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1 Department of Internal Medicine, Yale University School of Medicine, New Haven, CT, USA
2 Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT, USA
3 Division of Molecular Physiology, Faculty of Life Sciences, University of Dundee, Dundee, United Kingdom
* To whom correspondence should be addressed. E-mail: lawrence.young{at}yale.edu.
AMP-activated protein kinase (AMPK) is emerging as a key signaling pathway which 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 physiologic increases in cardiac work associated with exercise. Therefore, we evaluated cardiac AMPK activity in rats at rest and following 10 minutes of treadmill running at moderate (15% grade, 16m/min) or high intensity (15% grade, 32m/min). 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 physiologic AMPK effects: GLUT4 glucose transporter translocation to the sarcolemma and acetyl-CoA carboxylase phosphorylation. Thus, cardiac AMPK activity increases progressively with exercise intensity, supporting the hypothesis that AMPK has a physiologic role in the heart.
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