Skeletal muscle protein metabolism in the elderly: Interventions to counteract the 'anabolic resistance' of ageing - PubMed (original) (raw)
Skeletal muscle protein metabolism in the elderly: Interventions to counteract the 'anabolic resistance' of ageing
Leigh Breen et al. Nutr Metab (Lond). 2011.
Abstract
Age-related muscle wasting (sarcopenia) is accompanied by a loss of strength which can compromise the functional abilities of the elderly. Muscle proteins are in a dynamic equilibrium between their respective rates of synthesis and breakdown. It has been suggested that age-related sarcopenia is due to: i) elevated basal-fasted rates of muscle protein breakdown, ii) a reduction in basal muscle protein synthesis (MPS), or iii) a combination of the two factors. However, basal rates of muscle protein synthesis and breakdown are unchanged with advancing healthy age. Instead, it appears that the muscles of the elderly are resistant to normally robust anabolic stimuli such as amino acids and resistance exercise. Ageing muscle is less sensitive to lower doses of amino acids than the young and may require higher quantities of protein to acutely stimulate equivalent muscle protein synthesis above rest and accrue muscle proteins. With regard to dietary protein recommendations, emerging evidence suggests that the elderly may need to distribute protein intake evenly throughout the day, so as to promote an optimal per meal stimulation of MPS. The branched-chain amino acid leucine is thought to play a central role in mediating mRNA translation for MPS, and the elderly should ensure sufficient leucine is provided with dietary protein intake. With regards to physical activity, lower, than previously realized, intensity high-volume resistance exercise can stimulate a robust muscle protein synthetic response similar to traditional high-intensity low volume training, which may be beneficial for older adults. Resistance exercise combined with amino acid ingestion elicits the greatest anabolic response and may assist elderly in producing a 'youthful' muscle protein synthetic response provided sufficient protein is ingested following exercise.
Figures
Figure 1
Schematic representation of muscle protein metabolism in response to anabolic stimuli (exercise and/or amino acid ingestion) in young and elderly. We hypothesize the primary reason for muscle loss in the healthy older adults is the inability of elderly muscles to mount a robust 'youthful' protein synthetic response to anabolic stimuli above that seen in the basal-state. Shaded section indicates the difference in MPS between elderly and young in response to anabolic stimuli.
Figure 2
Dose response curve of MPS in elderly and young muscle with protein ingestion at rest. MPS in the young is stimulated above basal with ~2.5 g of crystalline EAA (found in ~5 g of intact protein) before reaching a plateau at ~10 g of crystalline EAA (found in ~20 g of intact protein). In the elderly, MPS is increased above rest after ingestion of 20 g of whey protein and, like younger adults, the response plateaus thereafter. Star indicates MPS in both young and elderly after 6.7 g of EAA (typically found in 15 g of whey protein) enriched with leucine (41% or ~2.8 g) [36]. Finely dashed lines indicate the hypothesized leucine 'threshold' which must be surpassed in order to stimulate a robust increase in rates of MPS. The threshold may be considerably lower in the young (<1 g leucine in 2.5 g of crystalline EAA's) compared with the elderly (~1.5-2 g of leucine contained in 15-20 g of whey protein).
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