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Journal of Nutrition and Metabolism
Volume 2012, Article ID 136937, 10 pages
Review Article

Does Branched-Chain Amino Acids Supplementation Modulate Skeletal Muscle Remodeling through Inflammation Modulation? Possible Mechanisms of Action

1Laboratory of Applied Nutrition and Metabolism, School of Physical Education and Sports, University of São Paulo, P.O. Box 05508-030 São Paulo, SP, Brazil
2Laboratory of Molecular and Cellular Physiology of Exercise, School of Physical Education and Sports, University of São Paulo, P.O. Box 05508-030, São Paulo, SP, Brazil
3Department of Nutrition, School of Public Health, University of São Paulo, P.O. Box 01246-904, São Paulo, SP, Brazil

Received 27 July 2011; Revised 1 December 2011; Accepted 12 January 2012

Academic Editor: Stanley Omaye

Copyright © 2012 Humberto Nicastro et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Skeletal muscle protein turnover is modulated by intracellular signaling pathways involved in protein synthesis, degradation, and inflammation. The proinflammatory status of muscle cells, observed in pathological conditions such as cancer, aging, and sepsis, can directly modulate protein translation initiation and muscle proteolysis, contributing to negative protein turnover. In this context, branched-chain amino acids (BCAAs), especially leucine, have been described as a strong nutritional stimulus able to enhance protein translation initiation and attenuate proteolysis. Furthermore, under inflammatory conditions, BCAA can be transaminated to glutamate in order to increase glutamine synthesis, which is a substrate highly consumed by inflammatory cells such as macrophages. The present paper describes the role of inflammation on muscle remodeling and the possible metabolic and cellular effects of BCAA supplementation in the modulation of inflammatory status of skeletal muscle and the consequences on protein synthesis and degradation.