Eight males were recruited to examine the effect of branched-chain amino acid (BCAA) supplementation on exercise capacity in a glycogen-depleted state in a warm environment. Following a exercise and dietary regimen designed to reduce glycogen availability, subjects returned to the laboratory the following morning and remained seated for 2 h, before cycling to volitional exhaustion at 50% VO2 peak in a warm environment [30.0 (0.2) degrees C; mean (SD)]. Four 250 ml aliquots of a 12 g l(-1) BCAA solution or placebo were ingested at 30 min intervals prior to exercise, with an additional 150 ml consumed every 15 min throughout exercise. BCAA ingestion had no effect on exercise capacity [placebo 103.9 (26.9) min; BCAA 111.0 (29.2) min; P = 0.129). No difference in heart rate (P = 0.345), core temperature (P = 0.628), or weighted mean skin temperature (P = 0.114) was apparent between trials. Ingestion of the BCAA solution produced a marked increase in plasma BCAA immediately prior to exercise [+ 1126 (158) micromol l(-1); P < 0.001) with this difference maintained throughout. Consequently, a significant reduction in the plasma concentration ratio of free tryptophan to BCAA was observed during the BCAA trial when compared to the placebo (P < 0.001). Plasma ammonia concentration was significantly elevated during exercise throughout the BCAA trial (P < 0.001), with no change from rest apparent during the placebo trial (P = 0.608). Blood glucose (P = 0.114) and lactate (P = 0.836) concentrations were not different between trials. Ingestion of a BCAA solution prior to, and during, prolonged exercise in glycogen-depleted subjects did not influence exercise capacity in a warm environment.

Exercise raises brain serotonin release and is postulated to cause fatigue in athletes; ingestion of branched-chain amino acids (BCAA), by competitively inhibiting tryptophan transport into brain, lowers brain tryptophan uptake and serotonin synthesis and release in rats, and reputedly in humans prevents exercise-induced increases in serotonin and fatigue. This latter effect in humans is disputed. But BCAA also competitively inhibit tyrosine uptake into brain, and thus catecholamine synthesis and release. Since increasing brain catecholamines enhances physical performance, BCAA ingestion could lower catecholamines, reduce performance and thus negate any serotonin-linked benefit. We therefore examined in rats whether BCAA would reduce both brain tryptophan and tyrosine concentrations and serotonin and catecholamine synthesis. Sedentary and exercising rats received BCAA or vehicle orally; tryptophan and tyrosine concentrations and serotonin and catecholamine synthesis rates were measured 1 h later in brain. BCAA reduced brain tryptophan and tyrosine concentrations, and serotonin and catecholamine synthesis. These reductions in tyrosine concentrations and catecholamine synthesis, but not tryptophan or serotonin synthesis, could be prevented by co-administering tyrosine with BCAA. Complete essential amino acid mixtures, used to maintain or build muscle mass, were also studied, and produced different effects on brain tryptophan and tyrosine concentrations and serotonin and catecholamine synthesis. Since pharmacologically increasing brain catecholamine function improves physical performance, the finding that BCAA reduce catecholamine synthesis may explain why this treatment does not enhance physical performance in humans, despite reducing serotonin synthesis. If so, adding tyrosine to BCAA supplements might allow a positive action on performance to emerge.

an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole Tryptophan (symbol Trp or W), historically also known as tryptophane, is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vit A common assertion in the US and the UK is that heavy consumption of turkey meat—as seen during Thanksgiving and Christmas—results in drowsiness, due to high levels of tryptophan contained in turkey. However, the amount of tryptophan in turkey is comparable with that of other meats. Drowsiness after eating may be caused by other foods eaten with the turkey, particularly carbohydrates. Ingestion of a meal rich in carbohydrates triggers the release of insulin. Insulin in turn stimulates the uptake of large neutral branched-chain amino acids (BCAA), but not tryptophan, into muscle, increasing the ratio of tryptophan to BCAA in the blood stream. The resulting increased tryptophan ratio reduces competition at the large neutral amino acid transporter (which transports both BCAA and aromatic amino acids), resulting in more uptake of tryptophan across the blood–brain barrier into the cerebrospinal fluid (CSF). Once in the CSF, tryptophan is converted into serotonin in the raphe nuclei by the normal enzymatic pathway. The resultant serotonin is further metabolised into the hormone melatonin—which is an important mediator of the circadian rhythm—by the pineal gland. Hence, these data suggest that "feast-induced drowsiness"—or postprandial somnolence—may be the result of a heavy meal rich in carbohydrates, which indirectly increases the production of melatonin in the brain, and thereby promotes sleep.