Alcohol Ingestion Impairs Maximal Post-Exercise Rates of Myofibrillar Protein Synthesis following a Single Bout of Concurrent Training

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

PLoS ONE ◽

10.1371/journal.pone.0089431 ◽

2014 ◽

Vol 9 (2) ◽

pp. e89431 ◽

Cited By ~ 115

Author(s):

Cameron J. Mitchell ◽

Tyler A. Churchward-Venne ◽

Gianni Parise ◽

Leeann Bellamy ◽

Steven K. Baker ◽

...

Keyword(s):

Protein Synthesis ◽

Resistance Training ◽

Muscle Hypertrophy ◽

Young Men ◽

Myofibrillar Protein ◽

Post Exercise ◽

Myofibrillar Protein Synthesis

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Hot-water immersion does not increase postprandial muscle protein synthesis rates during recovery from resistance-type exercise in healthy, young males

Journal of Applied Physiology ◽

10.1152/japplphysiol.00836.2019 ◽

2020 ◽

Vol 128 (4) ◽

pp. 1012-1022 ◽

Cited By ~ 2

Author(s):

Cas J. Fuchs ◽

Joey S. J. Smeets ◽

Joan M. Senden ◽

Antoine H. Zorenc ◽

Joy P. B. Goessens ◽

...

Keyword(s):

Amino Acids ◽

Protein Synthesis ◽

Dietary Protein ◽

Water Immersion ◽

Recovery Period ◽

Myofibrillar Protein ◽

Hot Water ◽

Single Bout ◽

Myofibrillar Protein Synthesis ◽

Hot Water Immersion

The purpose of this study was to assess the impact of postexercise hot-water immersion on postprandial myofibrillar protein synthesis rates during recovery from a single bout of resistance-type exercise in healthy, young men. Twelve healthy, adult men (age: 23 ± 1 y) performed a single bout of resistance-type exercise followed by 20 min of water immersion of both legs. One leg was immersed in hot water [46°C: hot-water immersion (HWI)], while the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine labeled milk protein with 45 g of carbohydrates. In addition, primed continuous L-[ ring-2H5]-phenylalanine and L-[1-13C]-leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5-h recovery period. Muscle temperature immediately after water immersion was higher in the HWI compared with the CON leg (37.5 ± 0.1 vs. 35.2 ± 0.2°C; P < 0.001). Incorporation of dietary protein-derived L-[1-13C]-phenylalanine into myofibrillar protein did not differ between the HWI and CON leg during the 5-h recovery period (0.025 ± 0.003 vs. 0.024 ± 0.002 MPE; P = 0.953). Postexercise myofibrillar protein synthesis rates did not differ between the HWI and CON leg based upon L-[1-13C]-leucine (0.050 ± 0.005 vs. 0.049 ± 0.002%/h; P = 0.815) and L-[ ring-2H5]-phenylalanine (0.048 ± 0.002 vs. 0.047 ± 0.003%/h; P = 0.877), respectively. Hot-water immersion during recovery from resistance-type exercise does not increase the postprandial rise in myofibrillar protein synthesis rates. In addition, postexercise hot-water immersion does not increase the capacity of the muscle to incorporate dietary protein-derived amino acids in muscle tissue protein during subsequent recovery. NEW & NOTEWORTHY This is the first study to assess the effect of postexercise hot-water immersion on postprandial myofibrillar protein synthesis rates and the incorporation of dietary protein-derived amino acids into muscle protein. We observed that hot-water immersion during recovery from a single bout of resistance-type exercise does not further increase myofibrillar protein synthesis rates or augment the postprandial incorporation of dietary protein-derived amino acids in muscle throughout 5 h of postexercise recovery.

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

Medicine & Science in Sports & Exercise ◽

10.1249/01.mss.0000671188.68270.42 ◽

2020 ◽

Vol 52 (7S) ◽

pp. 105-105

Author(s):

Marcus Waskiw-Ford

Keyword(s):

Amino Acids ◽

Protein Synthesis ◽

Essential Amino Acids ◽

Myofibrillar Protein ◽

Muscle Recovery ◽

Free Living ◽

Post Exercise ◽

Exercise Muscle ◽

Myofibrillar Protein Synthesis

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Differential Stimulation of Post-Exercise Myofibrillar Protein Synthesis in Humans Following Isonitrogenous, Isocaloric Pre-Exercise Feeding

Nutrients ◽

10.3390/nu11071657 ◽

2019 ◽

Vol 11 (7) ◽

pp. 1657 ◽

Cited By ~ 8

Author(s):

Robert W. Davies ◽

Joseph J. Bass ◽

Brian P. Carson ◽

Catherine Norton ◽

Marta Kozior ◽

...

Keyword(s):

Protein Synthesis ◽

Whey Protein ◽

Deuterium Oxide ◽

Vastus Lateralis ◽

Isotope Ratio Mass Spectrometry ◽

Negative Control ◽

Myofibrillar Protein ◽

Double Blind ◽

Post Exercise ◽

Myofibrillar Protein Synthesis

The aim of this study was to test the effects of two disparate isonitrogenous, isocaloric pre-exercise feeds on deuterium-oxide (D2O) derived measures of myofibrillar protein synthesis (myoPS) in humans. Methods: In a double-blind parallel group design, 22 resistance-trained men aged 18 to 35 years ingested a meal (6 kcal·kg−1, 0.8 g·kg−1 carbohydrate, 0.2 g·kg−1 fat) with 0.33 g·kg−1 nonessential amino acids blend (NEAA) or whey protein (WHEY), prior to resistance exercise (70% 1RM back-squats, 10 reps per set to failure, 25% duty cycle). Biopsies of M. vastus lateralis were obtained pre-ingestion (PRE) and +3 h post-exercise (POST). The myofibrillar fractional synthetic rate (myoFSR) was calculated via deuterium labelling of myofibrillar-bound alanine, measured by gas chromatography–pyrolysis–isotope ratio mass spectrometry (GC-Pyr-IRMS). Data are a mean percentage change (95% CI). Results: There was no discernable change in myoFSR following NEAA (10(−5, 25) %, p = 0.235), whereas an increase in myoFSR was observed after WHEY (28 (13, 43) %, p = 0.003). Conclusions: Measured by a D2O tracer technique, a disparate myoPS response was observed between NEAA and WHEY. Pre-exercise ingestion of whey protein increased post-exercise myoPS, whereas a NEAA blend did not, supporting the use of NEAA as a viable isonitrogenous negative control.

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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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Hypoenergetic diet-induced reductions in myofibrillar protein synthesis are restored with resistance training and balanced daily protein ingestion in older men

AJP Endocrinology and Metabolism ◽

10.1152/ajpendo.00550.2014 ◽

2015 ◽

Vol 308 (9) ◽

pp. E734-E743 ◽

Cited By ~ 58

Author(s):

Caoileann H. Murphy ◽

Tyler A. Churchward-Venne ◽

Cameron J. Mitchell ◽

Nathan M. Kolar ◽

Amira Kassis ◽

...

Keyword(s):

Protein Synthesis ◽

Resistance Training ◽

Older Men ◽

Myofibrillar Protein ◽

Energy Restriction ◽

Protein Distribution ◽

Protein Meal ◽

Fed State ◽

Sarcoplasmic Protein ◽

Myofibrillar Protein Synthesis

Strategies to enhance weight loss with a high fat-to-lean ratio in overweight/obese older adults are important since lean loss could exacerbate sarcopenia. We examined how dietary protein distribution affected muscle protein synthesis during energy balance (EB), energy restriction (ER), and energy restriction plus resistance training (ER + RT). A 4-wk ER diet was provided to overweight/obese older men (66 ± 4 yr, 31 ± 5 kg/m2) who were randomized to either a balanced (BAL: 25% daily protein/meal × 4) or skewed (SKEW: 7:17:72:4% daily protein/meal; n = 10/group) pattern. Myofibrillar and sarcoplasmic protein fractional synthetic rates (FSR) were measured during a 13-h primed continuous infusion of l-[ ring-13C6]phenylalanine with BAL and SKEW pattern of protein intake in EB, after 2 wk ER, and after 2 wk ER + RT. Fed-state myofibrillar FSR was lower in ER than EB in both groups ( P < 0.001), but was greater in BAL than SKEW ( P = 0.014). In ER + RT, fed-state myofibrillar FSR increased above ER in both groups and in BAL was not different from EB ( P = 0.903). In SKEW myofibrillar FSR remained lower than EB ( P = 0.002) and lower than BAL ( P = 0.006). Fed-state sarcoplasmic protein FSR was reduced similarly in ER and ER + RT compared with EB ( P < 0.01) in both groups. During ER in overweight/obese older men a BAL consumption of protein stimulated the synthesis of muscle contractile proteins more effectively than traditional, SKEW distribution. Combining RT with a BAL protein distribution “rescued” the lower rates of myofibrillar protein synthesis during moderate ER.

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