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Regulation of glycogen synthase activity and phosphorylation by exercise

Published online by Cambridge University Press:  05 March 2007

Jakob N. Nielsen  and
Jørgen F. P. Wojtaszewski
Jakob N. Nielsen
Affiliation:
Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, Copenhagen, Denmark
Jørgen F. P. Wojtaszewski*
Affiliation:
Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, Copenhagen, Denmark
*
*Corresponding author: Dr J. F. P. Wojtaszewski Fax: +45 35 32 16 00, Email: [email protected]
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Abstract

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Glycogen synthase (GS) catalyses the rate-limiting step of UDP-glucose incorporation into glycogen. Exercise is a potent regulator of GS activity, leading to activation of GS immediately after exercise promoting glycogen repletion by mechanisms independent of insulin. The incorporation of UDP-glucose is energy demanding, and during intense exercise GS is deactivated, diminishing energy utilization but also increasing the potential for glycogen breakdown. An apparent activation of GS is observed during moderate exercise, which could be considered as a potential waste of energy, although the cellular capacity for glycogen breakdown is considerably higher than that for glycogen synthesis. The understanding of this complex regulation of GS activity in response to exercise is just at its beginning. In the present review potential mechanisms by which exercise regulates GS activity are described, factors that may promote GS activation and factors that may deactivate GS are discussed, pointing to the view that GS activity during exercise is the result of the relative strength of these opposing factors.

Keywords

ExerciseContractionSkeletal muscleGlycogen synthasePhosphorylation
Type
Symposium 1: Exercise signalling pathways controlling fuel oxidation during and after exercise
Information
Proceedings of the Nutrition Society , Volume 63 , Issue 2 , May 2004 , pp. 233 - 237
Copyright
Copyright © The Nutrition Society 2004

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