ArticlePhysiological reports2019
Depletion of branched-chain aminotransferase 2 (BCAT2) enzyme impairs myoblast survival and myotube formation.
Article in Physiological reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Disrupting SRSF10-dependent BCAT2 exon skipping reprograms tumor-associated macrophages and enhances anti-PD-1 efficacy in gastric cancer.Cell death & disease · 2026Article
- The cytosolic branched-chain amino transferase 1 (BCAT1/BCATc) inhibitor reduces mitochondrial capacity in a myotube model of insulin resistance.Journal of endocrinological investigation · 2025Article
- High doses of rosuvastatin induce impaired branched-chain amino acid catabolism and lead to insulin resistance.Experimental physiology · 2023Article
- The mechanism of branched-chain amino acid transferases in different diseases: Research progress and future prospects.Frontiers in oncology · 2022Review
- Higher glucose availability augments the metabolic responses of the C2C12 myotubes to exercise-like electrical pulse stimulation.American journal of physiology. Endocrinology and metabolism · 2021Article
- Phenylbutyrate, a branched-chain amino acid keto dehydrogenase activator, promotes branched-chain amino acid metabolism and induces muscle catabolism in C2C12 cells.Experimental physiology · 2021Article
- Branched-chain Amino Acids: Catabolism in Skeletal Muscle and Implications for Muscle and Whole-body Metabolism.Frontiers in physiology · 2021Review
- Putative Genes and Pathways Involved in the Acne Treatment of Isotretinoin via Microarray Data Analyses.BioMed research international · 2020Article
- Depletion of branched-chain aminotransferase 2 (BCAT2) enzyme impairs myoblast survival and myotube formation.Physiological reports · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Much is known about the positive effects of branched-chain amino acids (BCAA) in regulating muscle protein metabolism. Comparatively much less is known about the effects of these amino acids and their metabolites in regulating myotube formation. Using cultured myoblasts, we showed that although leucine is required for myotube formation, this requirement is easily met by α-ketoisocaproic acid, the ketoacid of leucine. We then demonstrated increases in the expression of the first two enzymes in the catabolism of the three BCAA, branched-chain amino transferase (BCAT2) and branched-chain α-ketoacid dehydrogenase (BCKD), with ~3× increase in BCKD protein expression (p < .05) during differentiation. Furthermore, depletion of BCAT2 abolished myoblast differentiation, as indicated by reduction in the levels of myosin heavy chain-1, troponin and myogenin. Supplementation of incubation medium with branched-chain α-ketoacids or related metabolites derivable from BCAT2 functions did not rescue the defects. However, co-depletion of BCKD kinase partially rescued the defects. Collectively, our data indicate a requirement for BCAA catabolism during myotube formation and that this requirement for BCAT2 likely goes beyond the need for this enzyme to generate the α-ketoacids of the BCAA.
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