The impact of exercise and nutrition on the regulation of skeletal muscle mass. (1st August 2018)

• Record Type: Journal Article
• Authors: McGlory, Chris; van Vliet, Stephan; Stokes, Tanner; Mittendorfer, Bettina; Phillips, Stuart M.
• Is Part Of: Journal of physiology. Volume 597:Number 5(2019)
• Page Start: 1251
• Page End: 1258
• Publication Date: 2018-08-01
• Subjects: Food -- Supplement -- Omega‐3 -- Proteome -- Exercise; Physiology -- Periodicals; 612.005
• DOI: 10.1113/JP275443
• Languages: English
• ISSNs: 0022-3751

Abstract

Abstract: The maintenance of skeletal muscle mass and strength throughout life is a key determinant of human health and well‐being. There is a gradual loss of both skeletal muscle mass and strength with ageing (a process termed sarcopenia) that increases the risk of functional dependence, morbidity and mortality. Understanding the factors that regulate the size of human muscle mass, particularly during the later years of life, has therefore become an area of intense scientific inquiry. The amount of muscle mass is determined by coordinated changes in muscle protein synthesis (MPS) and muscle protein breakdown (MPB). In this review, we assess both classical and contemporary work that has examined how resistance exercise and nutrition impact on MPS and MPB. Special consideration is given to the role of different sources of dietary protein (food vs . supplements) and non‐protein nutrients such as omega‐3 fatty acids in regulating MPS. We also critically evaluate recent studies that have employed novel 'omic' technologies such as dynamic protein profiling to probe for changes in rates of MPS and MPB at the individual protein level following exercise. Finally, we provide suggestions for future research that we hope will yield important information for the development of exercise and nutritional strategies to counteract muscle loss in a variety of clinical settings. Abstract : Schematic illustration of the measurement of changes in the muscle proteome in response to nutritional intervention using labelled amino acid/deuterium and dynamic proteome profiling.