A possible role for AMP-activated protein kinase in exercise-induced glucose utilization: insights from humans and transgenic animals. (1st February 2003)

• Record Type: Journal Article
• Authors: Nielsen, J.N.; Jørgensen, S.B.; Frøsig, C.; Viollet, B.; Andreelli, F.; Vaulont, S.; Kiens, B.; Richter, E.A.; Wojtaszewski, J.F.P.
• Is Part Of: Biochemical Society transactions. Volume 31:Number 1(2003)
• Page Start: 186
• Page End: 190
• Publication Date: 2003-02-01
• Subjects: acetyl-CoA carboxylase -- glycogen -- skeletal muscle; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0310186
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Exercise-induced glucose uptake in skeletal muscle is mediated by an insulin-independent mechanism, but the actual signals to glucose transport in response to muscle contraction have not been identified. The 5´-AMP-activated protein kinase (AMPK) has emerged as a putative mediator of contraction-induced glucose transport, although no conclusive evidence has been provided so far. Recent experiments in AMPK transgenic mice suggest that glucose transport induced by 5-amino-4-imidazolecarboxamide riboside (AICAR) or hypoxia is mediated by AMPK. In contrast, contraction-induced glucose transport in rodent skeletal muscle induced by electrical stimulation in vitro or in situ is not influenced or is only partially reduced by abolishing both or one of the catalytic AMPK subunits. This is compatible with exercise studies done in humans, where no tight correlation is found between AMPK activity and glucose uptake during exercise. Taken together, these results question an essential role of AMPK in exercise-induced glucose uptake and imply that one or more additional pathways are involved in mediating glucose transport in skeletal muscle during exercise.