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Effect of dietary protein quality, feed restriction and short-term fasting on protein synthesis and turnover in tissues of the growing chicken

Published online by Cambridge University Press:  09 March 2007

R. Nieto ,
R. M. Palmer ,
I. Fernández-Fígares ,
L. Pérez  and
C. Prieto
R. Nieto
Affiliation:
Estación Experimental del Zaidin, Professor Albareda 1, 18008 Granada, Spain
R. M. Palmer
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 OFG
I. Fernández-Fígares
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 OFG
L. Pérez
Affiliation:
Estación Experimental del Zaidin, Professor Albareda 1, 18008 Granada, Spain
C. Prieto
Affiliation:
Estación Experimental del Zaidin, Professor Albareda 1, 18008 Granada, Spain
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Abstract

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The effect of dietary protein quality and quantity on fractional rates of protein synthesis (ks) and degradation (kd) in the skeletal muscle, liver, jejunum and skin of young growing chickens was studied. Chickens were either fasted overnight or were fed at frequent intervals, using continuous feeders, with equal amounts of a diet containing soya-bean meal as the sole protein source, unsupplemented, or supplemented with either lysine or methionine. Each of the three diets was provided at 2 or 0.9 × maintenance. On the higher intake, birds on the unsupplemented diet gained weight, lysine supplementation decreased and methionine supplementation increased body-weight gain (by −23% and + 22% respectively). Birds led at 0.9 × maintenance lost weight; supplementation with methionine or lysine did not influence this weight loss. None of the dietary regimens had significant effects on protein synthesis rates in any of the tissues, thus the mechanism whereby muscle mass increased in response to methionine supplementation appeared to be a decrease in the calculated rate of protein degradation. Similarly, on the 0.9 × maintenance diet the failure of the animals to grow appeared to be due to an increase in the rate of protein degradation rather than an effect on synthesis. Conversely, muscle ks was decreased in fasted chickens previously fed on the unsupplemented diet at 2 × maintenance, and in birds which had received the 0.9 × maintenance diet fasting resulted in a similar reduction in protein synthesis in muscle; ks in the liver and jejunum was also significantly decreased. The effect of fasting, unlike the effect of supplementation or restriction of the diet, appeared to be due to changes in the rate of protein synthesis.

Keywords

Protein qualityProtein turnoverFeed restrictionchickens
Type
Protein quality and protein turnover
Information
British Journal of Nutrition , Volume 72 , Issue 4 , October 1994 , pp. 499 - 507
Copyright
Copyright © The Nutrition Society 1994

References

REFERENCES

Aguilera, J. F. & Prieto, C. (1987). Necesidades energiticas de mantenimiento en pollos en crecimiento (Energy requirements for maintenance in growing chickens). Archivos de Zootecnia 36, 165–172.Google Scholar
Anderson, V. L. & McLean, R. A. (1974). Design of Experiments: A Realistic Approach, Vol. 5 [Owen, D. B., Lewis, P., Minton, P. D. & Pratt, J. W., editors]. New York: Marcel Dekker Inc.Google Scholar
Ashford, A. J. & Pain, V. M. (1986). Effect of diabetes on the rates of synthesis and degradation of ribosomes in rat muscle and liver in vivo. Journal of Biological Chemistry 261, 4059–4062.CrossRefGoogle ScholarPubMed
Attaix, D., Aurousseau, E., Manghebati, A. & Arnal, M. (1988). Contribution of liver, skin and skeletal muscle to whole-body protein synthesis in the young lamb. British Journal of Nutrition 60, 77–84.CrossRefGoogle ScholarPubMed
Bryan, L., Buttery, P. J. & Fisher, C. (1983). Protein synthesis in the growing broiler chicken. In IVth International Symposium on Protein Metabolism and Nutrition; les Colloques de I'INRA, no. 16, pp. 53–56. Clermont Ferrand, France: INRA Publ.Google Scholar
Garlick, P. J., Burns, H. J. G. & Palmer, R. M. (1988). Regulation of muscle protein turnover: possible implications for modifying the responses to trauma and nutrient intake. In Bailliere's Clinical Gastroenterology 2 pp. 915–940 [Burns, H. J. G., editor]. London: Bailliere Tindall.Google Scholar
Garlick, P. J., Fern, M. & Preedy, V. R. (1983). The effect of insulin infusion and food intake on muscle protein synthesis in postabsorptive rats. Biochemical Journal 210, 669–676.CrossRefGoogle 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] phenylalanine. Biochemical Journal 192, 712–723.CrossRefGoogle ScholarPubMed
Garlick, P. J. & Millward, D. J. (1972). An appraisal of techniques for the determination of protein turnover in vivo. Biochemical Journal 129, 1P–2P.CrossRefGoogle ScholarPubMed
Jepson, M. M., Bates, P. C. & Millward, D. J. (1988). The role of insulin and thyroid hormones in the regulation of muscle growth and protein turnover in response to dietary protein in the rat. British Journal of Nutrition 59, 397–415.Google ScholarPubMed
Klasing, K. C. & Calvert, C. C. (1987). Growth characteristics, protein synthesis, and protein degradation in muscle from fast and slow-growing chickens. Poultry Science 66, 1189–1196.CrossRefGoogle ScholarPubMed
Lin, R. I. & Schjeide, O. A. (1969). Micro estimation of RNA by the cupric ion catalyzed orcinol reaction. Analytical Biochemistry 21, 473–483.CrossRefGoogle Scholar
Lobley, G. E., Harris, P. M., Skene, P. A., Brown, D., Milne, V., Calder, A. G., Anderson, S. E., Garlick, P. J., Nevison, I. & Connell, A. (1992). Responses in tissue protein synthesis to sub- and supra-maintenance intake in ruminant lamb: comparison of large and continuous infusion techniques. British Journal of Nutrition 68, 373–388.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
McNurlan, M. A. & Garlick, P. J. (1981). Protein synthesis in liver and small intestine in protein deprivation and diabetes. American Journal of Physiology 241, E238–E245.Google ScholarPubMed
McNurlan, M. A., McHardy, K. C., Broom, J., Milne, E., Fearns, L. M., Reeds, P. J. & Garlick, P. J. (1987). The effect of indomethacin on the response of protein synthesis to feeding in rats and man. Clinical Science 73, 69–75.CrossRefGoogle ScholarPubMed
McNurlan, M. A., Pain, V. M. & Garlick, P. J. (1980). Conditions that alter rates of tissue protein synthesis in vivo. Biochemical Society Transactions 8, 283–285.CrossRefGoogle ScholarPubMed
Maruyama, K., Sunde, M. L. & Swick, R. S. (1978). Growth and muscle protein turnover in the chick. Biochemical Journal 176, 573–582.CrossRefGoogle ScholarPubMed
Millward, D. J., Garlick, P. J., Nnanyelugo, D. O. & Waterlow, J. C. (1976). The relative importance of muscle protein synthesis and breakdown in relation to muscle mass. Biochemical Journal 156, 185–188.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J., Stewart, R. J. C., Nnanyelugo, D. O. & Waterlow, J. C. (1975). Skeletal muscle growth and protein turnover. Biochemical Journal 150, 235–243.CrossRefGoogle ScholarPubMed
Munro, H. N. & Fleck, A. (1969). Analysis of tissues and body fluids for nitrogenous constituents. In Mammalian Protein Metabolism, Vol. 4, pp. 424–525 [Munro, H. N., editor]. New York: Academic Press.Google Scholar
Muramatsu, T., Coates, M. E., Hewitt, D., Salter, D. N. & Garlick P. J. (1983). The influence of the gut microflora on protein synthesis in liver and jejunal mucosa in chicks. British Journal of Nutrition 49, 453–462.CrossRefGoogle ScholarPubMed
Muramatsu, T., Salter, D. N. & Coates, M. E. (1985). Protein turnover of breast muscle in germ-free and conventional chicks. British Journal of Nutrition 54, 131–145.CrossRefGoogle ScholarPubMed
Pinchasov, Y., Nir, I. & Nitsan, Z. (1988). The synthesis in vivo of proteins in various tissues in chickens adapted to intermittent feeding. British Journal of Nutrition 60, 517–523.CrossRefGoogle ScholarPubMed
Reeds, P. J. & Davis, T. A. (1992). Hormonal regulation of muscle protein synthesis and degradation. In The Control of Fat and Lean Deposition, pp. 1–26 [Buttery, P. J., Boorman, K. N. and Lindsay, D. B., editors]. Oxford: Butterworth-Heinemann.Google Scholar
Reeds, P. J., Palmer, R. M., Hay, S. M. & McMillan, N. (1986). Protein synthesis in skeletal muscle measured at different times during a 24 hour period. Bioscience Reports 6, 209–213.CrossRefGoogle Scholar
Seve, B., Reeds, P. J., Fuller, M. F., Cadenhead, A. & Hay, S. M. (1986). Protein synthesis and retention in some tissues of the young pig as influenced by dietary protein intake after early weaning. Possible connection to the energy metabolism. Reproduction Nutrition Developpement 26, 849–861.CrossRefGoogle Scholar
Scott, M. L., Nesheim, M. C. & Young, R. J. (1982). Nutrition of the Chicken, 3rd ed. Ithaca, New York: M. L. Scott and Associates.Google Scholar
Southorn, B. G., Palmer, R. M. & Garlick, P. J. (1990). Acute effects of corticosterone on tissue protein synthesis and insulin sensitivity in rats in vivo. Biochemical Journal 27, 187–191.CrossRefGoogle Scholar
Statistical Analysis Systems Institute Inc. (1985). SAS Procedures Guide for Personal Computers. Version 6 Edition. Cary, NC: SAS Institute Inc.Google Scholar
Suzuki, O. & Yagi, K. (1976). A fluorimetric assay for βphenylethylamine in rat brain. Analytical Biochemistry 75, 192–200.CrossRefGoogle Scholar
Waterlow, J. C., Garlick, P. J. & Millward, D. J. (1978). Protein Turnover in Mammalian Tissues and in the Whole Body. Amsterdam: North-Holland.Google Scholar