Leucine-Enriched Essential Amino Acids Enhance Post-Exercise Muscle Recovery Independent Of ‘Free-Living’ Myofibrillar Protein Synthesis

Background: Leucine-enriched essential amino acids (LEAAs) acutely enhance post-exercise myofibrillar protein synthesis (MyoPS), which has been suggested to be important for muscle repair and recovery. However, the ability of LEAAs to concurrently enhance MyoPS and muscle damage recovery in free-living humans has not been studied. Methods: In a randomized, double-blind, placebo-controlled, parallel-group design, twenty recreationally active males consuming a controlled diet (1.2 g/kg/d of protein) were supplemented thrice daily with 4 g of LEAAs (containing 1.6 g leucine) or isocaloric placebo for four days following an acute bout of lower-body resistance exercise (RE). MyoPS at rest and integrated over 96 h of recovery was measured by D2O. Isometric and isokinetic torque, muscle soreness, Z-band streaming, muscle heat shock protein (HSP) 25 and 72, plasma creatine kinase (CK), and plasma interleukin-6 (IL-6) were measured over 96 h post-RE to assess various direct and indirect markers of muscle damage. Results: Integrated MyoPS increased ~72% over 96 h after RE (p < 0.05), with no differences between groups (p = 0.98). Isometric, isokinetic, and total peak torque decreased ~21% by 48 h after RE (p < 0.05), whereas total peak torque was ~10% greater overall during recovery in LEAAs compared to placebo (p < 0.05). There were moderate to large effects for peak torque in favour of LEAAs. Muscle soreness increased during recovery with no statistical differences between groups but small to moderate effects in favour of LEAAs that correlated with changes in peak torque. Plasma CK, plasma IL-6, and muscle HSP25 increased after RE (p < 0.05) but were not significantly different between groups (p ≥ 0.13). Consistent with a trend toward attenuated Z-band streaming in LEAAs (p = 0.07), muscle HSP72 expression was lower (p < 0.05) during recovery in LEAAs compared with placebo. There were no correlations between MyoPS and any measures of muscle damage (p ≥ 0.37). Conclusion: Collectively, our data suggest that LEAAs moderately attenuated muscle damage without concomitant increases in integrated MyoPS in the days following an acute bout of resistance exercise in free-living recreationally active men.

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Effects of Salmon Ingestion on Post-Exercise Muscle Protein Synthesis: Exploration of Whole Protein Foods Versus Isolated Nutrients

Current Developments in Nutrition ◽

10.1093/cdn/nzaa049_043 ◽

2020 ◽

Vol 4 (Supplement_2) ◽

pp. 650-650

Author(s):

Kevin Paulussen ◽

Amadeo Salvador ◽

Colleen McKenna ◽

Susannah Scaroni ◽

Alexander Ulanov ◽

...

Keyword(s):

Protein Synthesis ◽

Amino Acid ◽

Muscle Protein ◽

Muscle Protein Synthesis ◽

Myofibrillar Protein ◽

Post Exercise ◽

Exercise Muscle ◽

Amino Acid Concentrations ◽

Myofibrillar Protein Synthesis ◽

Stimulation Of

Abstract Objectives Healthy eating patterns consist of eating whole foods as opposed to single nutrients. The maintenance of skeletal muscle mass is of particular interest to overall health. As such, there is a need to underpin the role of eating nutrients within their natural whole-food matrix versus isolated nutrients on the regulation of postprandial muscle protein synthesis rates. This study assessed the effects of eating salmon, a potential food within a healthy Mediterranean style eating pattern, on the stimulation of post-exercise muscle protein synthesis rates versus eating these same nutrients in isolation 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 in the form of crystalline amino acids and fish oil (ISO). Blood and muscle biopsies were collected at rest and after exercise at 2 and 5 h during primed continuous infusions of L-[ring-2H5]phenylalanine for the measurement of myofibrillar protein synthesis and plasma amino acid profiles. Data were analyzed by using a 2-factor (time × condition) repeated-measures ANOVA with Tukey's post hoc test. Results Plasma essential amino acid concentrations increased to a similar extent in both SAL and ISO during the postprandial period (P > 0.05). Likewise, postprandial plasma leucine concentrations did not differ between nutrient condition (P > 0.05). The post-exercise myofibrillar protein synthetic responses were similarly stimulated in both nutrition conditions early (0–2 h; 0.079 ± 0.039%/h (SAL) compared to 0.071 ± 0.078%/h (ISO); P = 0.64) and returned to baseline later (2–5 h; 0.046 ± 0.020%/h (SAL) compared to 0.038 ± 0.025%/h (ISO); P = 0.90). Similarly, there were no differences in the stimulation of myofibrillar protein synthesis rates between SAL and ISO during the entire 0–5 h recovery period (0.058 ± 0.024%/h compared to 0.045 ± 0.027%/h, respectively; P = 0.66). Conclusions We show that the ingestion of salmon or its isolated nutrients increases plasma amino acid concentrations and enhances the stimulation of post-exercise muscle protein synthesis rates with no differences in the temporal or cumulative responses in healthy young adults. Funding Sources USDA National Institute of Food and Agriculture Hatch project.

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Supplementation of a suboptimal protein dose with leucine or essential amino acids: effects on myofibrillar protein synthesis at rest and following resistance exercise in men

The Journal of Physiology ◽

10.1113/jphysiol.2012.228833 ◽

2012 ◽

Vol 590 (11) ◽

pp. 2751-2765 ◽

Cited By ~ 170

Author(s):

Tyler A. Churchward-Venne ◽

Nicholas A. Burd ◽

Cameron J. Mitchell ◽

Daniel W. D. West ◽

Andrew Philp ◽

...

Keyword(s):

Amino Acids ◽

Protein Synthesis ◽

Resistance Exercise ◽

Essential Amino Acids ◽

Myofibrillar Protein ◽

Myofibrillar Protein Synthesis

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Presleep dietary protein-derived amino acids are incorporated in myofibrillar protein during postexercise overnight recovery

AJP Endocrinology and Metabolism ◽

10.1152/ajpendo.00273.2016 ◽

2018 ◽

Vol 314 (5) ◽

pp. E457-E467 ◽

Cited By ~ 33

Author(s):

Jorn Trommelen ◽

Imre W. K. Kouw ◽

Andrew M. Holwerda ◽

Tim Snijders ◽

Shona L. Halson ◽

...

Keyword(s):

Amino Acids ◽

Protein Synthesis ◽

Dietary Protein ◽

Myofibrillar Protein ◽

Whole Body ◽

Body Protein ◽

Protein Ingestion ◽

Casein Protein ◽

The Impact ◽

Myofibrillar Protein Synthesis

The purpose of this study was to determine the impact of ingesting 30 g casein protein with and without 2 g free leucine before sleep on myofibrillar protein synthesis rates during postexercise overnight recovery. Thirty-six healthy young men performed a single bout of resistance-type exercise in the evening (1945) after a full day of dietary standardization. Thirty minutes before sleep (2330), subjects ingested 30 g intrinsically l-[1-13C]phenylalanine-labeled protein with (PRO+leu, n = 12) or without (PRO, n = 12) 2 g free leucine, or a noncaloric placebo (PLA, n = 12). Continuous intravenous l-[ ring-2H5]phenylalanine, l-[1-13C]leucine, and l-[ ring-2H2]tyrosine infusions were applied. Blood and muscle tissue samples were collected to assess whole body protein net balance, myofibrillar protein synthesis rates, and overnight incorporation of dietary protein-derived amino acids into myofibrillar protein. Protein ingestion before sleep improved overnight whole body protein net balance ( P < 0.001). Myofibrillar protein synthesis rates did not differ significantly between treatments as assessed by l-[ ring-2H5]phenylalanine (0.057 ± 0.002, 0.055 ± 0.002, and 0.055 ± 0.004%/h for PLA, PRO, and PRO+leu, respectively; means ± SE; P = 0.850) or l-[1-13C]leucine (0.080 ± 0.004, 0.073 ± 0.004, and 0.083 ± 0.006%/h, respectively; P = 0.328). Myofibrillar l-[1-13C]phenylalanine enrichments increased following protein ingestion but did not differ between the PRO and PRO+leu treatments. In conclusion, protein ingestion before sleep improves whole body protein net balance and provides amino acids that are incorporated into myofibrillar protein during sleep. However, the ingestion of 30 g casein protein with or without additional free leucine before sleep does not increase muscle protein synthesis rates during postexercise overnight recovery.

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Correction: Acute Post-Exercise Myofibrillar Protein Synthesis Is Not Correlated with Resistance Training-Induced Muscle Hypertrophy in Young Men

PLoS ONE ◽

10.1371/journal.pone.0098731 ◽

2014 ◽

Vol 9 (5) ◽

pp. e98731

Author(s):

Keyword(s):

Protein Synthesis ◽

Resistance Training ◽

Muscle Hypertrophy ◽

Young Men ◽

Myofibrillar Protein ◽

Post Exercise ◽

Myofibrillar Protein Synthesis

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Increased net muscle protein balance in response to simultaneous and separate ingestion of carbohydrate and essential amino acids following resistance exercise

Applied Physiology Nutrition and Metabolism ◽

10.1139/apnm-2013-0264 ◽

2014 ◽

Vol 39 (3) ◽

pp. 329-339 ◽

Cited By ~ 6

Author(s):

Oliver C. Witard ◽

Tara L. Cocke ◽

Arny A. Ferrando ◽

Robert R. Wolfe ◽

Kevin D. Tipton

Keyword(s):

Amino Acids ◽

Resistance Exercise ◽

Acute Exercise ◽

Muscle Protein ◽

Exercise Bout ◽

Essential Amino Acids ◽

Delayed Response ◽

Protein Balance ◽

Post Exercise ◽

Exercise Muscle

Relative to essential amino acids (EAAs), carbohydrate (CHO) ingestion stimulates a delayed response of net muscle protein balance (NBAL). We investigated if staggered ingestion of CHO and EAA would superimpose the response of NBAL following resistance exercise, thus resulting in maximal anabolic stimulation. Eight recreationally trained subjects completed 2 trials: combined (COMB — drink 1, CHO+EAA; drink 2, placebo) and separated (SEP — drink 1, CHO; drink 2, EAA) post-exercise ingestion of CHO and EAA. Drink 1 was administered 1 h following an acute exercise bout and was followed 1 h later by drink 2. A primed, continuous infusion of l-[ring-13C6]-phenylalanine was combined with femoral arteriovenous sampling and muscle biopsies for the determination of muscle protein kinetics. Arterial amino acid concentrations increased following ingestion of EAA in both conditions. No difference between conditions was observed for phenylalanine delivery to the leg (COMB: 167 ± 23 μmol·min−1·(100 mL leg vol)−1 × 6 h; SEP: 167 ± 21 μmol·min−1·(100 mL leg vol)−1 × 6 h, P > 0.05). In the first hour following ingestion of the drink containing EAA, phenylalanine uptake was 50% greater for the SEP trial than the COMB trial. However, phenylalanine uptake was similar for COMB (110 ± 19 mg) and SEP (117 ± 24 mg) over the 6 h period. These data suggest that whereas separation of CHO and EAA ingestion following exercise may have a transient physiological impact on NBAL, this response is not reflected over a longer period. Thus, separation of CHO and EAA ingestion is unnecessary to optimize post-exercise muscle protein metabolism.

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