IMR Press / FBL / Volume 13 / Issue 14 / DOI: 10.2741/3102

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
How is AMPK activity regulated in skeletal muscles during exercise?
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1 St. Vincent’s Institute of Medical Research and Department of Medicine, University of Melbourne, Melbourne, Australia
2 Molecular Physiology Group, Copenhagen Muscle Research Centre, Dept. of Exercise and Sport Sciences, Section of Human Physiology, University of Copenhagen, Denmark
Academic Editors:Bruce Kemp, Stuart Macaulay
Front. Biosci. (Landmark Ed) 2008, 13(14), 5589–5604; https://doi.org/10.2741/3102
Published: 1 May 2008
(This article belongs to the Special Issue AMP-activated protein kinase)
Abstract

AMPK is a metabolic "master" controller activated in skeletal muscle by exercise in a time and intensity dependent manner, and has been implicated in regulating metabolic pathways in muscle during physical exercise. AMPK signaling in skeletal muscle is regulated by several systemic and intracellular factors and the regulation of skeletal muscle AMPK in response to exercise is the focus of this review. Specifically, the role of LKB1 and phosphatase PP2C in nucleotide-dependent activation of AMPK, and ionized calcium in CaMKK-dependent activation of AMPK in working muscle is discussed. We also discuss the influence of reactive oxygen species produced within the muscle as well as muscle glycogen and TAK1 in regulating AMPK during exercise. Currently, during intensive contraction, activation of alpha2-AMPK seems mainly to rely on AMP accumulating from ATP-hydrolysis whereas calcium signaling may have some importance during more gentle contraction conditions. Factors that regulate alpha1-AMPK during exercise are less clear but it appears, at least to some extent, to rely on an adenine nucleotide-dependent mechanism.

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