Czech J. Anim. Sci., 2004, 49(4):137-143 | DOI: 10.17221/4291-CJAS

The effect of branched chain amino acids on proteosynthesis in skeletal muscles of japanese quail during ontogenesis

J. Antalíková, M. Baranovská, J. Jankela
Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Ivanka pri Dunaji, Slovak Republic

We studied the influence of branched chain amino acids on the muscle proteosynthesis of Japanese quail during ontogenesis. We used in vitro incubation of these muscles: musculus extensor metacarpalis radialis (EMR) - wing muscle, musculus ambiens (MA) - leg muscle. The incorporation of 14C-tyrosine into the individual protein fractions was evaluated. Influences of valine, leucine and isoleucine on proteosynthesis on day 14, 28 and 53 of life of Japanese quails were compared. Different patterns of individual protein fractions were detected. During ontogenesis, in the MA the number of fractions remained unchanged while in the EMR it differed. Four fractions with molecular weight 200-1 000 kDa present on day 14 and 28 were absent on day 53. A new fraction over 200 kDa was detected on day 53. The 14C-tyrosine incorporation after leucine treatment was enhanced only in the MA of 28 days old quails. The protein content in the EMR decreased (50%) in several fractions. The addition of valine had no effect in the MA while in the EMR the protein content decreased in 14 and 28 days old quails. The incorporation of 14C-tyrosine was decreased by the influence of isoleucine in the EMR of 28 and 53 days old quails, in the MA only in 28 days old birds. We assume that the effect of regulatory amino acids on proteosynthesis depends both on muscle type and on the age of Japanese quail.

Keywords: proteosynthesis; isolated muscles; 14C-tyrosine incorporation; individual protein fraction

Published: April 30, 2004  Show citation

ACS AIP APA ASA Harvard Chicago Chicago Notes IEEE ISO690 MLA NLM Turabian Vancouver
Antalíková J, Baranovská M, Jankela J. The effect of branched chain amino acids on proteosynthesis in skeletal muscles of japanese quail during ontogenesis. Czech J. Anim. Sci. 2004;49(4):137-143. doi: 10.17221/4291-CJAS.
Share...
Download citation
  • BibTeX (.bib)
  • Bookends (.ris)
  • EasyBib (.ris)
  • EndNote (.enw)
  • EndNote 8 (.xml)
  • ISI WoS (.isi)
  • Medlars (.medlars)
  • Mendeley (.ris)
  • MODS (.xml)
  • Papers (.ris)
  • RefWorks (.txt)
  • RefManager (.ris)
  • RIS (.ris)
  • MS Word (.xml)
  • Zotero (.ris)
    • Open full article

    References

    1. Antalíková J., Jankela J., Baranovská M. (1999): The effect of branched chain amino acids on protein synthesis in two skeletal muscles of Japanese quail. Physiol. Res., 48, 59-63.
    2. Baracos V.E., Langman M., Mak A. (1989): An in vitro preparation of the extensor digitorum communis muscle from the chick (galus domesticus) for studies of protein turnover. Comp. Biochem. Physiol., 92A, 555-563. Go to original source... Go to PubMed...
    3. Boorman K.N., Bu ery P.J. (1972): Studies of branched chain amino acid antagonism in chicks. Proc. Nutr. Soc., 31, 112A-113A.
    4. Buse M.G., Reid S.S. (1975): Leucine: A possible regulator of protein turnover in muscle. J. Clin. Invest., 56, 1250-1261. Go to original source... Go to PubMed...
    5. Buse M.G., Weigand D.A. (1977): Studies concerning the specificity of the effect of leucine on the turnover of proteins in muscles of control and diabetic rats. Biochim. Biophys. Acta, 475, 81-89. Go to original source... Go to PubMed...
    6. Chua B., Siehl D.L., Morgan H.E. (1979): Effect of leucine and metabolites of branched chain amino acids on protein turnover in heart. J. Biol. Chem., 254, 8358-8362. Go to original source...
    7. Chua B., Siehl D.L., Morgan H.E. (1980): A role of leucine in regulation of protein turnover in working rat hearts. Am. J. Physiol., 239, E510-E514. Go to original source... Go to PubMed...
    8. Fairbanks G., Stack L., Wallach D.F.H. (1971): Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry, 10, 2607-2617. Go to original source... Go to PubMed...
    9. Fulks R.H., Li J.B., Goldberg A.L. (1975): Effects of insulin, glucose and amino acid on protein turnover in rat diaphragms. J. Biol. Chem., 250, 290-298. Go to original source...
    10. Hong S.C., Layman D. (1984): Effects of leucine on in vitro protein synthesis and degradation in rat skeletal muscles. J. Nutr., 114, 1204-1212. Go to original source... Go to PubMed...
    11. Klasing K.C., Jarrell V.L. (1985): Regulation of protein degradation in chick muscle by several hormones and metabolites. Poultry Sci., 64, 694-699. Go to original source... Go to PubMed...
    12. Li J.B., Fulks R.M., Goldberg A.L. (1973): Evidence that the intracellular pool of tyrosine serves as precursor for protein synthesis in muscle. J. Biol. Chem., 248, 7272-7275. Go to original source...
    13. Maltin C.A., Delday M.I., Baillie A.G.S., Garlick P.J. (1989): Fibre-type composition of nine rat muscles. I. Changes during the first year of life. Am. J. Physiol., 257, E823-E827. Go to original source... Go to PubMed...
    14. Mason S.L., Ward L.C. (1981): Branched chain amino acid metabolism in the Japanese quail II. Amino acid oxidation in vivo. Nutr. Rep. Int., 23, 213-218.
    15. May R.C., Piepenbrock N., Kelly R.A., Mitch W.E. (1991): Leucine induced amino acid antagonism in rats: muscle valine metabolism and growth impairment. J. Nutr., 121, 293-301. Go to original source... Go to PubMed...
    16. Mitch W.E., Clark A.S. (1984): Specifity of the effects of leucine and its metabolites on protein degradation in skeletal muscle. Biochem. J., 222, 579-586. Go to original source... Go to PubMed...
    17. Neuhoff V., Stamm R., Eibl H. (1985): Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: A systematic analysis. Electrophoresis, 6, 427-432. Go to original source...
    18. Nieto R., Palmer R.M., Fernándes-Fígares I., Pérez L., Prieto C. (1994): Effect of dietary protein quality, feed restriction and short-term fasting on protein synthesis and turnover in tissues of growing chicken. Brit. J. Nutr., 72, 499-507. Go to original source... Go to PubMed...
    19. Oddessey R., Goldberg A.L. (1979): Leucine degradation in cell-free extracts of skeletal muscle. Biochem. J., 178, 475-489. Go to original source... Go to PubMed...
    20. Pinchasov Y., Nir I. (1988): The synthesis in vivo of proteins in various tissues in chickens adapted to intermittent feeding. Brit. J. Nutr., 60, 517-523. Go to original source... Go to PubMed...
    21. Reeds P.J., Burrin D.G., Davis T.A., Fioro o M.L. (1993): Postnatal growth of gut and muscle: competitors and collaborators. Proc. Nutr. Soc., 52, 57-67. Go to original source... Go to PubMed...
    22. Smith E.L., Austic R.E. (1978): The branched chain amino acid antagonism in chicks. J. Nutr., 108, 1180-1191. Go to original source... Go to PubMed...
    23. Smith E.L., Hill R.L., Lehman I.R., Le owitz R.J., Handler P., White A. (1983): In: McGraw-Hill (ed.): Principles of Biochemistry: General Aspects. New York. 646-670.
    24. Tatsumi R., Ha ori A. (1995): Detection of giant myofibrillar proteins connectin and nebulin by electrophoresis in 2% polyacrylamide gels strengthened with agarose. Anal. Biochem., 224, 28-31. Go to original source... Go to PubMed...
    25. Tischler M.E., Desautels M., Goldberg A.L. (1982): Does leucine, leucyl-t-RNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? J. Biol. Chem., 265, 1613-1621. Go to original source...
    26. Torres N., Tovar A.R., Harper A.E. (1993): Metabolism of valine in rat skeletal muscle mitochondria. J. Nutr. Biochem., 4, 681-689. Go to original source...
    27. Udenfried S., Cooper J.R. (1952): The chemical estimation of tyrosine and tyramine. J. Biol. Chem., 196, 227-233. Go to original source...
    28. Veerkamp J.H., Wagenmakers A.J.M. (1981): In: Walser M., Wiliamson J.R. (eds.): Metabolism and Clinical Implications of Branched Chain Amino and Keto Acids. Elsevier, North Holland, New York. 163-168.

    This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International (CC BY NC 4.0), which permits non-comercial use, distribution, and reproduction in any medium, provided the original publication is properly cited. No use, distribution or reproduction is permitted which does not comply with these terms.


    Return to the content