Protein supplementation after exercise and before sleep does not further augment skeletal muscle mass or strength gains during resistance exercise training in active older men. This study was registered at the Netherlands Trial Registry (www.trialregister.nl) as NTR5082.

Resistance-type exercise increases muscle protein synthesis rates during acute postexercise recovery. The impact of resistance-type exercise training on (local) muscle protein synthesis rates under free-living conditions on a day-to-day basis remains unclear. We determined the impact of daily unilateral resistance-type exercise on local myofibrillar protein synthesis rates during a 3-day period. Twelve healthy young men (22 ± 1 yr) were recruited to participate in this study where they performed daily, unilateral resistance-type exercise during a 3-day intervention period. Two days before the exercise training subjects ingested 400 ml deuterated water (HO). Additional 50-ml doses of deuterated water were ingested daily during the training period. Saliva and blood samples were collected daily to assess body water and amino acid precursor deuterium enrichments, respectively. Muscle tissue biopsies were collected before and after the 3 days of unilateral resistance-type exercise training from both the exercised and the nonexercised, control leg for the assessment of muscle protein synthesis rates. Deuterated water dosing resulted in a steady-state body water enrichment of 0.70 ± 0.03%. Intramuscular free [H]alanine enrichment increased up to 1.84 ± 0.06 mole percent excess (MPE) before the exercise training and did not change in both the exercised and control leg during the 3 subsequent exercise training days (2.11 ± 0.11 and 2.19 ± 0.12 MPE, respectively; P > 0.05). Muscle protein synthesis rates averaged 1.984 ± 0.118 and 1.642 ± 0.089%/day in the exercised vs. nonexercised, control leg when assessed over the entire 3-day period ( P < 0.05). Daily resistance-type exercise stimulates (local) muscle protein synthesis in vivo in humans. NEW & NOTEWORTHY This study demonstrates that daily resistance-type exercise stimulates muscle protein synthesis rates in vivo in humans over multiple days. Whereas acute studies have shown that resistance-type exercise increases muscle protein synthesis rates by 50-100%, we observed a lower impact of resistance-type exercise under free-living conditions. We also compared precursor tracer selection for the calculation of muscle protein synthesis rates and observed that saliva deuterium enrichment serves as an appropriate and practical choice of precursor.

BackgroundAge-related decline in skeletal muscle mass is at least partly attributed to anabolic resistance to food intake. Resistance exercise sensitizes skeletal muscle tissue to the anabolic properties of amino acids.ObjectiveThe present study assessed protein digestion and amino acid absorption kinetics, whole-body protein balance, and the myofibrillar protein synthetic response to ingestion of different amounts of protein during recovery from resistance exercise in older men.MethodsForty-eight healthy older men [mean ± SEM age: 66 ± 1 y; body mass index (kg/m2): 25.4 ± 0.3] were randomly assigned to ingest 0, 15, 30, or 45 g milk protein concentrate after a single bout of resistance exercise consisting of 4 sets of 10 repetitions of leg press and leg extension and 2 sets of 10 repetitions of lateral pulldown and chest press performed at 75–80% 1-repetition maximum. Postprandial protein digestion and amino acid absorption kinetics, whole-body protein metabolism, and myofibrillar protein synthesis rates were assessed using primed, continuous infusions of l-[ring-2H5]-phenylalanine, l-[ring-2H2]-tyrosine, and l-[1-13C]-leucine combined with ingestion of intrinsically l-[1-13C]-phenylalanine and l-[1-13C]-leucine labeled protein.ResultsWhole-body net protein balance showed a dose-dependent increase after ingestion of 0, 15, 30, or 45 g of protein (0.015 ± 0.002, 0.108 ± 0.004, 0.162 ± 0.008, and 0.215 ± 0.009 μmol Phe · kg−1 · min−1, respectively; P < 0.001). Myofibrillar protein synthesis rates were higher after ingesting 30 (0.0951% ± 0.0062%/h, P = 0.07) or 45 g of protein (0.0970% ± 0.0062%/h, P < 0.05) than after 0 g (0.0746% ± 0.0051%/h). Incorporation of dietary protein–derived amino acids (l-[1-13C]-phenylalanine) into de novo myofibrillar protein showed a dose-dependent increase after ingestion of 15, 30, or 45 g protein (0.0171 ± 0.0017, 0.0296 ± 0.0030, and 0.0397 ± 0.0026 mole percentage excess, respectively; P < 0.05).ConclusionsDietary protein ingested during recovery from resistance exercise is rapidly digested and absorbed. Whole-body net protein balance and dietary protein-derived amino acid incorporation into myofibrillar protein show dose-dependent increases. Ingestion of ≥30 g protein increases postexercise myofibrillar protein synthesis rates in older men. This trial was registered at Nederlands Trial Register as NTR4492.

A healthy eating pattern, regardless of age, should consist of ingesting high quality protein preferably in adequate amounts across all meals throughout the day. Of particular relevance to overall health is the growth, development, and maintenance of skeletal muscle tissue. Skeletal muscle not only contributes to physical strength and performance, but also contributes to efficient macronutrient utilization and storage. Achieving an optimal amount of muscle mass begins early in life with transitions to “steady-state” maintenance as an adult, and then safeguarding against ultimate decline of muscle mass with age, all of which are influenced by physical activity and dietary (e.g., protein) factors. Current protein recommendations, as defined by recommended dietary allowances (RDA) for the US population or the population reference intakes (PRI) in Europe, are set to cover basic needs; however, it is thought that a higher protein intake might be necessary for optimizing muscle mass, especially for adults and individuals with an active lifestyle. It is necessary to balance the accurate assessment of protein quality (e.g., digestible indispensable amino acid score; DIAAS) with methods that provide a physiological correlate (e.g., established measures of protein synthesis, substrate oxidation, lean mass retention, or accrual, etc.) in order to accurately define protein requirements for these physiological outcomes. Moreover, current recommendations need to shift from single nutrient guidelines to whole food based guidelines in order to practically acknowledge food matrix interactions and other required nutrients for potentially optimizing the health effects of food. The aim of this paper is to discuss protein quality and amount that should be consumed with consideration to the presence of non-protein constituents within a food matrix and potential interactions with physical activity to maximize muscle mass throughout life.