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Department of Zoology, Brigham Young University, Provo, Utah 84602
Exercise induces a decline in liver
malonyl-CoA, an inhibitor of carnitine palmitoyltransferase-1. The
purpose of these experiments was to determine whether this decrease in
malonyl-CoA is accompanied by an activation of AMP-activated protein
kinase (AMPK) and inactivation of acetyl-CoA carboxylase (ACC). Rats
were killed at rest, after 10 min of running at 32 m/min up a 15%
grade or at 0, 15, or 60 min postexercise after 120 min of running at
16 m/min. There was no significant difference in AMPK and ACC
activities after 120 min of exercise, although a trend toward a
decrease in ACC and an increase in AMPK was noted 15 min postexercise.
After 10 min at 32 m/min, however, maximal ACC activity decreased from
487 ± 27 to 280 ± 39 nmol · g
1 · min1,
and the activation constant for citrate activation of ACC increased from 5.9 to 12.5 mM. AMPK activity increased from a resting value of
4.7 ± 0.4 to 9.8 ± 2.0 pmol · mg1 · min1
after exercise. These data provide indirect evidence of phosphorylation and inactivation of liver ACC during heavy exercise. In contrast, the
decrease in malonyl-CoA during long-term, low-intensity exercise may
occur by mechanisms other than phosphorylation of ACC.
carnitine palmitoyltransferase-1; malonyl-coenzyme A; postexercise ketosis; 3-hydroxybutyrate
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