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Dietary lysine deficiency greatly affects muscle and liver protein turnover in growing chickens*

Published online by Cambridge University Press:  09 March 2007

S. Tesseraud ,
R. Peresson ,
J. Lopes  and
A.M. Chagneau
S. Tesseraud
Affiliation:
Station de Recherches Avicoles, Institut National de la Recherche Agronomique, Centre de Tours-Nouzilly, 37380 Nouzilly, France
R. Peresson
Affiliation:
Station de Recherches Avicoles, Institut National de la Recherche Agronomique, Centre de Tours-Nouzilly, 37380 Nouzilly, France
J. Lopes
Affiliation:
Station de Recherches Avicoles, Institut National de la Recherche Agronomique, Centre de Tours-Nouzilly, 37380 Nouzilly, France
A.M. Chagneau
Affiliation:
Station de Recherches Avicoles, Institut National de la Recherche Agronomique, Centre de Tours-Nouzilly, 37380 Nouzilly, France
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Abstract

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We analysed the respective influences of age and lysine deficiency on skeletal muscle and liver protein turnover. Growing male broilers were fed ad libirum on isoenergetic diets containing 2OO g crude protein/kg which varied in their lysine content (7·7 or 10·1 g/kg). Fractional rates of protein synthesis (FSR) were measured in vivo in the liver and the pectoralis major muscle of 2-, 3- and 4-week-old chickens (flooding dose of l-[143H]phenylalanine). Fractional rates of proteolysis (FBR) were estimated for the same tissues as the difference between synthesis and growth. Over the 2-week period liver FSR and FBR were unchanged, whereas muscle FSR decreased with age. This developmental decline was related to the lower capacity for protein synthesis (Cs) without any modifications of the translational efficiency. Whatever the age, lysine deficiency resulted in significant decreases in body weight, tissue protein content and tissue protein deposition, apparently because of reduced amounts of proteins synthesized. We recorded a difference in the response of the two tissues to lysine deficiency, the pectoralis major being more sensitive than the liver. When comparing birds of the same age, liver FSR and FBR were not modified by the diet, where as muscle FSR, Cs and FBR were higher in chicks fed on a lysinc-deficient diet than in the controls. Conversely, when chicks of similar weights were compared, the main effect of the dietary deficiency was an increase in muscle FBR. The results suggest that lysine deficiency not only delayed chick development so that protein turnover was affected, but also induced greater changes in metabolism. Thus, the principal mechanism whereby muscle mass decreased appeared to be a change in FBR.

Keywords

LysineProtein turnoverChicken
Type
Poultry nutrition
Information
British Journal of Nutrition , Volume 75 , Issue 6 , June 1996 , pp. 853 - 865
Copyright
Copyright © The Nutrition Society 1996

References

REFERENCES

Akinwande, A. I. &Bragg, D. B. (1985). Effect of the level ofdietary lysine on turnover rate of liver protein in the chick. Poultry Science 64, 1938–1940.CrossRefGoogle Scholar
Arnal, M., Obled, C., Attaix, D.Patureau, M.P. & Bonin, D. (1987).Dietary control ofprotein turnover. Diabere Metabolisme 13, 630–642.Google Scholar
Attaix, D., Aurousseau, E., Bayle, G., Rosolowska-Huszcz, D. &Arnal, M. (1988). Respective influence of age and weaning on skeletal and visceral muscle protein synthesis in the lamb. Biochemical Journal 256, 791–795.CrossRefGoogle ScholarPubMed
Conway, J.M., Bier, D.M., Motil, K.J., Burke, J.F. &Young, V.R. (1980). Whole-body lysine flux in young adult meneffects of reduced total protein and of lysine intake. American Journal of Physiology 239, E192–E200.Google Scholar
Fuller, M. F., Reeds, P. J., Cadenhead, A., Seve, B. & Preston, T. (1987). Effect of the amount and quality of dietary protein on nitrogen metabolism and protein turnover of pigs. British Journal of Nutrition 58, 287–300CrossRefGoogle ScholarPubMed
Garlick, P.J., McNurlanM.A, M.A,, Essen, P. & Werneman, J. (1994). Measurement of tissue protein synthesis rates in vivo: critical analysis of contrasting methods. American Journal of Physiology 266, E287–E297.Google ScholarPubMed
Garlick, P. J., McNurlan, M. A. &Preedy, V.R. (1980). A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H]-Phe. Biochemical Journal 192, 719–723.CrossRefGoogle Scholar
Goldspink, D. F. &Kelly, F.J. (1984). Protein turnover and growth in the whole-body, liver and kidney of the rat from the foetus to the senility. Biochemical Journal 217, 507–516.CrossRefGoogle Scholar
Griffin, H.D. & Goddard, C. (1994). Rapidly growing broiler (meat-type) chickens: their originand use for comparative studies of the regulation of growth. International Journal of Biochemistry 26, 19–28.CrossRefGoogle Scholar
Kino, K. & Okumura, J. (1986 a). The effect of single essential amino acid deprivation on chick growth and nitrogen and energy balances at ad libitum and equalized-food intakes. Poultry Science 65, 1728–1735.CrossRefGoogle ScholarPubMed
Kino, K. & Okumura, J. (1986 b). Improvement of body weight and nitrogen balance of chicks fed histidine-free or lysine-free diets with supplementation of graded levels of sulfurcontainingamino acids. Poultry Science 65,1736–1740.CrossRefGoogle ScholarPubMed
Kino, K. &Okumura, J. (1987). Whole-body protein turnover in chicks fed control, histidine, or methionine plus cystine-free diets. Poultry Science 66, 1392–1397.CrossRefGoogle ScholarPubMed
Lobley, G.E. (1993). Species comparisons of tissue protein metabolism effects of age and hormonal action. Journal of Nutrition 123, 337–343.CrossRefGoogle ScholarPubMed
McDonald, M. L. & Swick, R. W. (1981). The effect of protein depletion and repletion on muscle-protein turnover in the chick. Biochemical Journal 194, 811–819.CrossRefGoogle Scholar
McNurlan, M. A. & Garlick, P.J. (1989). Influence of nutrient intake on protein turnover. Diabetes/Metabolism Reviews 5, 165–189.CrossRefGoogle ScholarPubMed
McNurlan, M.A., Tomkins, A. M. & Garlick, P.J. (1979). The effect of starvation on the rate of protein synthesis in rat liver and small intestine. Biochemical Journal 178, 375–379.CrossRefGoogle ScholarPubMed
Maruyama, K., Sunde, M.L. & Swick, R.W. (1978). Growth and muscle protein turnover in the chick. Biochemical Journal 176, 573–582.CrossRefGoogle ScholarPubMed
Meredith, C. N., Wen, Z. M., Bier, D. M., Matthews, D. E. & Young, V.R. (1986). Lysine kinetics at graded lysine intakes in young men. American Journal of Clinical Nutrition 43,787–794.CrossRefGoogle ScholarPubMed
Mosoni, L., Valluy, M.C., Sermrier, B., PrugnaudJ., J.,Obled, C., Guezmnec, C.Y. & Patureau, Mirand P. (1995). Altered response of protein synthesis to nutritional state and endurance training in old rats. American Journal of Physiology 268, E328–E335.Google ScholarPubMed
Munro, H. N. & Fleck, A. (1969). Analysis of tissues and body fluids for nitrogenous constituents. In Mammalian Protein Metabolism vol. 3, pp. 424–525 [ Munro, H.N., editor] New York: Academic Press.Google Scholar
Muramatsu, T. (1990). Nutrition and whole-body protein turnover in the chicken in relation to mammalian species. Nutrition Research Reviews 3, 211–228.CrossRefGoogle ScholarPubMed
Muramatsu, T., Muramatsu, S., Okumura, J. &Tasaki, I. (1987). Developmental fall in whole body protein turnover of chick embryos during incubation. British Poultry Science 28, 165–172.CrossRefGoogle ScholarPubMed
Muramatsu, T. &Okumura, J. (1985). Whole-body protein turnover in chicks at early stages of growth. Journal of Nutrition 115, 483–490.CrossRefGoogle ScholarPubMed
Nieto, R., Palmer, R. M., Fernandez-Figares, I., Perez, L. & Prieto, C. (1994). Effect of dietary protein quality, feed restriction and short-term fasting on protein synthesis and turnover in tissues of the growing chicken. British Journal of Nutrition 72, 499–507.CrossRefGoogle ScholarPubMed
Okumura, J., Mori, S. &Muramatsu, T. (1985). Relationship between food consumption and energy and nitrogen utilisation by chicks given varying amounts of standard and leucine-, isoleucine- and valine-deficient diets. British Poultry Science 26, 519–525.Google ScholarPubMed
Salter, D. N., Montgomery, A. I., Hudson, A., Quelch, D. B. & Elliot, R. J. (1990). Lysine requirements and wholebody protein turnover in growing pigs. British Journal of Nutrition 63, 503–513CrossRefGoogle ScholarPubMed
Smith, P.K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J. & Klenk, D. C. (1985). Measurement of protein using bicinchoninic acid. Analytical Biochemistry 150, 76–85.CrossRefGoogle ScholarPubMed
Suzuki, O. &Yagi, K. (1976). A fluorometric assay for phenylethylamine in rat brain. Analytical Biochemistry 75, 192–200.CrossRefGoogle ScholarPubMed
Tesseraud, S., Cammas, J. C. & Chapeau, A. M. (1994). Effect of age and divergent selection for body weight on muscle protein turnover in chickens. Reproduction Nutrition Development 34, 638–639.CrossRefGoogle Scholar
Tesseraud, S., Larbier, M., Chapeau, A. M. &Geraert, P. A. (1992). Effects of dietary lysine on muscle protein turnover in growing chickens. Reproduction Nutrition Development 32, 163–175.CrossRefGoogle ScholarPubMed
Tomas, F. M., Pym, R. A. &Johnson, R.J. (1991). Muscle protein turnover in chickens selected for increased growth rate, food consumption or efficiency of food utilisation effects of genotype and relationship to plasma IGF-I and growth hormone. British Poultry Science 32, 363–376.CrossRefGoogle ScholarPubMed
Vary, T.C. &Kimball, S.R. (1992 a). Regulation of hepatic protein synthesis in chronic inflammation and sepsis. American Journal of Physiology 262, C445–C452.CrossRefGoogle ScholarPubMed
Vary, T.C. & Kimball, S.R. (1992 b). Sepsis-induced changes in protein synthesis differential effects on fast- and slow-twitch muscles. American Journal of Physiology 262, C1513–C1519.CrossRefGoogle ScholarPubMed