AMP-activated protein kinase (AMPK) is becoming recognized as a critical regulator of energy metabolism in cells. Using a mouse model in which we specifically blocked AMPK activity in muscles, we have demonstrated that activation of AMPK is necessary for the effects of 5-aminoimidazole-4-carboxamide riboside (‘AICAR’) and hypoxia, and is possibly required for a portion of exercise-induced glucose uptake. These same mice could not maintain sufficient glycogen in their skeletal muscle and it was rapidly depleted when the animals were subjected to mild exercise. Using isolated strips, we observed muscle hypertrophy and increased tiredness in the AMPK-deficient muscle. We also performed microarray analysis and showed dramatic changes of transcription profile in muscles of the lazy mice. These could have a significant impact on muscle function and may contribute to the observed phenotype.
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February 2003
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Conference Article|
February 01 2003
Selective suppression of AMP-activated protein kinase in skeletal muscle: update on ‘lazy mice’
J. Mu;
J. Mu
*Department of Medicine, Howard Hughes Medical Institute, University of Pennsylvania Medical School, Clinical Research Building, 415 Curie Boulevard, Philadelphia, PA 19104-6148, U.S.A.
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E.R. Barton;
E.R. Barton
†Department of Physiology, 3700 Hamilton Walk, University of Pennsylvania Medical School, Philadelphia, PA 19104-6085, U.S.A.
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M.J. Birnbaum
M.J. Birnbaum
1
*Department of Medicine, Howard Hughes Medical Institute, University of Pennsylvania Medical School, Clinical Research Building, 415 Curie Boulevard, Philadelphia, PA 19104-6148, U.S.A.
1To whom correspondence should be addressed (e-mail birnbaum@mail.med.upenn.edu).
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Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
Copyright 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (1): 236–241.
Citation
J. Mu, E.R. Barton, M.J. Birnbaum; Selective suppression of AMP-activated protein kinase in skeletal muscle: update on ‘lazy mice’. Biochem Soc Trans 1 February 2003; 31 (1): 236–241. doi: https://doi.org/10.1042/bst0310236
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