Oliver C. Witard

Protein Ingestion to Stimulate Myofibrillar Protein Synthesis Requires Greater Relative Protein Intakes in Healthy Older Versus Younger Men

BACKGROUNDnAdequate protein ingestion-mediated stimulation of myofibrillar protein synthesis (MPS) is required to maintain skeletal muscle mass. It is currently unknown what per meal protein intake is required to maximally stimulate the response in older men and whether it differs from that of younger men.nnnMETHODSnWe retrospectively analyzed data from our laboratories that measured MPS in healthy older (~71 years) and younger (~22 years) men by primed constant infusion of l-ring-[(13)C6]phenylalanine after ingestion of varying amounts (0-40 g) of high-quality dietary protein as a single bolus and normalized to body mass and, where available, lean body mass (LBM).nnnRESULTSnThere was no difference (p = .53) in basal MPS rates between older (0.027±0.04%/h; means ± 95% CI) and young (0.028 ± 0.03%/h) men. Biphase linear regression and breakpoint analysis revealed the slope of first line segment was lower (p < .05) in older men and that MPS reached a plateau after ingestion of 0.40 ± 0.19 and 0.24 ± 0.06 g/kg body mass (p = .055) and 0.60 ± 0.29 and 0.25 ± 0.13 g/kg lean body mass (p < .01) in older and younger men, respectively.nnnCONCLUSIONSnThis is the first report of the relative (to body weight) protein ingested dose response of MPS in younger and older men. Our data suggest that healthy older men are less sensitive to low protein intakes and require a greater relative protein intake, in a single meal, than young men to maximally stimulate postprandial rates of MPS. These results should be considered when developing nutritional solutions to maximize MPS for the maintenance or enhancement of muscle mass with advancing age.

Myofibrillar muscle protein synthesis rates subsequent to a meal in response to increasing doses of whey protein at rest and after resistance exercise

BACKGROUNDnThe intake of whey, compared with casein and soy protein intakes, stimulates a greater acute response of muscle protein synthesis (MPS) to protein ingestion in rested and exercised muscle.nnnOBJECTIVEnWe characterized the dose-response relation of postabsorptive rates of myofibrillar MPS to increasing amounts of whey protein at rest and after exercise in resistance-trained, young men.nnnDESIGNnVolunteers (n = 48) consumed a standardized, high-protein (0.54 g/kg body mass) breakfast. Three hours later, a bout of unilateral exercise (8 × 10 leg presses and leg extensions; 80% one-repetition maximum) was performed. Volunteers ingested 0, 10, 20, or 40 g whey protein isolate immediately (~10 min) after exercise. Postabsorptive rates of myofibrillar MPS and whole-body rates of phenylalanine oxidation and urea production were measured over a 4-h postdrink period by continuous tracer infusion of labeled [(13)C6] phenylalanine and [(15)N2] urea.nnnRESULTSnMyofibrillar MPS (mean ± SD) increased (P < 0.05) above 0 g whey protein (0.041 ± 0.015%/h) by 49% and 56% with the ingestion of 20 and 40 g whey protein, respectively, whereas no additional stimulation was observed with 10 g whey protein (P > 0.05). Rates of phenylalanine oxidation and urea production increased with the ingestion of 40 g whey protein.nnnCONCLUSIONSnA 20-g dose of whey protein is sufficient for the maximal stimulation of postabsorptive rates of myofibrillar MPS in rested and exercised muscle of ~80-kg resistance-trained, young men. A dose of whey protein >20 g stimulates amino acid oxidation and ureagenesis. This trial was registered at http://www.isrctn.org/ as ISRCTN92528122.

Branched-Chain Amino Acid Ingestion Can Ameliorate Soreness from Eccentric Exercise

PURPOSEnThe purpose of this study was to examine the role of branched-chain amino acid (BCAA) supplementation during recovery from intense eccentric exercise.nnnMETHODSnTwenty-four non-weight-trained males were assigned to one of two groups: one group (supplementary, SUP) ingested BCAA beverages (n = 12); the second group (placebo, PLA) ingested artificially flavored water (n = 12). Diet was controlled throughout the testing period to match habitual intake. The eccentric exercise protocol consisted of 12 x 10 repetitions of unilateral eccentric knee extension exercise at 120% concentric one repetition maximum. On the day of the exercise, supplements were consumed 30 min before exercise, 1.5 h after exercise, between lunch and dinner, and before bed. On the following 2 d, four supplements were consumed between meals. Muscle soreness, muscle function, and putative blood markers of muscle damage were assessed before and after (1, 8, 24, 48, and 72 h) exercise.nnnRESULTSnMuscle function decreased after the eccentric exercise (P < 0.0001), but the degree of force loss was unaffected by BCAA ingestion (51% +/- 3% with SUP vs -48% +/- 7% with PLA). A decrease in flexed muscle soreness was observed in SUP compared with PLA at 48 h (21 +/- 3 mm vs 32 +/- 3 mm, P = 0.02) and 72 h (17 +/- 3 mm vs 27 +/- 4 mm, P = 0.038). Flexed muscle soreness, expressed as area under the curve, was lower in SUP than in PLA (P = 0.024).nnnCONCLUSIONSnBCAA supplementation may attenuate muscle soreness, but it does not ameliorate eccentric exercise-induced decrements in muscle function or increases in reputed blood markers of muscle damage, when consumed before exercise and for 3 d after an eccentric exercise bout.

Resistance Exercise Increases Postprandial Muscle Protein Synthesis in Humans

PURPOSEnWe examined the impact of an acute bout of resistance-type exercise on mixed muscle protein synthesis in the fed state.nnnMETHODSnAfter a standardized breakfast, 10 untrained males completed a single, unilateral lower-limb resistance-type exercise session. A primed, continuous infusion of l-[ring-C6]phenylalanine was combined with muscle biopsy collection from both the exercised (Ex) and the nonexercised (NEx) leg to assess the impact of local muscle contractions on muscle protein synthesis rates after food intake. Western blotting with phosphospecific and pan antibodies was used to determine the phosphorylation status of AMP-activated kinase (AMPK), 4E-binding protein (4E-BP1), mammalian target of rapamycin (mTOR), and p70 ribosomal protein S6 kinase (S6K1).nnnRESULTSnMuscle protein synthesis rates were approximately 20% higher in Ex compared with NEx (0.098% +/- 0.005% vs 0.083% +/- 0.002%.h, respectively, P < 0.01). In the fed state, resistance-type exercise did not elevate AMPK phosphorylation. However, the phosphorylation status of 4E-BP1 was approximately 20% lower after cessation of exercise in Ex compared with NEx (P < 0.05). Conversely, 4E-BP1 phosphorylation was significantly higher in Ex compared with NEx after 6 h of recovery (P < 0.05) with no changes in mTOR phosphorylation. S6 phosphorylation was greater in Ex versus NEx after cessation of exercise (P < 0.05), although S6K1 phosphorylation at T was not up-regulated (P > 0.05).nnnCONCLUSIONnWe conclude that resistance-type exercise performed in a fed state further elevates postprandial muscle protein synthesis rates, which is accompanied by an increase in S6 and 4E-BP1 phosphorylation state.

Effect of increased dietary protein on tolerance to intensified training.

PURPOSEnThe purpose of the present study was to examine the effect of increased protein intake on short-term decrements in endurance performance during a block of high-intensity training.nnnMETHODSnTrained male cyclists (VO(2max) = 64.2 ± 6.5 mL·kg(-1)·min(-1)) completed two 3-wk trials both divided equally into normal (NOR), intensified (INT), and recovery (REC) training. In a counterbalanced crossover experimental design, cyclists received either a high-protein (PRO; 3 g protein·kg(-1) body mass (BM)·d(-1)) or a normal diet (CON; 1.5 g protein·kg(-1) BM·d(-1)) during INT and REC. Dietary carbohydrate content remained constant at 6 g·kg(-1) BM·d(-1). Energy balance was maintained during each training week. Endurance performance was assessed with a VO(2max) test and a preloaded time trial. Alterations in blood metabolite responses to exercise were measured at rest, during, and after exercise. Cyclists completed the Daily Analysis of Life Demands for Athletes (DALDA) questionnaire each day.nnnRESULTSnIncreased dietary protein intake led to a possible attenuation (4.3%; 90% confidence limits ×/÷5.4%) in the decrement in time trial performance after a block of high-intensity training compared with NOR (PRO = 2639 ± 350 s; CON = 2555 ± 313 s). Restoration of endurance performance during recovery training possibly benefited (2.0%; ×/÷4.9%) from additional protein intake. Frequency of symptoms of stress described as worse than normal reported after a block of high-intensity training was very likely (97%) attenuated (17; ±11 AUC of a scores part B, DALDA for INT + REC) by increasing the protein content of the diet. No discernable changes in blood metabolite concentrations were observed in PRO.nnnCONCLUSIONSnAdditional protein intake reduced symptoms of psychological stress and may result in a worthwhile amelioration of the performance decline experienced during a block of high-intensity training.

The response of muscle protein synthesis following whole-body resistance exercise is greater following 40 g than 20 g of ingested whey protein

The currently accepted amount of protein required to achieve maximal stimulation of myofibrillar protein synthesis (MPS) following resistance exercise is 20–25 g. However, the influence of lean body mass (LBM) on the response of MPS to protein ingestion is unclear. Our aim was to assess the influence of LBM, both total and the amount activated during exercise, on the maximal response of MPS to ingestion of 20 or 40 g of whey protein following a bout of whole‐body resistance exercise. Resistance‐trained males were assigned to a group with lower LBM (≤65 kg; LLBM n = 15) or higher LBM (≥70 kg; HLBM n = 15) and participated in two trials in random order. MPS was measured with the infusion of 13C6‐phenylalanine tracer and collection of muscle biopsies following ingestion of either 20 or 40 g protein during recovery from a single bout of whole‐body resistance exercise. A similar response of MPS during exercise recovery was observed between LBM groups following protein ingestion (20 g – LLBM: 0.048 ± 0.018%·h−1; HLBM: 0.051 ± 0.014%·h−1; 40 g – LLBM: 0.059 ± 0.021%·h−1; HLBM: 0.059 ± 0.012%·h−1). Overall (groups combined), MPS was stimulated to a greater extent following ingestion of 40 g (0.059 ± 0.020%·h−1) compared with 20 g (0.049 ± 0.020%·h−1; P = 0.005) of protein. Our data indicate that ingestion of 40 g whey protein following whole‐body resistance exercise stimulates a greater MPS response than 20 g in young resistance‐trained men. However, with the current doses, the total amount of LBM does not seem to influence the response.

High dietary protein restores overreaching induced impairments in leukocyte trafficking and reduces the incidence of upper respiratory tract infection in elite cyclists

The present study examined whether a high protein diet prevents the impaired leukocyte redistribution in response to acute exercise caused by a large volume of high-intensity exercise training. Eight cyclists (VO2max: 64.2±6.5mLkg(-1)min(-1)) undertook two separate weeks of high-intensity training while consuming either a high protein diet (3gkg(-1)proteinBM(-1)day(-1)) or an energy and carbohydrate-matched control diet (1.5gkg(-1)proteinBM(-1)day(-1)). High-intensity training weeks were preceded by a week of normal-intensity training under the control diet. Leukocyte and lymphocyte sub-population responses to acute exercise were determined at the end of each training week. Self-reported symptoms of upper-respiratory tract infections (URTI) were monitored daily by questionnaire. Undertaking high-intensity training with a high protein diet restored leukocyte kinetics to similar levels observed during normal-intensity training: CD8(+) TL mobilization (normal-intensity: 29,319±13,130cells/μL×∼165min vs. high-intensity with protein: 26,031±17,474cells/μL×∼165min, P>0.05), CD8(+) TL egress (normal-intensity: 624±264cells/μL vs. high-intensity with protein: 597±478cells/μL, P>0.05). This pattern was driven by effector-memory populations mobilizing (normal-intensity: 6,145±6,227cells/μL×∼165min vs. high-intensity with protein: 6,783±8,203cells/μL×∼165min, P>0.05) and extravastating from blood (normal-intensity: 147±129cells/μL vs. high-intensity with protein: 165±192cells/μL, P>0.05). High-intensity training while consuming a high protein diet was associated with fewer symptoms of URTI compared to performing high-intensity training with a normal diet (P<0.05). To conclude, a high protein diet might reduce the incidence of URTI in athletes potentially mediated by preventing training-induced impairments in immune-surveillance.

Protein Considerations for Optimising Skeletal Muscle Mass in Healthy Young and Older Adults

Skeletal muscle is critical for human health. Protein feeding, alongside resistance exercise, is a potent stimulus for muscle protein synthesis (MPS) and is a key factor that regulates skeletal muscle mass (SMM). The main purpose of this narrative review was to evaluate the latest evidence for optimising the amino acid or protein source, dose, timing, pattern and macronutrient coingestion for increasing or preserving SMM in healthy young and healthy older adults. We used a systematic search strategy of PubMed and Web of Science to retrieve all articles related to this review objective. In summary, our findings support the notion that protein guidelines for increasing or preserving SMM are more complex than simply recommending a total daily amount of protein. Instead, multifactorial interactions between protein source, dose, timing, pattern and macronutrient coingestion, alongside exercise, influence the stimulation of MPS, and thus should be considered in the context of protein recommendations for regulating SMM. To conclude, on the basis of currently available scientific literature, protein recommendations for optimising SMM should be tailored to the population or context of interest, with consideration given to age and resting/post resistance exercise conditions.

Growing older with health and vitality: a nexus of physical activity, exercise and nutrition

The preservation of skeletal muscle mass and strength with advancing age are, we propose, critical aspects of ageing with health and vitality. Physical inactivity and poor nutrition are known to accelerate the gradual age-related decline in muscle mass and strength—sarcopenia—however, both are subject to modification. The main purpose of this review is to present the latest, evidence-based recommendations for physical activity and exercise, as well as diet for older adults that would help in preserving muscle mass and strength. We take the position that future physical activity/exercise guidelines need to make specific reference to resistance exercise and highlight the benefits of higher-intensity aerobic exercise training, alongside advocating older adults perform aerobic-based physical activity and household tasks (e.g., carrying groceries). In terms of dietary recommendations, greater emphasis should be placed on optimal rather than minimum protein intakes for older adults. Indeed, guidelines that endorse a daily protein intake of 1.2–1.5xa0g/kg BM/day, which are levels 50–90xa0% greater than the current protein Recommendation Dietary Allowance (0.8xa0g/kg BM/day), are likely to help preserve muscle mass and strength and are safe for healthy older adults. Being cognisant of factors (e.g., reduced appetite) that may preclude older adults from increasing their total daily protein intake, we echo the viewpoint of other active researchers in advocating that protein recommendations for older adults be based on a per meal approach in order to maximize muscle protein synthesis (MPS). On this basis, assuming three meals are consumed daily, a protein dose of 0.4–0.5xa0g/kg BM should be contained in each meal. We are beginning to understand ways in which to increase the utilization of ingested protein for the stimulation of MPS, namely by increasing the proportion of leucine contained in a given dose of protein, co-ingesting other nutrients (e.g., carbohydrate and fat or supplementation with n-3 polyunsaturated fatty acids) or being physically active prior to protein intake. Clearly, developing simple lifestyle interventions targeted at preserving muscle mass and strength with advancing age is crucial for facilitating longer, healthier lives into older age.

Fish oil supplementation suppresses resistance exercise and feeding-induced increases in anabolic signaling without affecting myofibrillar protein synthesis in young men

Fish oil (FO) supplementation potentiates muscle protein synthesis (MPS) in response to a hyperaminoacidemic–hyperinsulinemic infusion. Whether FO supplementation potentiates MPS in response to protein ingestion or when protein ingestion is combined with resistance exercise (RE) remains unknown. In a randomized, parallel group design, 20 healthy males were randomized to receive 5 g/day of either FO or coconut oil control (CO) for 8 weeks. After supplementation, participants performed a bout of unilateral RE followed by ingestion of 30 g of whey protein. Skeletal muscle biopsies were obtained before and after supplementation for assessment of muscle lipid composition and relevant protein kinase activities. Infusion of l‐[ring‐13C6] phenylalanine was used to measure basal myofibrillar MPS at rest (REST), in a nonexercised leg following protein ingestion (FED) and following RE and protein ingestion (FEDEX). MPS was significantly elevated above REST during FEDEX in both the FO and CO groups, but there was no effect of supplementation. There was a significant increase in MPS in both groups above REST during FED but no effect of supplementation. Supplementation significantly decreased panPKB activity at REST in the FO group but not the CO group. There was a significant increase from REST at post‐RE for PKB and AMPKα2 activity in the CO group but not in the FO group. In FEDEX, there was a significant increase in p70S6K1 activity from REST at 3 h in the CO group only. These data highlight that 8 weeks of FO supplementation alters kinase signaling activity in response to RE plus protein ingestion without influencing MPS.