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      Effects of soluble milk protein or casein supplementation on muscle fatigue following resistance training program: a randomized, double-blind, and placebo-controlled study

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          Abstract

          Background

          The effects of protein supplementation on muscle thickness, strength and fatigue seem largely dependent on its composition. The current study compared the effects of soluble milk protein, micellar casein, and a placebo on strength and fatigue during and after a resistance training program.

          Methods

          Sixty-eight physically active men participated in this randomized controlled trial and underwent 10 weeks of lower-body resistance training. Participants were randomly assigned to the Placebo (PLA), Soluble Milk Protein (SMP, with fast digestion rate) or Micellar Casein (MC, with slow digestion rate) group. During the 10-week training period, participants were instructed to take 30 g of the placebo or protein twice a day, or three times on training days. Tests were performed on quadriceps muscles at inclusion (PRE), after 4 weeks (MID) and after 10 weeks (POST) of training. They included muscle endurance (maximum number of repetitions during leg extensions using 70% of the individual maximal load), fatigue (decrease in muscle power after the endurance test), strength, power and muscle thickness.

          Results

          Muscle fatigue was significantly lower (P < 0.05) in the SMP group at MID and POST (-326.8 ± 114.1 W and -296.6 ± 130.1 W, respectively) as compared with PLA (-439.2 ± 153.9 W and -479.2 ± 138.1 W, respectively) and MC (-415.1 ± 165.1 W and -413.7 ± 139.4 W, respectively). Increases in maximal muscle power, strength, endurance and thickness were not statistically different between groups.

          Conclusions

          The present study demonstrated that protein composition has a large influence on muscular performance after prolonged resistance training. More specifically, as compared with placebo or micellar casein, soluble milk protein (fast digestible) appeared to significantly reduce muscle fatigue induced by intense resistance exercise.

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          Most cited references33

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          Low-Load High Volume Resistance Exercise Stimulates Muscle Protein Synthesis More Than High-Load Low Volume Resistance Exercise in Young Men

          Background We aimed to determine the effect of resistance exercise intensity (% 1 repetition maximum—1RM) and volume on muscle protein synthesis, anabolic signaling, and myogenic gene expression. Methodology/Principal Findings Fifteen men (21±1 years; BMI = 24.1±0.8 kg/m2) performed 4 sets of unilateral leg extension exercise at different exercise loads and/or volumes: 90% of repetition maximum (1RM) until volitional failure (90FAIL), 30% 1RM work-matched to 90%FAIL (30WM), or 30% 1RM performed until volitional failure (30FAIL). Infusion of [ring-13C6] phenylalanine with biopsies was used to measure rates of mixed (MIX), myofibrillar (MYO), and sarcoplasmic (SARC) protein synthesis at rest, and 4 h and 24 h after exercise. Exercise at 30WM induced a significant increase above rest in MIX (121%) and MYO (87%) protein synthesis at 4 h post-exercise and but at 24 h in the MIX only. The increase in the rate of protein synthesis in MIX and MYO at 4 h post-exercise with 90FAIL and 30FAIL was greater than 30WM, with no difference between these conditions; however, MYO remained elevated (199%) above rest at 24 h only in 30FAIL. There was a significant increase in AktSer473 at 24h in all conditions (P = 0.023) and mTORSer2448 phosphorylation at 4 h post-exercise (P = 0.025). Phosporylation of Erk1/2Tyr202/204, p70S6KThr389, and 4E-BP1Thr37/46 increased significantly (P<0.05) only in the 30FAIL condition at 4 h post-exercise, whereas, 4E-BP1Thr37/46 phosphorylation was greater 24 h after exercise than at rest in both 90FAIL (237%) and 30FAIL (312%) conditions. Pax7 mRNA expression increased at 24 h post-exercise (P = 0.02) regardless of condition. The mRNA expression of MyoD and myogenin were consistently elevated in the 30FAIL condition. Conclusions/Significance These results suggest that low-load high volume resistance exercise is more effective in inducing acute muscle anabolism than high-load low volume or work matched resistance exercise modes.
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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.

            Leucine is a nutrient regulator of muscle protein synthesis by activating mTOR and possibly other proteins in this pathway. The purpose of this study was to examine the role of leucine in the regulation of human myofibrillar protein synthesis (MPS). Twenty-four males completed an acute bout of unilateral resistance exercise prior to consuming either: a dose (25 g) of whey protein (WHEY); 6.25 g whey protein with total leucine equivalent to WHEY (LEU); or 6.25 g whey protein with total essential amino acids (EAAs) equivalent to WHEY for all EAAs except leucine (EAA-LEU). Measures of MPS, signalling through mTOR, and amino acid transporter (AAT) mRNA abundance were made while fasted (FAST), and following feeding under rested (FED) and post-exercise (EX-FED) conditions. Leucinaemia was equivalent between WHEY and LEU and elevated compared to EAA-LEU (P=0.001). MPS was increased above FAST at 1–3 h post-exercise in both FED (P <0.001) and EX-FED (P <0.001) conditions with no treatment effect.At 3–5 h, only WHEY remained significantly elevated above FAST in EX-FED(WHEY 184% vs. LEU 55% and EAA-LEU 35%; P =0.036). AAT mRNA abundance was increased above FAST after feeding and exercise with no effect of leucinaemia. In summary, a low dose of whey protein supplemented with leucine or all other essential amino acids was as effective as a complete protein (WHEY) in stimulating postprandial MPS; however only WHEY was able to sustain increased rates of MPS post-exercise and may therefore be most suited to increase exercise-induced muscle protein accretion.
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              Muscle hypertrophy, hormonal adaptations and strength development during strength training in strength-trained and untrained men.

              Hormonal and neuromuscular adaptations to strength training were studied in eight male strength athletes (SA) and eight non-strength athletes (NA). The experimental design comprised a 21-week strength-training period. Basal hormonal concentrations of serum total testosterone (T), free testosterone (FT) and cortisol (C) and maximal isometric strength, right leg 1 repetition maximum (RM) of the leg extensors were measured at weeks 0, 7, 14 and 21. Muscle cross-sectional area (CSA) of the quadriceps femoris was measured by magnetic resonance imaging (MRI) at weeks 0 and 21. In addition, the acute heavy resistance exercises (AHRE) (bilateral leg extension, five sets of ten RM, with a 2-min rest between sets) including blood samples for the determination of serum T, FT, C, and GH concentrations were assessed before and after the 21-week training. Significant increases of 20.9% in maximal force and of 5.6% in muscle CSA in NA during the 21-week strength training period were greater than those of 3.9% and -1.8% in SA, respectively. There were no significant changes in serum basal hormone concentrations during the 21-week experiment. AHRE led to significant acute decreases in isometric force and acute increases in serum hormones both at weeks 0 and 21. Basal T concentrations (mean of 0, 7, 14 and 21 weeks) and changes in isometric force after the 21-week period correlated with each other (r=0.84, P<0.01) in SA. The individual changes in the acute T responses between weeks 0 and 21 and the changes in muscle CSA during the 21-week training correlated with each other (r=0.76, P<0.05) in NA. The correlations between T and the changes in isometric strength and in muscle CSA suggest that both serum basal testosterone concentrations and training-induced changes in acute testosterone responses may be important factors for strength development and muscle hypertrophy.
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                Author and article information

                Contributors
                Journal
                J Int Soc Sports Nutr
                J Int Soc Sports Nutr
                Journal of the International Society of Sports Nutrition
                BioMed Central
                1550-2783
                2014
                11 July 2014
                : 11
                : 36
                Affiliations
                [1 ]National Institute for health and medical research (INSERM), unit 1093, Cognition, Action and sensorimotor plasticity, Dijon, France
                [2 ]Centre for Performance Expertise, UFR STAPS, Dijon, France
                [3 ]Lactalis R&D, Retiers, France
                [4 ]Chair of Medical Evaluation ESC, Dijon, France
                [5 ]CEN Nutriment, Dijon, France
                [6 ]Faculté des Sciences du Sport, Université de Bourgogne, BP 27877, 21078 Dijon, Cedex, France
                Article
                1550-2783-11-36
                10.1186/1550-2783-11-36
                4107592
                25057266
                5833c601-af30-4507-8b56-396fa2dddf0c
                Copyright © 2014 Babault et al.; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                : 23 December 2013
                : 1 July 2014
                Categories
                Research Article

                Sports medicine
                muscle power,endurance,muscle thickness,branched-chain amino acids
                Sports medicine
                muscle power, endurance, muscle thickness, branched-chain amino acids

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