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In this blog, I'll be sharing posts on BCAAs including from knowledge and experience worldwide.
Furthermore, BCAA supplementation before and after exercise has beneficial effects for decreasing exercise-induced muscle damage and promoting muscle-protein synthesis; this suggests the possibility that BCAAs are a useful supplement in relation to exercise and sports.
The branched-chain amino acids (BCAAs) 3 leucine, iso-leucine, and valine are among the nine essential amino acids for humans and account for ;35% of the essential amino acids in muscle proteins and ;40% of the preformed amino acids required by mammals (1). Because animal and human cells have a tightly controlled enzymatic system for BCAA degradation, BCAAs that are ingested in excess are quickly disposed of (2). Although BCAAs are absolutely required for protein synthesis, some intermediates formed in their catabo-lism [e.g., branched-chain a-keto acids (BCKA)] can be toxic at high concentrations (1). Therefore, the disposal of excess BCAAs is critically important for maintaining normal body conditions.
It is known that BCAAs can be oxidized in skeletal muscle, whereas other essential amino acids are catabolized [ca·tab·o·lism (k -t b -l z m). n. The metabolic breakdown of complex molecules into simpler ones, often resulting in a release of energy] mainly in liver (3). Exercise greatly increases energy expenditure and promotes oxidation of BCAAs (3). It is believed that BCAAs contribute to energy metabolism during exercise as energy sources and substrates to expand the pool of citric acid–cycle intermediates (anaplerosis) and for gluconeogenesis. In contrast, leucine is special among the BCAAs, because it promotes muscle-protein synthesis in vivo when orally administered to animals (4).
As a consequence of these findings, BCAAs are receiving considerable attention as potentially helpful dietary supplements for individuals who enjoy exercise and participate in sports.
Toxicity of BCAA. Acute and subacute toxicity studies of BCAAs using mice and rats (30) and a chronic toxicity study using rats (31) were reported. The BCAA composition used in these studies was a 2.1:1:1.2 leucine : isoleucine : valine ratio. No animals died from the single dose of 10 g of BCAA/kg body wt in the acute toxicity study, and the half-maximal lethal dose was estimated as .10 g/kg body wt. No toxic effects of BCAAs were observed at a dose of 2.5 g/kg/day for 3 mo or 1.25 g/kg/day for 1 y. There are no reports concerning BCAA toxicity in relation to exercise and sports.
It is clear that exercise promotes degradation of BCAAs. Promotion of fatty acid oxidation appears to be associated with greater rates of BCAA oxidation, which suggests that fatty acids may be regulators of BCAA oxidation. Furthermore, muscle-protein synthesis is enhanced after exercise. From these findings, it may be concluded that the BCAA requirement is increased by exercise.
BCAA supplementation before and after exercise has beneficial effects for decreasing exercise-induced muscle damage and promoting muscle-protein synthesis; this suggests that BCAAs may be a useful supplement in relation to exercise and sports.
Although in many human exercise studies, a dose of .5 g of BCAA was used as a supplement, the minimum dose to produce the beneficial effects of BCAA supplementation remains to be established.
Furthermore, the most effective ratio of the three BCAAs is unclear. Toxicity studies of BCAAs using animals showed that BCAAs are quite safe amino acids when the three BCAAs are provided in a ratio similar to that of animal protein (e.g., a 2:1:1 leucine : isoleucine : valine ratio). Although leucine is the most potent amino acid among the BCAAs for stimulating protein synthesis, supplementation of leucine alone may cause BCAA imbalance via the activating effect of its keto acid on the BCKDH complex.
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These results demonstrate that BCAA supplementation during an intensive training program effectively reduces the muscle soreness and fatigue sensation, and that the perceived changes could be attributed to the attenuation of muscle damage and inflammation.
Branched-chain amino acid ingestion can ameliorate soreness from eccentric exercise.
These results suggest that muscle damage may be suppressed by BCAA supplementation.
BCAA supplementation increased the plasma BCAA concentration during the exercise test, while plasma BCAA concentration decreased in the placebo trial. The RER during the exercise test in the BCAA trial was lower than that in the placebo trial (p<0.05). The VO2 and workload levels at LT point in the BCAA trial were higher than those in the placebo trial (VO2: 29.8+/-6.8 vs. 26.4+/-5.4 mL/kg/min; workload: 175+/-42 vs. 165+/-38 W, p<0.05, respectively). The VO2max in the BCAA trial was higher than that in the placebo trial (47.1+/-5.7 vs. 45.2+/-5.0 mL/kg/min, p<0.05). These results suggest that BCAA supplementation may be effective to increase the endurance exercise capacity.
The purpose of this study was to investigate whether short-term amino acid supplementation could maintain a short-term net anabolic hormonal profile and decrease muscle cell damage during a period of high-intensity resistance training (overreaching), thereby enhancing recovery and decreasing the risk of injury and illness. Eight previously resistance trained males were randomly assigned to either a high branched chain amino acids (BCAA) or placebo group. Subjects consumed the supplement for 3 weeks before commencing a fourth week of supplementation with concomitant high-intensity total-body resistance training (overreaching) (3 x 6-8 repetitions maximum, 8 exercises). Blood was drawn prior to and after supplementation, then again after 2 and 4 days of training. Serum was analyzed for testosterone, cortisol, and creatine kinase. Serum testosterone levels were significantly higher (p < 0.001), and cortisol and creatine kinase levels were significantly lower (p < 0.001, and p = 0.004, respectively) in the BCAA group during and following resistance training. These findings suggest that short-term amino acid supplementation, which is high in BCAA, may produce a net anabolic hormonal profile while attenuating training-induced increases in muscle tissue damage.
Athletes' nutrient intake, which periodically increases amino acid intake to reflect the increased need for recovery during periods of overreaching, may increase subsequent competitive performance while decreasing the risk of injury or illness.
Too Much Protein, Eaten Along With Fat, May Lead To Insulin Resistance
"Insulin resistance occurred in animals with a diet high in the branched-chain amino acids, but only if they were ingested along with a high level of fat in the diet," Newgard said. Because obese humans tend to ingest high-fat diets, the combination of high-BCAA and high-fat intake might contribute to insulin resistance in obese humans, but additional studies are needed. BCAAs comprise as much as 25 percent of amino acids in dietary protein, and are particularly enriched in diets high in animal (meat) proteins.
"I want to be clear that our animal data suggest that there is nothing wrong with obtaining protein from sources that are high in branched-chain amino acids, as long as you are not eating beyond what your energy needs are," said Newgard, who is a professor of pharmacology and cancer biology and professor of medicine at Duke. "If you add a lot of unneeded protein to a fatty diet, perhaps that's where you get into problems. The ancient Greeks were right: everything in moderation."
Insulin resistance happens when insulin, released by the beta cells in the pancreas, doesn't work normally to stimulate glucose uptake into tissues.