A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle

Mol Cell. 2001 May;7(5):1085-94. doi: 10.1016/s1097-2765(01)00251-9.


Eukaryotic cells possess systems for sensing nutritional stress and inducing compensatory mechanisms that minimize the consumption of ATP while utilizing alternative energy sources. Such stress can also be imposed by increased energy needs, such as in skeletal muscle of exercising animals. In these studies, we consider the role of the metabolic sensor, AMP-activated protein kinase (AMPK), in the regulation of glucose transport in skeletal muscle. Expression in mouse muscle of a dominant inhibitory mutant of AMPK completely blocked the ability of hypoxia or AICAR to activate hexose uptake, while only partially reducing contraction-stimulated hexose uptake. These data indicate that AMPK transmits a portion of the signal by which muscle contraction increases glucose uptake, but other AMPK-independent pathways also contribute to the response.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • AMP-Activated Protein Kinases
  • Animals
  • Biological Transport, Active / drug effects
  • Biological Transport, Active / physiology
  • Enzyme Activation / drug effects
  • Glucose / metabolism
  • Hypoxia / metabolism
  • Hypoxia / physiopathology*
  • Male
  • Mice
  • Mice, Transgenic
  • Multienzyme Complexes / physiology*
  • Muscle Contraction / physiology*
  • Muscle, Skeletal / enzymology
  • Myocardium / enzymology
  • Phosphorylation / drug effects
  • Protein-Serine-Threonine Kinases / physiology*
  • Signal Transduction


  • Multienzyme Complexes
  • Protein-Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Glucose