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Adam D. Osmond, Dean J. Directo, Marcus L. Elam, Gabriela Juache, Vince C. Kreipke, Desiree E. Saralegui, Robert Wildman, Michael Wong and Edward Jo

, and active rest, have been widely implemented by athletes and exercising individuals. Several prior investigations support the use of supplementary branched-chain amino acids (BCAA) as a nutritional countermeasure to EIMD or related symptoms. When compared with nutritive (eg, carbohydrate) and

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Dariush Sheikholeslami-Vatani, Slahadin Ahmadi and Hassan Faraji

et al., 2013 ) and ROS production ( Yu et al., 2009 ). By contrast, branched-chain amino acids (BCAA), including isoleucine, leucine, and valine, have unique properties that play important metabolic and physiological roles in all living organisms. It is also found that BCAA might affect gene

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J. Mark Davis

The mechanisms of central fatigue are largely unexplored, but the central fatigue hypothesis suggests that increased brain serotonin (5-HT) can cause a deterioration in sport and exercise performance. There is now convincing evidence that exercise-induced increases in the plasma free tryptophan (f-TRP)/branched-chain amino acids (BCCA) ratio are associated with increased brain 5-HT and the onset of fatigue during prolonged exercise. Furthermore, when drugs are administered to alter brain 5-HT, they have the predicted effects on exercise performance. The influence of nutritional manipulations of f-TRP/BCCA on performance is less well established. The effects of BCCA supplementation on exercise performance are mixed, and the published studies often suffer from methodological flaws. Alternatively, dramatic reductions in f-TRP/BCCA and enhanced performance accompany carbohydrate feedings during prolonged exercise. However, it is difficult to distinguish between the effects of carbohydrate feedings on mechanisms that reside in the brain versus the muscles themselves.

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André X. Bigard, Pierre Lavier, Lionel Ullmann, Hélène Legrand, Philippe Douce and Charles Y. Guezennec

This study was conducted to test the hypothesis that a branched-chain amino acid (BCAA) supplementation would minimize changes in body composition and alterations in plasma amino acid profile induced by prolonged exercises at altitude. Twenty-four highly trained subjects participated in six successive sessions of ski mountaineering (6-8 hr duration, altitude 2,500-4,100 m). Twelve subjects took a dietary supplement of BCAA (BCAA group) and 12 took a dietary supplement that was 98% carbohydrate (C group). Body weight decreased in C subjects (-2.1%,p < .01), while the body weight loss recorded in the BCAA group was not statistically significant (-1.2%, NS). Changes in body composition that resulted from repeated skiing exercise at altitude were not significantly minimized by BCAA administration. Peak power output recorded during an incremental bicycle exercise decreased in C subjects but did not change significantly in BCAA subjects. Results of this study demonstrate that neither changes in body composition related to the ski mountaineering program nor muscular performance during isometric contraction was significantly affected by BCAA administration.

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Yoshiharu Shimomura, Asami Inaguma, Satoko Watanabe, Yuko Yamamoto, Yuji Muramatsu, Gustavo Bajotto, Juichi Sato, Noriko Shimomura, Hisamine Kobayashi and Kazunori Mawatari

The authors examined the effect of branched-chain amino acid (BCAA) supplementation on squat-exercise-induced delayed-onset muscle soreness (DOMS) using 12 young, healthy, untrained female participants. The experiment was conducted with a crossover double-blind design. In the morning on the exercise-session day, the participants ingested either BCAA (isoleucine:leucine:valine = 1:2.3:1.2) or dextrin at 100 mg/kg body weight before the squat exercise, which consisted of 7 sets of 20 squats/set with 3-min intervals between sets. DOMS showed a peak on Days 2 and 3 in both trials, but the level of soreness was significantly lower in the BCAA trial than in the placebo. Leg-muscle force during maximal voluntary isometric contractions was measured 2 d after exercise (Day 3), and the BCAA supplementation suppressed the muscle-force decrease (to ~80% of the value recorded under the control conditions) observed in the placebo trial. Plasma BCAA concentrations, which decreased after exercise in the placebo trial, were markedly elevated during the 2 hr postexercise in the BCAA trial. Serum myoglobin concentration was increased by exercise in the placebo but not in the BCAA trial. The concentration of plasma elastase as an index of neutrophil activation appeared to increase after the squat exercise in both trials, but the change in the elastase level was significant only in the placebo trial. These results suggest that muscle damage may be suppressed by BCAA supplementation.

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Beau Kjerulf Greer, John L. Woodard, Jim P. White, Eric M. Arguello and Emily M. Haymes

The purpose of this study was to determine whether branched-chain amino acid (BCAA) supplementation attenuates indirect indicators of muscle damage during endurance exercise as compared with an isocaloric, carbohydrate (CHO) beverage or a noncaloric placebo (PLAC) beverage. Nine untrained men performed three 90-min cycling bouts at 55% VO2peak. Subjects, blinded to beverage selection, ingested a total of 200 kcal of energy via the CHO or BCAA beverage before and at 60 min of exercise, or they drank the PLAC beverage. Creatine kinase (CK), lactate dehydrogenase (LDH), isokinetic leg-extension and fexion torque, and muscle soreness were assessed before and immediately, 4 h, 24 h, and 48 h post exercise. The trials were separated by 8 wk. CK activities were significantly lower after the BCAA trial than in the PLAC trial at 4, 24, and 48 h post exercise, as well as lower than the CHO beverage at 24 h post exercise. CK was lower in the CHO trial at the 24- and 48-h time points than in the PLAC trial. LDH activities were lower in the BCAA trial at 4 h than in the PLAC trial. As compared with the CHO and PLAC trials, ratings of perceived soreness were lower at 24 h post exercise, and leg-fexion torque was higher at the 48-h time point after the BCAA trial. The present data suggest that BCAA supplementation attenuates muscle damage during prolonged endurance exercise in untrained college-age men. CHO ingestion attenuates CK activities at 24 and 48 h post exercise as compared with a placebo beverage.

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Scott C. Forbes, Linda McCargar, Paul Jelen and Gordon J. Bell

The purpose was to investigate the effects of a controlled typical 1-day diet supplemented with two different doses of whey protein isolate on blood amino acid profiles and hormonal concentrations following the final meal. Nine males (age: 29.6 ± 6.3 yrs) completed four conditions in random order: a control (C) condition of a typical mixed diet containing ~10% protein (0.8 g·kg–1), 65% carbohydrate, and 25% fat; a placebo (P) condition calorically matched with carbohydrate to the whey protein conditions; a low-dose condition of 0.8 grams of whey protein isolate per kilogram body mass per day (g·kg–1·d–1; W1) in addition to the typical mixed diet; or a high-dose condition of 1.6 g·kg–1·d–1 (W2) of supplemental whey protein in addition to the typical mixed diet. Following the final meal, significant (p < .05) increases in total amino acids, essential amino acids (EAA), branch-chained amino acids (BCAA), and leucine were observed in plasma with whey protein supplementation while no changes were observed in the control and placebo conditions. There was no significant group difference for glucose, insulin, testosterone, cortisol, or growth hormone. In conclusion, supplementing a typical daily food intake consisting of 0.8 g of protein·kg–1·d–1 with a whey protein isolate (an additional 0.8 or 1.6 g·kg–1·d–1) significantly elevated total amino acids, EAA, BCAA, and leucine but had no effect on glucose, insulin, testosterone, cortisol, or growth hormone following the final meal. Future acute and chronic supplementation research examining the physiological and health outcomes associated with elevated amino acid profiles is warranted.

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Romain Meeusen and Lieselot Decroix

opportunity to manipulate the central nervous system through changes in diet or supplementation with specific nutrients, including amino acids such as branched-chain amino acids (BCAAs), tyrosine, carbohydrates (CHO), and caffeine (Table  1 ). Table 1 Overview of the Effect of Nutritional Supplements on

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Amy J. Hector and Stuart M. Phillips

stimulators of MPS ( Tang et al., 2009 ). Indeed, during dietary energy restriction, whey protein (a fast-digested protein derived from milk that contains a high proportion of the branched chain amino acid leucine) ingestion resulted in a robust increase in MPS that was significantly higher than consumption

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Samuel G. Impey, Kelly M. Hammond, Robert Naughton, Carl Langan-Evans, Sam O. Shepherd, Adam P. Sharples, Jessica Cegielski, Kenneth Smith, Stewart Jeromson, David L. Hamilton, Graeme L. Close and James P. Morton

 = .058) but no effect of condition ( p  = .968). Figure 3 —mRNA expression of (a) PGC-1α, (b) p53, (c) Parkin, and (d) Beclin1. * p  < .05 significant difference from preexercise. Plasma Amino Acids, Serum Insulin, and p70S6K1-Related Signaling Plasma leucine, branched chain amino acids, and essential