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1 The University of Nottingham
2 University of Nottingham
* To whom correspondence should be addressed. E-mail: michael.rennie{at}nottingham.ac.uk.
Skeletal muscle demonstrates extraordinary mutability in its responses to exercise of different modes, intensity and duration, which must involve alterations of muscle protein turnover, both acutely and chronically. Here we bring together information on the alterations in the rates of synthesis and degradation of human muscle protein by different types of exercise and the influences of nutrition, age and sexual dimorphism. Where possible we summarize the likely changes in activity of signalling proteins associated with control of protein turnover. Exercise of both the resistance and non-resistance types appears to depress muscle protein synthesis (MPS) and muscle protein breakdown (MPB) during exercise, whereas both are elevated after exercise in the fasted state, when net muscle protein balance remains negative. Positive net balance is achieved only when amino acid availability is increased, thereby raising MPS markedly. Such post-exercise increases in amino acids are less important for inhibiting MPB than insulin, the secretion of which is stimulated most by glucose availability, without itself stimulating MPS. Exercise training appears to increase basal muscle protein turnover, with differential responses of the myofibrillar and mitochondrial protein fractions to acute exercise in the trained state. Ageing reduces the responses of myofibrillar protein and anabolic signalling to resistance exercise. There appear to be few if any differences in the response of young women and young men to acute exercise, although there are indications that in older women the responses may be blunted more than in older men.
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