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      Post-exercise branched chain amino acid supplementation does not affect recovery markers following three consecutive high intensity resistance training bouts compared to carbohydrate supplementation

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          Abstract

          Background

          Amino acid supplementation has been shown to potentially reduced exercise-induced muscle soreness. Thus, the purpose of this study was to examine if branched chain amino acid and carbohydrate (BCAACHO) versus carbohydrate-only sports drink (CHO) supplementation attenuated markers of muscle damage while preserving performance markers following 3 days of intense weight training.

          Methods

          Healthy resistance-trained males ( n = 30) performed preliminary testing (T1) whereby they: 1) donated a baseline blood draw, 2) performed knee extensor dynamometry to obtain peak quadriceps isometric and isokinetic torque as well as electromyography (EMG) activity at 60°/s and 120°/s, and 3) performed a one repetition maximum (1RM) barbell back squat. The following week participants performed 10 sets x 5 repetitions at 80 % of their 1RM barbell back squat for 3 consecutive days and 48 h following the third lifting bout participants returned for (T2) testing whereby they repeated the T1 battery. Immediately following and 24 h after the three lifting bouts, participants were randomly assigned to consume one of two commercial products in 600 mL of tap water: 1) BCAAs and CHO (3 g/d L-leucine, 1 g/d L-isoleucine and 2 g/d L-valine with 2 g of CHO; n = 15), or 2) 42 g of CHO only ( n = 15). Additionally, venous blood was drawn 24 h following the first and second lifting bouts and 48 h following the third bout to assess serum myoglobin concentrations, and a visual analog scale was utilized prior, during, and after the 3-d protocol to measure subjective perceptions of muscular soreness.

          Results

          There were similar decrements in 1RM squat strength and isokinetic peak torque measures in the BCAA-CHO and CHO groups. Serum myoglobin concentrations ( p = 0.027) and perceived muscle soreness ( p < 0.001) increased over the intervention regardless of supplementation. A group*time interaction was observed for monocyte percentages ( p = 0.01) whereby BCAA-CHO supplementation attenuated increases in this variable over the duration of the protocol compared to CHO supplementation.

          Conclusion

          BCAA-CHO supplementation did not reduce decrements in lower body strength or improve select markers of muscle damage/soreness compared to CHO supplementation over three consecutive days of intense lower-body training.

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          Most cited references34

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          Exercise-Induced Muscle Damage in Humans

          Exercise-induced muscle injury in humans frequently occurs after unaccustomed exercise, particularly if the exercise involves a large amount of eccentric (muscle lengthening) contractions. Direct measures of exercise-induced muscle damage include cellular and subcellular disturbances, particularly Z-line streaming. Several indirectly assessed markers of muscle damage after exercise include increases in T2 signal intensity via magnetic resonance imaging techniques, prolonged decreases in force production measured during both voluntary and electrically stimulated contractions (particularly at low stimulation frequencies), increases in inflammatory markers both within the injured muscle and in the blood, increased appearance of muscle proteins in the blood, and muscular soreness. Although the exact mechanisms to explain these changes have not been delineated, the initial injury is ascribed to mechanical disruption of the fiber, and subsequent damage is linked to inflammatory processes and to changes in excitation-contraction coupling within the muscle. Performance of one bout of eccentric exercise induces an adaptation such that the muscle is less vulnerable to a subsequent bout of eccentric exercise. Although several theories have been proposed to explain this "repeated bout effect," including altered motor unit recruitment, an increase in sarcomeres in series, a blunted inflammatory response, and a reduction in stress-susceptible fibers, there is no general agreement as to its cause. In addition, there is controversy concerning the presence of sex differences in the response of muscle to damage-inducing exercise. In contrast to the animal literature, which clearly shows that females experience less damage than males, research using human studies suggests that there is either no difference between men and women or that women are more prone to exercise-induced muscle damage than are men.
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            Muscle function after exercise-induced muscle damage and rapid adaptation.

            This brief review focuses on the time course of changes in muscle function and other correlates of muscle damage following maximal effort eccentric actions of the forearm flexor muscles. Data on 109 subjects are presented to describe an accurate time course of these changes and attempt to establish relationships among the measures. Peak soreness is experienced 2-3 d postexercise while peak swelling occurs 5 d postexercise. Maximal strength and the ability to fully flex the arm show the greatest decrements immediately after exercise with a linear restoration of these functions over the next 10 d. Blood creatine kinase (CK) levels increase precipitously at 2 d after exercise which is also the time when spontaneous muscle shortening is most pronounced. Whether the similarity in the time courses of some of these responses implies that they are caused by similar factors remains to be determined. Performance of one bout of eccentric exercise produces an adaptation such that the muscle is more resistant to damage from a subsequent bout of exercise. The length of the adaptation differs among the measures such that when the exercise regimens are separated by 6 wk, all measures show a reduction in response on the second, compared with the first, bout. After 10 wk, only CK and muscle shortening show a reduction in response. After 6 months only the CK response is reduced. A combination of cellular factors and neurological factors may be involved in the adaptation process.
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              Signaling pathways involved in translational control of protein synthesis in skeletal muscle by leucine.

              Numerous reports established that in skeletal muscle the indispensable branched-chain amino acid leucine is unique in its ability to initiate signal transduction pathways that modulate translation initiation. Oral administration of leucine stimulates protein synthesis in association with hyperphosphorylation of the translational repressor, eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), resulting in enhanced availability of the mRNA cap-binding protein eIF4E, for binding eIF4G and forming the active eIF4F complex. In addition, leucine enhances phosphorylation of the 70-kDa ribosomal protein S6 kinase (S6K1). These results suggest that leucine upregulates protein synthesis in skeletal muscle by enhancing both the activity and synthesis of proteins involved in mRNA translation. The stimulatory effects of leucine on translation initiation are mediated in part through the protein kinase mammalian target of rapamycin (mTOR), where both insulin signaling and leucine signaling converge to promote a maximal response.
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                Author and article information

                Contributors
                wck0007@auburn.edu
                pwm0009@auburn.edu
                aem0026@auburn.edu
                amh0078@auburn.edu
                jjs0016@auburn.edu
                moblecb@auburn.edu
                aej0015@auburn.edu
                weimawh@auburn.edu
                gdo0001@auburn.edu
                kyoung@auburn.vcom.edu
                drjordanmoon@gmail.com
                334-844-1925 , mdr0024@auburn.edu
                Journal
                J Int Soc Sports Nutr
                J Int Soc Sports Nutr
                Journal of the International Society of Sports Nutrition
                BioMed Central (London )
                1550-2783
                26 July 2016
                26 July 2016
                2016
                : 13
                : 30
                Affiliations
                [1 ]School of Kinesiology, Molecular and Applied Sciences Laboratory, Auburn University, 301 Wire Road, Office 286, Auburn, AL 36849 USA
                [2 ]Edward Via College of Osteopathic Medicine – Auburn Campus, Auburn, AL USA
                [3 ]American Public University System, School of Health Sciences, Charles Town, WV USA
                Article
                142
                10.1186/s12970-016-0142-y
                4962429
                27468258
                0539c54e-e427-46b8-ab04-eb84b99045dc
                © The Author(s). 2016

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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
                : 26 August 2015
                : 19 July 2016
                Funding
                Funded by: MusclePharm
                Categories
                Research Article
                Custom metadata
                © The Author(s) 2016

                Sports medicine
                branched chain amino acids,resistance training,muscle damage,immune system
                Sports medicine
                branched chain amino acids, resistance training, muscle damage, immune system

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