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Department of Zoology, Brigham Young University, Provo, Utah 84602
Received 9 December 1996; accepted in final form 16 May 1997.
Rasmussen, B. B., and W. W. Winder. Effect
of exercise intensity on skeletal muscle malonyl-CoA and acetyl-CoA
carboxylase. J. Appl. Physiol. 83(4):
1104-1109, 1997.
Malonyl-CoA is synthesized by acetyl-CoA
carboxylase (ACC) and is an inhibitor of fatty acid oxidation. Exercise
induces a decline in skeletal muscle malonyl-CoA, which is accompanied
by inactivation of ACC and increased activity of AMP-activated protein
kinase (AMPK). This study was designed to determine the effect of
exercise intensity on the enzyme kinetics of ACC, malonyl-CoA levels,
and AMPK activity in skeletal muscle. Male Sprague-Dawley rats were
killed (pentobarbital sodium anesthesia) at rest or after 5 min of
exercise (10, 20, 30, or 40 m/min at 5% grade). The fast-twitch red
and white regions of the quadriceps muscle were excised and frozen in
liquid nitrogen. A progressive decrease in red quadriceps ACC maximal
velocity (from 28.6 ± 1.5 to 14.3 ± 0.7 nmol · g
1 · min
1,
P < 0.05), an increase in activation
constant for citrate, and a decrease in malonyl-CoA (from 1.9 ± 0.2 to 0.9 ± 0.1 nmol/g, P < 0.05) were seen with the
increase in exercise intensity from rest to 40 m/min. AMPK activity
increased more than twofold. White quadriceps ACC activity decreased
only during intense exercise. We conclude that the extent of ACC
inactivation during short-term exercise is dependent on exercise
intensity.
fatty acid oxidation; quadriceps; adenosine
5
-monophosphate-activated protein; coenzyme A
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