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AMP-activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?

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Authors:
  • Jensen, Thomas Elbenhardt ;
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    Orcid logo0000-0001-6139-8268
    Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Wojtaszewski, Jørgen ;
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    Orcid logo0000-0001-8185-3408
    Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Richter, Erik
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    Orcid logo0000-0002-6850-3056
    Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
DOI:
10.1111/j.1748-1716.2009.01979.x
Abstract:
In skeletal muscle, the contraction-activated heterotrimeric 5'-AMP-activated protein kinase (AMPK) protein is proposed to regulate the balance between anabolic and catabolic processes by increasing substrate uptake and turnover in addition to regulating the transcription of proteins involved in mitochondrial biogenesis and other aspects of promoting an oxidative muscle phenotype. Here, the current knowledge on the expression of AMPK subunits in human quadriceps muscle and evidence from rodent studies suggesting distinct AMPK subunit expression pattern in different muscle types is reviewed. Then, the intensity and time dependence of AMPK activation in human quadriceps and rodent muscle are evaluated. Subsequently, a major part of this review critically examines the evidence supporting a necessary and/or sufficient role of AMPK in a broad spectrum of skeletal muscle contraction-relevant processes. These include glucose uptake, glycogen synthesis, post-exercise insulin sensitivity, fatty acid (FA) uptake, intramuscular triacylglyceride hydrolysis, FA oxidation, suppression of protein synthesis, proteolysis, autophagy and transcriptional regulation of genes relevant to promoting an oxidative phenotype.
Type:
Journal review article
Language:
English
Published in:
Acta Physiologica (print Edition), 2009, Vol 196, Issue 1, p. 155-174
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2009
Scientific Level:
Scientific
ID:
18945453

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