Journal article
AMPK-independent pathways regulate skeletal muscle fatty acid oxidation
N Dzamko, JD Schertzer, JG Ryall, R Steel, SL Macaulay, S Wee, ZP Chen, BJ Michell, JS Oakhill, MJ Watt, SB Jørgensen, GS Lynch, BE Kemp, GR Steinberg
Journal of Physiology | WILEY | Published : 2008
Abstract
The activation of AMP-activated protein kinase (AMPK) and phosphorylation/inhibition of acetyl-CoA carboxylase 2 (ACC2) is believed to be the principal pathway regulating fatty acid oxidation. However, during exercise AMPK activity and ACC Ser-221 phosphorylation does not always correlate with rates of fatty acid oxidation. To address this issue we have investigated the requirement for skeletal muscle AMPK in controlling aminoimidazole-4-carboxymide-1-β-D-ribofuranoside (AICAR) and contraction-stimulated fatty acid oxidation utilizing transgenic mice expressing a muscle-specific kinase dead (KD) AMPK α2. In wild-type (WT) mice, AICAR and contraction increased AMPK α2 and α1 activities, the p..
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Funding Acknowledgements
We thank Professor Morris Birnbaum for providing AMPK KD mice. These studies were supported by grants from the National Health and Medical Research Council (G. R. S., M. J. W., B. E. K., G. S. L.) and Diabetes Australia Research Trust (G. R. S.). N. D. was supported by a National Heart Foundation scholarship. S. B. J. was supported by a Danish Research Council of Health and Diseases postdoctoral fellowship. B. E. K. is an Australian Research Council Federation Fellow. S. W. is a Peter Doherty Fellow, M. J. W. is a R. Douglas Wright Fellow and G. R. S. a National Health and Medical Research Council Senior Research Fellow.