Feeding stimulates robust increases in muscle protein synthesis (MPS); however, ageing may alter the anabolic response to protein ingestion and the subsequent aminoacidaemia. With this as background, we aimed to determine in the present study the dose -response of MPS with the ingestion of isolated whey protein, with and without prior resistance exercise, in the elderly. For the purpose of this study, thirty-seven elderly men (age 71 (SD 4) years) completed a bout of unilateral leg-based resistance exercise before ingesting 0, 10, 20 or 40 g of whey protein isolate (W0 -W40, respectively). Infusion of L-[1-13 C]leucine and L-[ring-13 C 6 ]phenylalanine with bilateral vastus lateralis muscle biopsies were used to ascertain whole-body leucine oxidation and 4 h post-protein consumption of MPS in the fed-state of non-exercised and exercised leg muscles. It was determined that whole-body leucine oxidation increased in a stepwise, dose-dependent manner. MPS increased above basal, fasting values by approximately 65 and 90 % for W20 and W40, respectively (P,0·05), but not with lower doses of whey. While resistance exercise was generally effective at stimulating MPS, W20 and W40 ingestion post-exercise increased MPS above W0 and W10 exercised values (P,0·05) and W40 was greater than W20 (P, 0·05). Based on the study, the following conclusions were drawn. At rest, the optimal whey protein dose for non-frail older adults to consume, to increase myofibrillar MPS above fasting rates, was 20 g. Resistance exercise increases MPS in the elderly at all protein doses, but to a greater extent with 40 g of whey ingestion. These data suggest that, in contrast to younger adults, in whom post-exercise rates of MPS are saturated with 20 g of protein, exercised muscles of older adults respond to higher protein doses.

Non-technical summary A single bout of resistance exercise stimulates the synthesis of new muscle proteins. Chronic performance of resistance exercise (i.e. weight training) is what makes your muscles grow bigger; a process known as hypertrophy. However, it is unknown if increasing the time that muscle is under tension will lead to greater increases in muscle protein synthesis. We report that leg extension exercise at 30% of the best effort (which is a load that is comparatively light), with a slow lifting movement (6 s up and 6 s down) performed to fatigue produces greater increases in rates of muscle protein synthesis than the same movement performed rapidly (1 s up and 1 s down). These results suggest that the time the muscle is under tension during exercise may be important in optimizing muscle growth; this understanding enables us to better prescribe exercise to those wishing to build bigger muscles and/or to prevent muscle loss that occurs with ageing or disease.Abstract We aimed to determine if the time that muscle is under loaded tension during low intensity resistance exercise affects the synthesis of specific muscle protein fractions or phosphorylation of anabolic signalling proteins. Eight men (24 ± 1 years (SEM), BMI = 26.5 ± 1.0 kg m −2 ) performed three sets of unilateral knee extension exercise at 30% of one-repetition maximum strength involving concentric and eccentric actions that were 6 s in duration to failure (SLOW) or a work-matched bout that consisted of concentric and eccentric actions that were 1 s in duration (CTL). Participants ingested 20 g of whey protein immediately after exercise and again at 24 h recovery. Needle biopsies (vastus lateralis) were obtained while fasted at rest and after 6, 24 and 30 h post-exercise in the fed-state following a primed, constant infusion of L-[ring -13 C 6 ]phenylalanine. Myofibrillar protein synthetic rate was higher in the SLOW condition versus CTL after 24-30 h recovery (P < 0.001) and correlated to p70S6K phosphorylation (r = 0.42, P = 0.02). Exercise-induced rates of mitochondrial and sarcoplasmic protein synthesis were elevated by 114% and 77%, respectively, above rest at 0-6 h post-exercise only in the SLOW condition (both P < 0.05). Mitochondrial protein synthesis rates were elevated above rest during 24-30 h recovery in the SLOW (175%) and CTL (126%) conditions (both P < 0.05). Lastly, muscle PGC-1α expression was increased at 6 h post-exercise compared to rest with no difference between conditions (main effect for time, P < 0.001). These data show that greater muscle time under tension increased the acute amplitude of mitochondrial and sarcoplasmic protein synthesis and also resulted in a robust, but delayed stimulation of myofibrillar protein synthesis 24-30 h after resistance exercise.

A low-protein (6.25 g) mixed macronutrient beverage can be as effective as a high-protein dose (25 g) at stimulating increased MPS rates when supplemented with a high (5.0 g total leucine) amount of leucine. These results have important implications for formulations of protein beverages designed to enhance muscle anabolism. This trial was registered at clinicaltrials.gov as NCT 1530646.

Omega‐3 (n‐3) fatty acid supplementation enhances muscle protein synthesis and muscle size. Whether n‐3 fatty acid supplementation attenuates human muscle disuse atrophy is unknown. We determined the influence of n‐3 fatty acid supplementation on muscle size, mass, and integrated rates of myofibrillar protein synthesis (MyoPS) following 2 wk of muscle disuse and recovery in women. Twenty women (BMI = 23.0 ± 2.3 kg/m2, age = 22 ± 3 yr) underwent 2 wk of unilateral limb immobilization followed by 2 wk of return to normal activity. Starting 4 wk prior to immobilization, participants consumed either 5 g/d of n‐3 fatty acid or an isoenergetic quantity of sunflower oil (control). Muscle size and mass were measured pre‐ and postimmobilization, and after recovery. Serial muscle biopsies were obtained to measure integrated (daily) MyoPS. Following immobilization, the decline in muscle volume was greater in the control group compared to the n‐3 fatty acid group (14 vs. 8%, P < 0.05) and was not different from preimmobilization at recovery in the n‐3 fatty acid group; however, it was still lower in the control group (P < 0.05). Muscle mass was reduced in the control group only (P < 0.05). MyoPS was higher in the n‐3 group compared with the control group at all times (P < 0.05). We conclude that n‐3 fatty acid supplementation attenuates skeletal muscle disuse atrophy in young women, which may be mediated by higher rates of MyoPS.—McGlory, C., Gorissen, S. H. M., Kamal, M., Bahniwal, R., Hector, A. J., Baker, S. K., Chabowski, A., Phillips, S. M. Omega‐3 fatty acid supplementation attenuates skeletal muscle disuse atrophy during two weeks of unilateral leg immobilization in healthy young women. FASEB J. 33, 4586–4597 (2019). http://www.fasebj.org

Aging impairs the sensitivity of skeletal muscle to anabolic stimuli, such as amino acids and resistance exercise. Beef is a nutrient-rich source of dietary protein capable of stimulating muscle protein synthesis (MPS) rates in older men at rest. To date, the dose-response of myofibrillar protein synthesis to graded ingestion of protein-rich foods, such as beef, has not been determined. We aimed to determine the dose-response of MPS with and without resistance exercise to graded doses of beef ingestion. Thirty-five middle-aged men (59 ± 2 years) ingested 0 g, 57 g (2 oz; 12 g protein), 113 g (4 oz; 24 g protein), or 170 g (6 oz; 36 g protein) of (15% fat) ground beef (n = 7 per group). Subjects performed a bout of unilateral resistance exercise to allow measurement of the fed state and the fed plus resistance exercise state within each dose. A primed constant infusion of l-[1-(13)C]leucine was initiated to measure leucine oxidation and of l-[ring-(13)C(6)]phenylalanine was initiated to measure myofibrillar MPS. Myofibrillar MPS was increased with ingestion of 170 g of beef to a greater extent than all other doses at rest and after resistance exercise. There was more leucine oxidation with ingestion of 113 g of beef than with 0 g and 57 g, and it increased further after ingestion of 170 g of beef (all p < 0.05). Ingestion of 170 g of beef protein is required to stimulate a rise in myofibrillar MPS over and above that seen with lower doses. An isolated bout of resistance exercise was potent in stimulating myofibrillar MPS, and acted additively with feeding.

There exists a large body of scientific evidence to support protein intakes in excess of the recommended dietary allowance (RDA) (0.8 g protein/kg/day) to promote the retention of skeletal muscle and loss of adipose tissue during dietary energy restriction. Diet-induced weight loss with as low as possible ratio of skeletal muscle to fat mass loss is a situation we refer to as high-quality weight loss. We propose that high-quality weight loss is often of importance to elite athletes in order to maintain their muscle (engine) and shed unwanted fat mass, potentially improving athletic performance. Current recommendations for protein intakes during weight loss in athletes are set at 1.6-2.4 g protein/kg/day. However, the severity of the caloric deficit and type and intensity of training performed by the athlete will influence at what end of this range athletes choose to be. Other considerations regarding protein intake that may help elite athletes achieve weight loss goals include the quality of protein consumed, and the timing and distribution of protein intake throughout the day. This review highlights the scientific evidence used to support protein recommendations for high-quality weight loss and preservation of performance in athletes. Additionally, the current knowledge surrounding the use of protein supplements, branched chain amino acids (BCAA), β-hydroxy β-methylbutyrate (HMB), and other dietary supplements with weight loss claims will be discussed.

Skeletal muscle supports locomotion and serves as the largest site of postprandial glucose disposal; thus it is a critical organ for physical and metabolic health. Skeletal muscle mass is regulated by the processes of muscle protein synthesis (MPS) and muscle protein breakdown (MPB), both of which are sensitive to external loading and aminoacidemia. Hyperaminoacidemia results in a robust but transient increase in rates of MPS and a mild suppression of MPB. Resistance exercise potentiates the aminoacidemia-induced rise in MPS that, when repeated over time, results in gradual radial growth of skeletal muscle (i.e., hypertrophy). Factors that affect MPS include both quantity and composition of the amino acid source. Specifically, MPS is stimulated in a dose-responsive manner and the primary amino acid agonist of this process is leucine. MPB also appears to be regulated in part by protein intake, which can exert a suppressive effect on MPB. At high protein doses the suppression of MPB may interfere with skeletal muscle adaptation following resistance exercise. In this review, we examine recent advancements in our understanding of how protein ingestion impacts skeletal muscle growth following resistance exercise in young adults during energy balance and energy restriction. We also provide practical recommendations for exercisers who wish to maximize the hypertrophic response of skeletal muscle during resistance exercise training.

We conclude that whey protein supplementation attenuated the decline in postprandial rates of MPS after weight loss, which may be of importance in the preservation of lean mass during longer-term weight loss interventions. This trial was registered at clinicaltrials.gov as NCT01530646.