Nutraceutical Effects of Branched-Chain Amino Acids on Skeletal Muscle

BCAA catabolism in skeletal muscle is regulated by the branched-chain [alpha]-keto acid dehydrogenase (BCKDH) complex, located at the second step in the BCAA catabolic pathway. The activity of the BCKDH complex is regulated by a phosphorylation/dephosphorylation cycle. Almost all of BCKDH complex in...

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Bibliographic Details
Published in:The Journal of nutrition 2006-02, Vol.136 (2), p.529S-532S
Main Authors: Shimomura, Yoshiharu, Yamamoto, Yuko, Bajotto, Gustavo, Sato, Juichi, Murakami, Taro, Shimomura, Noriko, Kobayashi, Hisamine, Mawatari, Kazunori
Format: Article
Language:English
Subjects:
3-methyl-2-oxobutanoate dehydrogenase (lipoamide)
3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) - metabolism
amino acid metabolism
amino acid requirements
Amino Acids, Branched-Chain - metabolism
Amino Acids, Branched-Chain - pharmacology
Animals
biochemical pathways
Biological and medical sciences
branched chain amino acids
Dietary Supplements
ergogenic aids
exercise
Exercise - physiology
Feeding. Feeding behavior
Female
functional foods
Fundamental and applied biological sciences. Psychology
human nutrition
Humans
leucine
literature reviews
Male
muscle fatigue
Muscle Fatigue - drug effects
muscle protein
Muscle Proteins - metabolism
Muscle, Skeletal - drug effects
Muscle, Skeletal - metabolism
Nutritional Physiological Phenomena
Organ Specificity
Pain - diet therapy
protein degradation
protein synthesis
Rats
skeletal muscle
Striated muscle. Tendons
Vertebrates: anatomy and physiology, studies on body, several organs or systems
Vertebrates: osteoarticular system, musculoskeletal system
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Summary:BCAA catabolism in skeletal muscle is regulated by the branched-chain [alpha]-keto acid dehydrogenase (BCKDH) complex, located at the second step in the BCAA catabolic pathway. The activity of the BCKDH complex is regulated by a phosphorylation/dephosphorylation cycle. Almost all of BCKDH complex in skeletal muscle under normal and resting conditions is in an inactive/phosphorylated state, which may contribute to muscle protein synthesis and muscle growth. Exercise activates the muscle BCKDH complex, resulting in enhanced BCAA catabolism. Therefore, exercise may increase the BCAA requirement. It has been reported that BCAA supplementation before exercise attenuates the breakdown of muscle proteins during exercise in humans and that leucine strongly promotes protein synthesis in skeletal muscle in humans and rats, suggesting that a BCAA supplement may attenuate muscle damage induced by exercise and promote recovery from the damage. We have examined the effects of BCAA supplementation on delayed-onset muscle soreness (DOMS) and muscle fatigue induced by squat exercise in humans. The results obtained showed that BCAA supplementation prior to squat exercise decreased DOMS and muscle fatigue occurring for a few days after exercise. These findings suggest that BCAAs may be useful for muscle recovery following exercise.
ISSN:0022-3166
1541-6100
DOI:10.1093/jn/136.2.529s