating metabolism and energy demand. In rodents, exercise accelerates fatty acid metabolism, enhances glucose uptake, and stimulates nitric oxide (NO) production in skeletal muscle. AMPK phosphorylates and inhibits acetyl-coenzyme A (CoA) carboxylase (ACC) and enhances GLUT-4 translocation. It has been reported that human skeletal muscle malonyl-CoA levels do not change in response to exercise, suggesting that other mechanisms besides inhibition of ACC may be operating to accelerate fatty acid oxidation. Here, we show that a 30-s bicycle sprint exercise increases the activity of the human skeletal muscle AMPK-alpha 1 and -alpha 2 isoforms approximately two- to threefold and the phosphorylation of ACC at Ser79 (AMPK phosphorylation site) ~8.5-fold. Under these conditions, there is also an ~5.5-fold increase in phosphorylation of neuronal NO synthase-µ (nNOSµ) at Ser1451. These observations support the concept that inhibition of ACC is an important component in stimulating fatty acid oxidation in response to exercise and that there is coordinated regulation of nNOSµ to protect the muscle from ischemia/metabolic stress.

AMP-activated protein kinase; nitric oxide synthase; exercise

* Authors contributed equally to the study.




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