Stimulate Muscle Protein Synthesis Rates Research Articles

The Muscle Protein Synthetic Response to the Ingestion of a Plant-Based Protein Blend Is Not Different From Milk Protein in Healthy, Young Males

Abstract Objectives It has been reported that plant-based proteins are not as effective as animal-based proteins in their capacity to stimulate muscle protein synthesis rates. This has been attributed to the lower essential amino acid content and the selective deficiency in specific amino acids. It has been hypothesized that a blend of different plant-based proteins may complement each other and, as such, compensate for such deficits. This study compares post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein with the ingestion of a 30 g blend of wheat, corn, and pea protein in vivo, in healthy young males. Methods In a randomized, double blind, parallel-group design, 24 healthy young males (24 ± 4 y) received a primed continuous infusion of L-[ring-13C6]-phenylalanine and ingested 30 g milk protein (MILK), or a 30 g protein blend with 15 g wheat, 7.5 g corn, and 7.5 g pea protein (PLANT) in beverage form (n = 12 per group). Both interventional drinks were matched for leucine content. Blood and muscle biopsies were collected for 5 h following protein ingestion to assess post-prandial plasma amino acid profiles and myofibrillar protein synthesis rates. Data are expressed as mean ± SD. Results MILK increased plasma essential amino acid concentrations ∼2 fold more than PLANT over the 5 h post-prandial period (incremental area under curve (iAUC): 151 ± 31 vs 79 ± 12 mmol∙5 h∙L−1 respectively; P < 0.001). Similarly, the leucine iAUC was ∼16% greater for MILK vs PLANT (36 ± 7 vs 31 ± 4 mmol∙5 h∙L−1 respectively; P < 0.05). Ingestion of both MILK and PLANT increased myofibrillar protein synthesis rates when compared to basal post-absorptive values (P < 0.001), with no significant differences between treatments (0.053 ± 0.013 vs 0.064 ± 0.016%∙h−1, respectively; P > 0.05). Conclusions Ingestion of 30 g of a wheat, corn, and pea protein blend increases muscle protein synthesis rates in healthy, young males. The post-prandial muscle protein synthetic response to the ingestion of 30 g of a wheat, corn and pea protein blend does not differ from the ingestion of an equivalent amount of milk protein in healthy, young males. Funding Sources TiFN

Leucine Is More Readily Oxidized When Ingested as an Isolated Nutrient versus Incorporated in Its Whole-Food Matrix

Abstract Objectives The ingestion of free amino acids, or isolated sources of protein, results in faster postprandial release of dietary amino acids into circulation, which stimulates muscle protein synthesis rates. However, indirect evidence suggests that this rapid release of dietary amino acids after the ingestion of free amino acids is coupled with higher amino acid oxidation rates when compared to a whole-food source. Whole food protein results in a reduced peak amplitude and prolonged postprandial aminoacidemia. This study aimed to assess the effects of eating a whole food source of protein on the stimulation of whole-body leucine oxidation rates versus eating these same nutrients in isolated form in healthy young adults. Methods In a crossover design, 10 recreationally active adults (24 ± 4 y; 5 M, 5 F) performed an acute bout of resistance exercise followed by the ingestion of salmon (SAL) (20.5 g protein and 7.5 g fat) or its matched constituents as crystalline amino acids and fish oil (ISO). Participants received priming doses of NaH13CO2 and L-[1–13C]leucine before initiating a constant L-[1–13C]leucine infusion. Blood and breath samples were collected at rest and after resistance exercise at regular intervals for the measurement of whole-body leucine oxidation rates and plasma leucine profiles. Data were tested using linear fixed effects models with time and group as fixed factors with Bonferroni's post hoc test. Results Postprandial plasma leucine concentrations did not differ between the SAL and ISO conditions (P > 0.05). Time to peak plasma leucine concentrations was faster in ISO (50 ± 27 min) vs. SAL (114 ± 64 min, P = 0.022) condition. Postprandial leucine oxidation rates were elevated from baseline at t = 30 min to t = 120 min in ISO and t = 60 min to t = 180 min in SAL (P < 0.001), with no total differences between group (P = 0.129). Time to peak leucine oxidation occurred sooner in ISO (66 ± 22 min; 1.358 ± 0.699 nmol · kg−1 · min−1) when compared to the SAL condition (105 ± 20 min; 1.067 ± 0.3076 nmol · kg−1 · min−1; P = 0.002). Conclusions We show that the ingestion of a whole-food source of protein resulted in a delayed stimulation of leucine oxidation when compared to free amino acid ingestion, but a similar net increase in oxidation during the 5 h postprandial period in healthy young adults. Funding Sources USDA National Institute of Food and Agriculture Hatch project 1017928

Mycoprotein represents a bioavailable and insulinotropic non-animal-derived dietary protein source: a dose-response study.

The anabolic potential of a dietary protein is determined by its ability to elicit postprandial rises in circulating essential amino acids and insulin. Minimal data exist regarding the bioavailability and insulinotropic effects of non-animal-derived protein sources. Mycoprotein is a sustainable and rich source of non-animal-derived dietary protein. We investigated the impact of mycoprotein ingestion, in a dose-response manner, on acute postprandial hyperaminoacidaemia and hyperinsulinaemia. In all, twelve healthy young men completed five experimental trials in a randomised, single-blind, cross-over design. During each trial, volunteers consumed a test drink containing either 20 g milk protein (MLK20) or a mass matched (not protein matched due to the fibre content) bolus of mycoprotein (20 g; MYC20), a protein matched bolus of mycoprotein (40 g; MYC40), 60 g (MYC60) or 80 g (MYC80) mycoprotein. Circulating amino acid, insulin and uric acid concentrations, and clinical chemistry profiles, were assessed in arterialised venous blood samples during a 4-h postprandial period. Mycoprotein ingestion resulted in slower but more sustained hyperinsulinaemia and hyperaminoacidaemia compared with milk when protein matched, with overall bioavailability equivalent between conditions (P>0·05). Increasing the dose of mycoprotein amplified these effects, with some evidence of a plateau at 60-80 g. Peak postprandial leucine concentrations were 201 (sem 24) (30 min), 118 (sem 10) (90 min), 150 (sem 14) (90 min), 173 (sem 23) (45 min) and 201 (sem 21 (90 min) µmol/l for MLK20, MYC20, MYC40, MYC60 and MYC80, respectively. Mycoprotein represents a bioavailable and insulinotropic dietary protein source. Consequently, mycoprotein may be a useful source of dietary protein to stimulate muscle protein synthesis rates.

Daily resistance-type exercise stimulates muscle protein synthesis in vivo in young men.

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 (2H2O). 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 [2H]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.

Pre-Sleep Protein Ingestion to Improve the Skeletal Muscle Adaptive Response to Exercise Training.

Protein ingestion following resistance-type exercise stimulates muscle protein synthesis rates, and enhances the skeletal muscle adaptive response to prolonged resistance-type exercise training. As the adaptive response to a single bout of resistance exercise extends well beyond the first couple of hours of post-exercise recovery, recent studies have begun to investigate the impact of the timing and distribution of protein ingestion during more prolonged recovery periods. Recent work has shown that overnight muscle protein synthesis rates are restricted by the level of amino acid availability. Protein ingested prior to sleep is effectively digested and absorbed, and thereby stimulates muscle protein synthesis rates during overnight recovery. When applied during a prolonged period of resistance-type exercise training, protein supplementation prior to sleep can further augment gains in muscle mass and strength. Recent studies investigating the impact of pre-sleep protein ingestion suggest that at least 40 g of protein is required to display a robust increase in muscle protein synthesis rates throughout overnight sleep. Furthermore, prior exercise allows more of the pre-sleep protein-derived amino acids to be utilized for de novo muscle protein synthesis during sleep. In short, pre-sleep protein ingestion represents an effective dietary strategy to improve overnight muscle protein synthesis, thereby improving the skeletal muscle adaptive response to exercise training.

Neuromuscular electrical stimulation prior to presleep protein feeding stimulates the use of protein-derived amino acids for overnight muscle protein synthesis.

Neuromuscular electrical stimulation (NMES) as well as presleep dietary protein ingestion represent effective strategies to stimulate muscle protein synthesis rates. Here we demonstrate that in older men after a day of bed rest, the application of NMES prior to presleep protein feeding stimulates the use of dietary protein-derived amino acids for overnight muscle protein synthesis by 18% compared with presleep protein feeding only.

Refining dietary protein recommendations for the athlete

Refining dietary protein recommendations for the athlete

Contributions to the understanding of the anabolic properties of different dietary proteins

Contributions to the understanding of the anabolic properties of different dietary proteins

The curious case of anabolic resistance: old wives' tales or new fables?

the progressive loss of muscle mass, commonly termed sarcopenia, accompanies the process of healthy aging ([27][1]). The underlying basis of this condition, in a very simplistic view, would be at a more advanced age skeletal muscle proteins are being lost because of an imbalance between muscle

Co-ingestion of protein and leucine stimulates muscle protein synthesis rates to the same extent in young and elderly lean men

The progressive loss of skeletal muscle mass with aging is attributed to a disruption in the regulation of skeletal muscle protein turnover. We investigated the effects on whole-body protein balance and mixed-muscle protein synthesis rates of the ingestion of carbohydrate with or without protein and free leucine after simulated activities of daily living. Eight elderly (75 +/- 1 y) and 8 young (20 +/- 1 y) lean men were randomly assigned to 2 crossover experiments in which they consumed either carbohydrate (CHO) or carbohydrate plus protein and free leucine (CHO+Pro+Leu) after performing 30 min of standardized activities of daily living. Primed, continuous infusions with L-[ring-13C6]phenylalanine and L-[ring-2H2]tyrosine were applied, and blood and muscle samples were collected to assess whole-body protein turnover and the protein fractional synthetic rate in the vastus lateralis muscle over a 6-h period. Whole-body phenylalanine and tyrosine flux were significantly higher in the young than in the elderly men (P < 0.01). Protein balance was negative in the CHO experiment but positive in the CHO+Pro+Leu experiment in both groups. Mixed-muscle protein synthesis rates were significantly greater in the CHO+Pro+Leu than in the CHO experiment in both the young (0.082 +/- 0.005%/h and 0.060 +/- 0.005%/h, respectively; P < 0.01) and the elderly (0.072 +/- 0.006%/h and 0.043 +/- 0.003%/h, respectively; P < 0.01) subjects, with no significant differences between groups. Co-ingestion of protein and leucine with carbohydrate after activities of daily living improves whole-body protein balance, and the increase in muscle protein synthesis rates is not significantly different between lean young and elderly men.

Response of human muscle protein synthesis to feeding: a comparison of methods

Feeding has been shown to stimulate muscle protein synthesis rates (FSR) in humans. However, while a substantial stimulation (+60–100%) of muscle FSR in response to feeding has been shown in studies using the constant infusion method, a much smaller response (+30%, P=NS) has been detected with the flooding method. The aim of this study was to assess whether the response of muscle protein synthesis to feeding depends on the technique used for measurement. Muscle FSR were measured both in the fasting and feeding states in two groups (n=8) of healthy volunteers (Age 31±2 y), with the same tracer and feeding regimen. However, in one group FSR were assessed with a flooding amount of L-[2H5]phenylalanine (45 mg/kg BW) and in the other one with a primed constant infusion of the same labeled amino acid (6 μmol/kg/h). Fasting FSR obtained with the flooding method were similar to that obtained with the constant infusion method calculated with phenylalanine within the tissue taken as the precursor pool for protein synthesis (1.86±0.13 vs. 1.94±0.15 %/day). The results also show that feeding is associated with a stimulation of FSR, whether assessed by the flooding method (+22%, P<0.01) or constant infusion (+13%, P<0.05). Lower fasting FSR (1.31±0.07 %/day, P<0.01) and a greater stimulation after feeding (+25%, P<0.05) were observed with the constant infusion method when plasma was used as a surrogate precursor pool. This study demonstrates that human muscle FSR measured with the flooding method is comparable to that obtained with the constant infusion, and that, under similar experimental conditions, the two methods give comparable estimates of stimulation from feeding. Supported by NIH grants AG017446 and 5-MO1-RR-10710