Of the 20 amino acids recognized to compose the building blocks of human protein, only three possess a branched side chain: leucine, isoleucine, and valine. Numerous supplements are sold consisting of these three amino acids, collectively known as the branched-chain amino acids (BCAA), with claims
Daniel L. Plotkin, Kenneth Delcastillo, Derrick W. Van Every, Kevin D. Tipton, Alan A. Aragon, and Brad J. Schoenfeld
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.
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
Kazunori Nosaka, P.▀ Sacco, and K.▀ Mawatari
This study investigated the effect of a supplement containing 9 essential and 3 non-essential amino acids on muscle soreness and damage by comparing two endurance exercise bouts of the elbow fexors with amino acid or placebo supplementation in a double blind crossover design. The supplement was ingested 30 min before (10 h post-fasting) and immediately after exercise (Experiment 1), or 30 min before (2-3 h after breakfast), immediately post, and 8 more occasions over 4-day post-exercise (Experiment 2). Changes in muscle soreness and indicators of muscle damage for 4 days following exercise were compared between supplement conditions using two-way ANOVA. No significant differences between conditions were evident for Experiment 1; however, plasma creatine kinase, aldolase, myoglobin, and muscle soreness were significantly lower for the amino acid versus placebo condition in Experiment 2. These results suggest that amino acid supplementation attenuates DOMS and muscle damage when ingested in recovery days.
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
Amy J. Hector and Stuart M. Phillips
only the branched-chain amino acids (BCAAs; leucine, isoleucine, and valine) has been of interest for promoting skeletal muscle anabolism and high-quality weight loss. A common concern with BCAA supplementation is the antagonism of these amino acids in competing for the BCAA transporter. Indeed
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.
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.
Louise M. Burke, Julie A Winter, David Cameron-Smith, Marc Enslen, Michelle Farnfield, and Jacques Decombaz
The authors undertook 2 crossover-designed studies to characterize plasma amino acid (AA) responses to the intake of 20 g of protein. In Study 1, 15 untrained and overnight-fasted subjects consumed 20 g protein from skim milk, soy milk, beefsteak, boiled egg, and a liquid meal supplement. In Study 2, 10 fasted endurance-trained subjects consumed 20 g protein from a protein-rich sports bar at rest and after a 60-min submaximal ride. Plasma AA concentrations were measured immediately before and for 180 min after food ingestion using a gas-chromatography flame-ionization detection technique. A pharmacokinetic analysis was undertaken for profiles of total AAs (TAA), essential AAs, branched-chain AAs (BCAA), and leucine. Although area-under-the-curve values for plasma TAA were similar across protein sources, the pattern of aminoacidemia showed robust differences between foods, with liquid forms of protein achieving peak concentrations twice as quickly after ingestion as solid protein-rich foods (e.g., ~50 min vs ~100 min) and skim milk achieving a significantly faster peak leucine concentration than all other foods (~25 min). Completing exercise before ingesting protein sources did not cause statistically significant changes in the pattern of delivery of key AAs, BCAAs, and leucine apart from a 20–40% increase in the rate of elimination. These results may be useful to plan the type and timing of intake of protein-rich foods to maximize the protein synthetic response to various stimuli such as exercise.
Mark Hargreaves and Rodney Snow
Although skeletal muscle is capable of oxidizing selected amino acids, exercise in the fed and carbohydrate-replete condition results in only a small increase in amino acid utilization. Nevertheless, it may be important to increase the dietary protein requirements of active individuals. There is ongoing debate as to whether the amino acids for oxidation are derived from the free amino acid pool, from net protein breakdown, or a combination of both. There has been interest in the potential ergogenic benefits of amino acid ingestion; however, BCAA ingestion does not appear to affect fatigue during prolonged exercise, there is little support from controlled studies to recommend glutamine ingestion for enhanced immune function, and although glutamine stimulates muscle glycogen synthesis, its addition to carbohydrate supplements provides no additional benefit over ingestion of carbohydrate alone.