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Protein expression of pectoralis major muscle in chickens in response to dietary methionine status

Published online by Cambridge University Press:  08 March 2007

A. Corzo*
Affiliation:
Department of Poultry Science, Mississippi State University, MS 39762, USA
M. T. Kidd
Affiliation:
Department of Poultry Science, Mississippi State University, MS 39762, USA
W. A. Dozier III
Affiliation:
USDA-ARS Poultry Research Unit, Mississippi State, MS 39762, USA
L. A. Shack
Affiliation:
Department of Basic Sciences, Mississippi State University, MS 39762, USA
S. C. Burgess
Affiliation:
Department of Basic Sciences, Mississippi State University, MS 39762, USA
*
*Corresponding author: Dr Alejandro Corzo, fax +1 662 325 8292, email acorzo@poultry.msstate.edu
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Abstract

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The present study evaluated the effect of dietary methionine on breast-meat accretion and protein expression in skeletal muscle of broiler chickens in vivo. All broilers received a common pre-test diet up to 21d of age, and were subsequently fed either a methionine-deficient (MD) or -adequate (MA) diet (3·1 V. 4·5g/kg diet) from age 21 to 42d. Dietary cystine levels were 3·7 V. 3·6g/kg diet for the MD and MA diet, respectively. Detrimental effects on carcass yield (P=0·004), abdominal fat percentage (P=0·001), and breast-meat weight (P=0·001), yield (P=0·001), and uniformity (P=0·002) were observed and validated in birds fed MD diets. Via tandem MS, a total of 190 individual proteins were identified from pectoralis major (PM) muscle tissue. From the former composite, peptides from three proteins were observed to be present exclusively in breast muscle from those chickens fed the MD diet (pyruvate kinase, myosin alkali light chain-1, ribosomal-protein-L-29). No proteins were observed to be uniquely expressed in chickens fed MA diets. Research is warranted to further explore the possibility of the proteins pyruate kinase, myosin alkali light chain-1, or ribosomal protein L-29, as potential biological indicators of differences in protein expression of PM of chickens in response to a dietary methionine deficiency.

Type
Research Article
Copyright
Copyright © The Nutrition Society 2006

References

Adkins, JN, Varnum, SM, Auberry, KJ, Moore, RJ, Angell, NH, Smith, RD, Springer, DL, Pounds, JG, Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry. Mol Cell Proteomics (2002) 1 947955.CrossRefGoogle Scholar
Andrulis, IL, Chen, J, Ray, PN, Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol (1987) 7 24352443.Google ScholarPubMed
Aviagen North America Broiler Management Guide. Huntsville, AL:AVA. (2005).Google Scholar
Baker, DH, Fernandez, SR, Webel, DM, Parsons, CM, Sulfur amino acid requirement and cystine replacement value of broiler chicks during the period three to six weeks posthatching. Poult Sci (1996) 75 737742.CrossRefGoogle ScholarPubMed
Bartov, I, Jensen, LS, Veltmann, JR jr, Effect of corticosterone and prolactin on fattening in broiler chicks. Poult Sci (1980) 59 13281334.CrossRefGoogle ScholarPubMed
Blommaart, EF, Luiken, JJ, Meijer, AJ, Autophagic proteolysis:control and specificity Histochem (1997) 29 365385.CrossRefGoogle ScholarPubMed
Brodersen, D, Nissen, P, The social life of ribosomal proteins. FEBS J (2005) 272 20982108CrossRefGoogle ScholarPubMed
Buse, MG, Reid, SS, Leucine, a possible regulator of protein turnover in muscle. J Clin Invest (1975) 56 12501261.CrossRefGoogle ScholarPubMed
Chen, H, Pan, YX, Wong, EA, Webb, KE Jr, Dietary protein level and stage of development affect expression of an intestinal peptide transporter (cPepT1) in chickens. J Nutr (2005) 135 193198CrossRefGoogle ScholarPubMed
Corzo, A, Kidd, MT, Koter, MD, Burgess, SC, Assessment of dietary amino acid scarcity on growth and blood plasma proteome status of broiler chicks. Poult Sci (2005) 84 419425.CrossRefGoogle Scholar
Fafournoux, P, Bruhat, A, Jousse, C, Amino acid regulation of gene expression. Biochem J (2000) 351 112.CrossRefGoogle ScholarPubMed
Garlick, PJ, Grant, I, Amino acid infusion increases the sensitivity of muscle protein synthesis in vivo to insulin. Effect of branched-chain amino acids. Biochem J (1988) 579 579584.CrossRefGoogle Scholar
Hickling, D, Guenter, W, Jackson, ME, The effects of dietary methionine and lysine on broiler chicken performance and breast meat yield. Can J Anim Sci (1990) 70 673678.CrossRefGoogle Scholar
Hitomi, Y, Ito, A, Naito, Y, Yoshida, A, Liver-specific induction of ribosomal protein gene expression by amino acid starvation in rats. Biosci Biotechnol Biochem (1993) 57 12161217.CrossRefGoogle ScholarPubMed
Hong, SO, Layman, DK, Effects of leucine on in vitro protein synthesis and degradation in rat skeletal muscles. J Nutr (1984) 114 12041212.CrossRefGoogle ScholarPubMed
Huyghebaert, G, Pack, M, Effects of dietary protein content, addition of nonessential amino acids and dietary methionine to cysteine balance on response to dietary sulphur-containing amino acids in broilers Br Poult Sci (1996) 37 623639.CrossRefGoogle ScholarPubMed
Jensen, LS, Wyatt, CL, Fancher, BI, Sulfur amino acid requirement of broiler chickens from 3 to 6 weeks of age. Poult Sci (1989) 68 163168.CrossRefGoogle ScholarPubMed
Jeroch, H, Pack, M, Effects of dietary sulfur amino acids and crude protein on the performance of finishing broilers. Arch Anim Nutr (1995) 48 109118.Google ScholarPubMed
Jousse, C, Averous, J, Bruhat, A, Carraro, V, Mordier, S, Fafournoux, P, Amino acids as regulators of gene expression: molecular mechanisms. Biochem Biophys Res Comm (2004) 313 447452.CrossRefGoogle ScholarPubMed
Kalinowski, A, Moran, ET jr, Wyatt, CL, Methionine and cystine requirements of slow- and fast-feathering broiler males from three to six weeks of age. Poult Sci (2003) 82 14281437.CrossRefGoogle ScholarPubMed
Laine, RO, Shay, NF, Kilberg, MS, Nuclear retention of the induced mRNA following amino acid-dependent transcriptional regulation of mammalian ribosomal proteins L17 and S25. J Biol Chem (1994) 269 96939697.CrossRefGoogle ScholarPubMed
Llames, CR, Fontaine, J, Determination of amino acids in feeds: collaborative study J AOAC Int (1994) 77 13621402CrossRefGoogle Scholar
Lonberg, N, Gilbert, W, Primary structure of chicken muscle pyruvate kinase mRNA. Proc Natl Acad Sci USA (1983) 80 36613665.CrossRefGoogle ScholarPubMed
Long, W, Saffer, L, Wei, L, Barrett, EJ, Amino acids regulate skeletal muscle PHAS-I and p70 S6-kinase phosphorylation independently of insulin Am J Physiol (2000) 279 E301E306.Google ScholarPubMed
Matsuda, G, Maita, T, Umegane, T, The primary structure of L-1 light chain of chicken fast skeletal muscle myosin and its genetic implication. FEBS Lett (1981) 126 111113.CrossRefGoogle ScholarPubMed
Murphy, ME, Amino acid compositions of avian eggs and tissues:nutritional implications J Avian Biol (1981) 25 2738.CrossRefGoogle Scholar
Nagra, CL, Meyer, RK, Influence of corticosterone on the metabolism of palmitate and glucose in cockerels. Gen Comp Endocrinol (1963) 3 131138.CrossRefGoogle Scholar
National Center for Biotechnology Information Non redundant protein database -NCBInrPDB, Accessed 10 April 2005. http://ncbi.nlm.nih.gov/entrez/query.fcgi?db = protein. (2005).Google Scholar
National Research Council Nutrient Requirements of Poultry, 9th revised ed. Washington, DC: National Academy Press. (1994).Google Scholar
Nedergaard, m, Takano, t, Hansen, aj, Beyond the role of glutamate as a neurotransmitter. Nat Rev Neurosci (2002) 3 748755.CrossRefGoogle ScholarPubMed
Nicholson, B, McGivan, JD, Induction of high affinity glutamate transport activity by amino acid deprivation in renal epithelial cells does not involve an increase in the amount of transporter protein. J Biol Chem (1996) 271 1215912164CrossRefGoogle Scholar
Nika, H, Hultin, T, Location of the sulfhydryl groups involved in disulfide interaction between the neighboring proteins L6 and L29 in mammalian ribosomes. Eur J Biochem (1984) 142 521526.CrossRefGoogle ScholarPubMed
Schutte, JB, Pack, M, Sulfur amino acid requirements of broiler chicks from fourteen to thirty-eight days of age. 1. Performance and carcass yield. Poult Sci (1995 a) 74 480487.CrossRefGoogle ScholarPubMed
Schutte, JB, Pack, M, Effects of dietary sulphur containing amino acids on performance and breast meat deposition of broiler chicks during the growing and finishing phases. Br Poult Sci (1995 b) 36 747762.CrossRefGoogle ScholarPubMed
Soeno, Y, Yahima, H, Kawamura, Y, Kimura, S, Maruyama, K, Obinata, T, Organization of connectin/titin filaments in sarcomeres of differentiating chicken skeletal muscle cells. Mol Cell Biochem (1999) 190 125131CrossRefGoogle ScholarPubMed
Tremblay, F, Marette, A, Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells. J Biol Chem (2001) 276 3805238060.CrossRefGoogle ScholarPubMed
van Sluijters, DA, Dubbelhuis, PF, Blommaart, EF,Meijer, AJ, Amino-acid-dependent signal transduction. Biochem J (2000) 351 545550.CrossRefGoogle ScholarPubMed
Washburn, MP, Wolters, D, Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol (2001) 19 242247.CrossRefGoogle ScholarPubMed
Wool, IC, Chan, YL, Gluck, A, Structure and evolution of mammalian ribosomal proteins. Biochem Cell Biol (1995) 73 933947.CrossRefGoogle ScholarPubMed