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First published online April 26, 2005
Journal of Experimental Biology 208, 1601-1610 (2005)
Published by The Company of Biologists 2005
doi: 10.1242/jeb.01502
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Review article: Basal metabolic rate and cellular energetics

Control of muscle bioenergetic gene expression: implications for allometric scaling relationships of glycolytic and oxidative enzymes

Christopher D. Moyes* and Christophe M. R. LeMoine

Department of Biology, Queen's University, Kingston, Canada K7L 3N6

* Author for correspondence (e-mail: moyesc{at}biology.queensu.ca)

Accepted 18 January 2005

Summary

Muscle metabolic properties vary with body size, with larger animals relying relatively less on oxidative metabolism as a result of lower specific activities of mitochondrial enzymes and greater specific activities of glycolytic enzymes. While many have argued reasons why such relationships might be grounded in physical relationships, an explanation for the regulatory basis of the differences in enzyme levels remains unexplored. Focusing on skeletal muscle, we review potential cellular and genetic explanations for the relationship between bioenergetic enzymes and body mass. Differences in myonuclear domain (the ratio of fiber volume to nuclei number) in conjunction with constitutive expression may explain part of the variation in mitochondrial content among fiber types and species. Superimposed on such constitutive determinants are (1) extrinsic signalling pathways that control the muscle contractile and metabolic phenotype and (2) intrinsic signalling pathways that translate changes in cellular milieu (ions, metabolites, oxygen, redox) arising through the contractile phenotype into changes in enzyme synthesis. These signalling pathways work through transcriptional regulation, as well as post-transcriptional, translational and post-translational regulation, acting via synthesis and degradation.

Key words: allometry, scaling, metabolic rate, mitochondria, glycolysis, citrate synthase, cytochrome c oxidase, nuclear respiratory factor, peroxisome proliferator activated receptor, PGC-1


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