How nutrition and exercise maintain the human musculoskeletal mass

In this article we review some of our recent work concerning the effects of nutrition and exercise on protein synthesis and signal transduction in human musculoskeletal tissues. A great deal of new information is being generated by the application of recently refined techniques for measuring protein turnover. The field remains one that is largely descriptive but increasingly we are beginning to discern mechanisms underlying lean tissue maintenance, growth and wasting especially as multidisciplinary tools are applied to its study. Several types of exercise and nutrition are potent stimuli for protein synthesis in skeletal muscle. By contrast, collagen in the extracellular matrix in muscle and tendon appears to be mechanically but not nutritionally sensitive. The rates of collagen turnover in a variety of tissues are sufficiently high to account for a sizeable proportion of whole body protein turnover. One of the most recent surprises is the high turnover rate of human bone collagen and its anabolic response to feeding. As our understanding of the normal physiology of these processes advances, we become better able to construct testable hypotheses concerning the effects of ageing and disease on the musculoskeletal mass. Current evidence suggests that one of the major problems with loss of muscle during ageing is an inability of the tissue to respond adequately to increased availability of nutrients

Changes in body composition in triathletes during an Ironman race

PURPOSE: Triathletes lose body mass during an Ironman triathlon. However, the associated body composition changes remain enigmatic. Thus, the purpose of this study was to investigate Ironman-induced changes in segmental body composition, using for the first time dual-energy X-ray absorptiometry (DXA) and peripheral quantitative computed tomography (pQCT). METHODS: Before and after an Ironman triathlon, segmental body composition and lower leg tissue mass, areas and densities were assessed using DXA and pQCT, respectively, in eight non-professional male triathletes. In addition, blood and urine samples were collected for the determination of hydration status. RESULTS: Body mass decreased by 1.9 ± 0.8 kg. This loss was due to 0.4 ± 0.3 and 1.4 ± 0.8 kg decrease in fat and lean mass, respectively (P < 0.01). Calf muscle density was reduced by 1.93 ± 1.04 % (P < 0.01). Hemoglobin, hematocrit, and plasma [K(+)] remained unchanged, while plasma [Na(+)] (P < 0.05), urine specific gravity and plasma and urine osmolality increased (P < 0.01). CONCLUSIONS: The loss in lean mass was explained by a decrease in muscle density, as an indicator of glycogen loss, and increases in several indicators for dehydration. The measurement of body composition with DXA and pQCT before and after an Ironman triathlon provided exact values for the loss in fat and lean mass. Consequently, these results yielded more detailed insights into tissue catabolism during ultra-endurance exercise

Effects of contraction and insulin on protein synthesis, AMP-activated protein kinase and phosphorylation state of translation factors in rat skeletal muscle.

In rat epitrochlearis skeletal muscle, contraction inhibited the basal and insulin-stimulated rates of protein synthesis by 75 and 70%, respectively, while increasing adenosine monophosphate-activated protein kinase (AMPK) activity. Insulin, on the other hand, stimulated protein synthesis (by 30%) and increased p70 ribosomal protein S6 kinase (p70S6K) Thr389, 40S ribosomal protein S6 (rpS6) Ser235/236, rpS6 Ser240/244 and eukaryotic initiation factor-4E-binding protein-1 (4E-BP1) Thr37/46 phosphorylation over basal values. Electrical stimulation had no effect on mammalian target of rapamycin complex 1 (mTORC1) signalling, as reflected by the lack of reduction in basal levels of p70S6K, rpS6 Ser235/236, rpS6 Ser240/244 and 4E-BP1 phosphorylation, but did antagonize mTORC1 signalling after stimulation of the pathway by insulin. Eukaryotic elongation factor-2 (eEF2) Thr56 phosphorylation increased rapidly on electrical stimulation reaching a maximum at 1 min, whereas AMPK Thr172 phosphorylation slowly increased to reach threefold after 30 min. Eukaryotic elongation factor-2 kinase (eEF2K) was not activated after 30 min of contraction when AMPK was activated. This could not be explained by the expression of a tissue-specific isoform of eEF2K in skeletal muscle lacking the Ser398 AMPK phosphorylation site. Therefore, in this skeletal muscle system, the contraction-induced inhibition of protein synthesis could not be attributed to a reduction in mTORC1 signalling but could be due to an increase in eEF2 phosphorylation independent of AMPK activation