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Suppression of myofibrillar proteolysis in chick skeletal muscles by α-ketoisocaproate

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Summary.

We previously reported that L-leucine suppresses myofibrillar proteolysis in chick skeletal muscles. In the current study, we compared the effects of L- and D-enantiomers of leucine on myofibrillar proteolysis in skeletal muscle of chicks. We also assessed whether leucine itself or its metabolite, α-ketoisocaproate (α-KIC), mediates the effects of leucine. Food-deprived (24 h) chicks were orally administered 225 mg/100 g body weight L-leucine, D-leucine or α-KIC and were sacrificed after 2 h. L-Leucine administration had an obvious inhibitory effect on myofibrillar proteolysis (plasma Nτ-methylhistidine concentration) in chicks while D-leucine and α-KIC were much more effective. We also examined the expression of the proteolytic-related genes (ubiquitin, proteasome, m-calpain and cathepsin B) by real-time PCR of cDNA in chick skeletal muscles. Ubiquitin mRNA expression was decreased by D-leucine and α-KIC but not L-leucine. Proteasome and m-calpain mRNA expressions as well as cathepsin B mRNA expression were likewise decreased by L-leucine, D-leucine and α-KIC. These results indicate that D-leucine and α-KIC suppress proteolytic-related genes, resulting in an decrease in myofibrillar proteolysis while L-leucine is much less effective in skeletal muscle of chicks, may be explain by conversion of D-leucine to α-KIC.

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Authors and Affiliations

  1. Department of Animal Physiology and Nutrition, National Institute of Livestock and Grassland Science, Tsukuba, Japan

    K. Nakashima, Y. Yakabe, A. Ishida, M. Yamazaki & H. Abe

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  1. K. Nakashima
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  2. Y. Yakabe
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  3. A. Ishida
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  4. M. Yamazaki
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  5. H. Abe
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Nakashima, K., Yakabe, Y., Ishida, A. et al. Suppression of myofibrillar proteolysis in chick skeletal muscles by α-ketoisocaproate. Amino Acids 33, 499–503 (2007). https://doi.org/10.1007/s00726-006-0404-0

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  • DOI: https://doi.org/10.1007/s00726-006-0404-0

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