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1Sections of Cardiovascular Medicine, Endocrinology, and Metabolism, Department of Internal Medicine and 2Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510; and 3Faculty of Life Sciences, Division of Molecular Physiology, University of Dundee DD1 5EH, Scotland, United Kingdom
Submitted 16 April 2003 ; accepted in final form 15 May 2003
AMP-activated protein kinase (AMPK) is emerging as a key signaling pathway
that modulates cellular metabolic processes. In skeletal muscle, AMPK is
activated during exercise. Increased myocardial substrate metabolism during
exercise could be explained by AMPK activation. Although AMPK is known to be
activated during myocardial ischemia, it remains uncertain whether AMPK is
activated in response to the physiological increases in cardiac work
associated with exercise. Therefore, we evaluated cardiac AMPK activity in
rats at rest and after 10 min of treadmill running at moderate (15% grade, 16
m/min) or high (15% grade, 32 m/min) intensity. Total AMPK activity in the
heart increased in proportion to exercise intensity (P < 0.05).
AMPK activity associated with the 
2-catalytic subunit
increased 2.8 ± 0.4-fold (P < 0.02 vs. rest) and 4.5
± 0.6-fold (P < 0.001 vs. rest) with moderate- and
high-intensity exercise, respectively. AMPK activity associated with the
1-subunit increased to a lesser extent. Phosphorylation of
the Thr172-regulatory site on AMPK -catalytic subunits
increased during exercise (P < 0.001). There was no increase in
Akt phosphorylation during exercise. The changes in AMPK activity during
exercise were associated with physiological AMPK effects (GLUT4 translocation
to the sarcolemma and ACC phosphorylation). Thus cardiac AMPK activity
increases progressively with exercise intensity, supporting the hypothesis
that AMPK has a physiological role in the heart.
energy metabolism; signal transduction; glucose
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