scholarly journals Potential therapeutic effects of branched-chain amino acids supplementation on resistance exercise-based muscle damage in humans

2011 ◽  
Vol 8 (1) ◽  
Author(s):  
Claudia R da Luz ◽  
Humberto Nicastro ◽  
Nelo E Zanchi ◽  
Daniela FS Chaves ◽  
Antonio H Lancha
Keyword(s):  
Amino Acids ◽  
Resistance Exercise ◽  
Muscle Damage ◽  
Branched Chain Amino Acids ◽  
Therapeutic Effects ◽  
Branched Chain

scholarly journals Branched-chain amino acids do not improve muscle recovery from resistance exercise in untrained young adults

Amino Acids ◽  
2019 ◽  
Vol 51 (9) ◽  
pp. 1387-1395 ◽  
Author(s):  
José Maria Estoche ◽  
Jeferson Lucas Jacinto ◽  
Mirela Casonato Roveratti ◽  
Juliano Moro Gabardo ◽  
Cosme Franklim Buzzachera ◽  
...  
Keyword(s):  
Amino Acids ◽  
Young Adults ◽  
Resistance Exercise ◽  
Branched Chain Amino Acids ◽  
Muscle Recovery ◽  
Branched Chain

scholarly journals Associations between Plasma Branched Chain Amino Acids and Health Biomarkers in Response to Resistance Exercise Training Across Age

Nutrients ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 3029
Author(s):  
Mariwan H. Sayda ◽  
Bethan E. Phillips ◽  
John P. Williams ◽  
Paul L. Greenhaff ◽  
Daniel J. Wilkinson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Exercise Training ◽  
Resistance Exercise ◽  
Branched Chain Amino Acids ◽  
Metabolic Health ◽  
Whole Body ◽  
Gas Chromatography Mass Spectrometry ◽  
Resistance Exercise Training ◽  
Fasting Plasma ◽  
Branched Chain

Leucine, isoleucine and valine (i.e., the branched chain amino acids, BCAA) play a key role in the support of tissue protein regulation and can be mobilized as energy substrates during times of starvation. However, positive relationships exist between elevated levels of BCAA and insulin resistance (IR). Thus, we sought to investigate the links between fasting plasma BCAA following a progressive resistance exercise training (RET) programme, an intervention known to improve metabolic health. Fasting plasma BCAA were quantified in adults (young: 18–28 y, n = 8; middle-aged: 45–55 y, n = 9; older: 65–75 y, n = 15; BMI: 23–28 kg/m2, both males and females (~50:50), in a cross-sectional, intervention study. Participants underwent 20-weeks whole-body RET. Measurements of body composition, muscle strength (1-RM) and metabolic health biomarkers (e.g., HOMA-IR) were made at baseline and post-RET. BCAA concentrations were determined by gas-chromatography mass spectrometry (GC-MS). No associations were observed across age with BCAA; however, RET elicited (p < 0.05) increases in plasma BCAA (all age-groups), while HOMA-IR scores reduced (p < 0.05) following RET. After RET, positive correlations in lean body mass (p = 0.007) and strength gains (p = 0.001) with fasting BCAA levels were observed. Elevated BCAA are not a robust marker of ageing nor IR in those with a healthy BMI; rather, despite decreasing IR, RET was associated with increased BCAA.

Branched-chain Amino Acids and Alleviation of Muscle Damage and Fatigue in the Hyper-running Rat Model

2007 ◽  
Vol 39 (Supplement) ◽  
pp. S364 ◽  
Author(s):  
Maki Okada ◽  
Makoto Bannai ◽  
Michio Takahashi ◽  
Masaru Ohtani ◽  
Kimiaki Maruyama
Keyword(s):  
Amino Acids ◽  
Muscle Damage ◽  
Rat Model ◽  
Branched Chain Amino Acids ◽  
Branched Chain

scholarly journals Dose-dependent increases in p70S6K phosphorylation and intramuscular branched-chain amino acids in older men following resistance exercise and protein intake

2014 ◽  
Vol 2 (8) ◽  
pp. e12112 ◽  
Author(s):  
Randall F. D'Souza ◽  
James F. Markworth ◽  
Vandre C. Figueiredo ◽  
Paul A. Della Gatta ◽  
Aaron C. Petersen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Resistance Exercise ◽  
Protein Intake ◽  
Older Men ◽  
Branched Chain Amino Acids ◽  
Branched Chain ◽  
Dose Dependent

Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise

2004 ◽  
Vol 287 (1) ◽  
pp. E1-E7 ◽  
Author(s):  
Håkan K. R. Karlsson ◽  
Per-Anders Nilsson ◽  
Johnny Nilsson ◽  
Alexander V. Chibalin ◽  
Juleen R. Zierath ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Kinase ◽  
Resistance Exercise ◽  
P38 Mapk ◽  
Recovery Period ◽  
Plasma Concentrations ◽  
Branched Chain Amino Acids ◽  
Mitogen Activated Protein Kinase ◽  
Branched Chain

The aim of the study was to investigate the effect of resistance exercise alone or in combination with oral intake of branched-chain amino acids (BCAA) on phosphorylation of the 70-kDa S6 protein kinase (p70S6k) and mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase (ERK1/2), and p38 MAPK in skeletal muscle. Seven male subjects performed one session of quadriceps muscle resistance training (4 × 10 repetitions at 80% of one repetition maximum) on two occasions. In a randomized order, double-blind, crossover test, subjects ingested a solution of BCAA or placebo during and after exercise. Ingestion of BCAA increased plasma concentrations of isoleucine, leucine, and valine during exercise and throughout recovery after exercise (2 h postexercise), whereas no change was noted after the placebo trial. Resistance exercise led to a robust increase in p70S6k phosphorylation at Ser424 and/or Thr421, which persisted 1 and 2 h after exercise. BCAA ingestion further enhanced p70S6k phosphorylation 3.5-fold during recovery. p70S6k phosphorylation at Thr389 was unaltered directly after resistance exercise. However, during recovery, Thr389 phosphorylation was profoundly increased, but only during the BCAA trial. Furthermore, phosphorylation of the ribosomal protein S6 was also increased in the recovery period only during the BCAA trial. Exercise led to a marked increase in ERK1/2 and p38 MAPK phosphorylation, which was completely suppressed upon recovery and unaltered by BCAA. In conclusion, BCAA, ingested during and after resistance exercise, mediate signal transduction through p70S6k in skeletal muscle.

Intake of branched-chain amino acids influences the levels of MAFbx mRNA and MuRF-1 total protein in resting and exercising human muscle

2012 ◽  
Vol 302 (5) ◽  
pp. E510-E521 ◽  
Author(s):  
Marcus Borgenvik ◽  
William Apró ◽  
Eva Blomstrand
Keyword(s):  
Amino Acids ◽  
Resistance Exercise ◽  
Total Protein ◽  
Muscle Protein ◽  
Recovery Period ◽  
Branched Chain Amino Acids ◽  
Vastus Lateralis Muscle ◽  
Early Recovery ◽  
Placebo Condition ◽  
Branched Chain

Resistance exercise and amino acids are two major factors that influence muscle protein turnover. Here, we examined the effects of resistance exercise and branched-chain amino acids (BCAA), individually and in combination, on the expression of anabolic and catabolic genes in human skeletal muscle. Seven subjects performed two sessions of unilateral leg press exercise with randomized supplementation with BCAA or flavored water. Biopsies were collected from the vastus lateralis muscle of both the resting and exercising legs before and repeatedly after exercise to determine levels of mRNA, protein phosphorylation, and amino acid concentrations. Intake of BCAA reduced ( P < 0.05) MAFbx mRNA by 30 and 50% in the resting and exercising legs, respectively. The level of MuRF-1 mRNA was elevated ( P < 0.05) in the exercising leg two- and threefold under the placebo and BCAA conditions, respectively, whereas MuRF-1 total protein increased by 20% ( P < 0.05) only in the placebo condition. Phosphorylation of p70S6k increased to a larger extent (∼2-fold; P < 0.05) in the early recovery period with BCAA supplementation, whereas the expression of genes regulating mTOR activity was not influenced by BCAA. Muscle levels of phenylalanine and tyrosine were reduced (13–17%) throughout recovery ( P < 0.05) in the placebo condition and to a greater extent (32–43%; P < 0.05) following BCAA supplementation in both resting and exercising muscle. In conclusion, BCAA ingestion reduced MAFbx mRNA and prevented the exercise-induced increase in MuRF-1 total protein in both resting and exercising leg. Further-more, resistance exercise differently influenced MAFbx and MuRF-1 mRNA expression, suggesting both common and divergent regulation of these two ubiquitin ligases.

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