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The -subunit of AMPK is essential for submaximal contraction-mediated glucose transport in skeletal muscle in vitro

Departments of ¹Anatomy and Physiology and ²Rehabilitation, and ³Lipid Research Unit, Laval University Hospital Research Center, Québec, Canada

Submitted 14 April 2008 ; accepted in final form 22 September 2008

AMP-activated protein kinase (AMPK) is a key signaling protein in the regulation of skeletal muscle glucose uptake, but its role in mediating contraction-induced glucose transport is still debated. The effect of contraction on glucose transport is impaired in EDL muscle of transgenic mice expressing a kinase-dead, dominant negative form of the AMPK₂ subunit (KD-AMPK₂ mice). However, maximal force production is reduced in this muscle, raising the possibility that the defect in glucose transport was due to a secondary decrease in force production and not impaired AMPK₂ activity. Generation of force-frequency curves revealed that muscle force production is matched between wild-type (WT) and KD-AMPK₂ mice at frequencies 50 Hz. Moreover, AMPK activation is already maximal at 50 Hz in muscles of WT mice. When EDL muscles from WT mice were stimulated at a frequency of 50 Hz for 2 min (200-ms train, 1/s, 30 volts), contraction caused an 3.5-fold activation of AMPK₂ activity and an 2-fold stimulation of glucose uptake. Conversely, whereas force production was similar in EDL of KD-AMPK₂ animals, no effect of contraction was observed on AMPK₂ activity, and glucose uptake stimulation was reduced by 50% (P < 0.01) As expected, 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate (AICAR) caused a 2.3-fold stimulation of AMPK₂ activity and a 1.7-fold increase in glucose uptake in EDL from WT mice, whereas no effect was detected in muscle from KD-AMPK₂ mice. These data demonstrate that AMPK activation is essential for both AICAR and submaximal contraction-induced glucose transport in skeletal muscle but that AMPK-independent mechanisms are also involved.

adenosine 5'-monophosphate-activated protein kinase

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