Hostname: page-component-cd9895bd7-jn8rn Total loading time: 0 Render date: 2024-12-25T01:01:15.035Z Has data issue: false hasContentIssue false
  • English
  • Français

Casein and soya-bean protein have different effects on whole body protein turnover at the same nitrogen balance

Published online by Cambridge University Press:  09 March 2007

K. Nielsen ,
J. Kondrup ,
P. Elsner ,
A. Juul  and
E. S. Jensen
K. Nielsen
Affiliation:
Clinical Nutrition Unit, Medical Department A and Department of Growth and Reproduction, Rigshospitalet, University Hospital, Copenhagen, Denmark
J. Kondrup
Affiliation:
Clinical Nutrition Unit, Medical Department A and Department of Growth and Reproduction, Rigshospitalet, University Hospital, Copenhagen, Denmark
P. Elsner
Affiliation:
Department of Biochemistry A, The Panum Institute, Copenhagen, Denmark
A. Juul
Affiliation:
Clinical Nutrition Unit, Medical Department A and Department of Growth and Reproduction, Rigshospitalet, University Hospital, Copenhagen, Denmark
E. S. Jensen
Affiliation:
Department of Environmental Science, National Laboratory, Risoe, Roskilde, Denmark
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The present study examined whether different proteins have different effects on whole-body protein turnover in adult rats. The rats were either starved, given a protein-free but energy-sufficient diet (1 MJ/kg body weight (BW) per d) or a diet containing intact casein, hydrolysed casein, or hydrolysed soya-bean protein at a level of 9.1 g/kg BW per d. The diets, which were isoenergetic with the same carbohydrate: fat ratio, were given as a continuous intragastric infusion for at least 4 d. During the last 19 h 15N-glycine (a primed continuous infusion) was given intragastrically and 15N was recovered from urinary ammonia and urea during isotope steady state for measurement of protein synthesis and protein degradation. Compared with starvation the protein-free diet decreased N excretion by 75%, probably by increasing the rate of reutilization of amino acids from endogenous proteins for protein synthesis. The protein diets produced a positive N balance which was independent of the protein source. Intact and hydrolysed casein increased protein synthesis 2.6- and 2.0-fold respectively, compared with the protein- free diet. Protein degradation increased 1.4- and 1.2-fold respectively. Hydrolysed soya-bean protein did not increase protein synthesis but decreased protein degradation by 35% compared with the protein-free diet. Compared with the hydrolysed soya-bean protein, intact casein resulted in 2.2- and 2.8-fold higher rates of protein synthesis and degradation respectively. These results are not easily explained by known sources of misinterpretation associated with the 15N-glycine method. Hydrolysed casein and hydrolysed soya-bean protein produced similar concentrations of insulin-like growth factor-1, insulin, glucagon, and corticosterone. The difference in amino acid composition between the dietary proteins was reflected in plasma amino acid composition and this is suggested to be responsible for the different effect on protein turnover. Preliminary results from this study have previously been published in abstract form (Nielsen et al. 1991).

Keywords

Protein turnover15N-glycineCaseinSoya-bean proteinRat
Type
Dietary protein effects on protein turnover
Information
British Journal of Nutrition , Volume 72 , Issue 1 , July 1994 , pp. 69 - 81
Copyright
Copyright © The Nutrition Society 1994

References

REFERENCES

Arnstein, R. V. & Neuberger, A. (1953). The synthesis of glycine and serine by the rat. Biochemical Journal 55, 271–280.CrossRefGoogle ScholarPubMed
Bang, P., Eriksson, U., Sara, V., Wivall, I-L. & Hall, K. (1991). Comparison of acid ethanol extraction and acid gel filtration prior to IGF-I and IGF-II radioimmunoassays: improvement of determinations in acid ethanol extracts by the use of truncated IGF-I as radioligand. Acta Endocrinologica 124, 620–629.Google ScholarPubMed
Clemmons, D. R. & Underwood, L. E. (1991). Nutritional regulation of IGF-I and IGF binding protein. Annual Reviews of Nutrition 11, 393–412.CrossRefGoogle Scholar
Fern, E. B., Garlick, P. J. & Waterlow, J. C. (1985 a). The concept of the single body pool of metabolic nitrogen in determining the rate of whole-body nitrogen turnover. Human Nutrition: Clinical Nutrition 39C, 85–99.Google Scholar
Fern, E. B., Garlick, P. J. & Waterlow, J. C. (1985 b). Apparent compartmentation ofbody nitrogen in one human subject: its consequences in measuring the rate of whole-body protein synthesis with 15N. Clinical Science 68,271–282.CrossRefGoogle Scholar
Fulks, R. M., Li, J. B. & Goldberg, A. L. (1975). Effects of insulin, glucose, and amino acids on protein turnover in rat diaphragm. Journal of Biological Chemistry 250, 290–298.CrossRefGoogle ScholarPubMed
Gaebler, O. H., Glovinsky, R., Lees, H., Kurrie, D. & Choitz, H. G. (1959). Effects of growth hormone and corticotropin on metabolism of N15 from glycine, L-alanine, and ammonium citrate. Endocrinology 65,283–292.CrossRefGoogle ScholarPubMed
Garlick, P. J. & Grant, I. (1988). Amino acid infusion increases the sensitivity of muscle protein synthesis in vivo to insulin. Effect of branched-chain amino acids. Journal of Biochemistry 254, 57–584.CrossRefGoogle ScholarPubMed
Golden, M. H. N. & Jackson, A. A. (1981). Assumptions and errors in the use of 15N-excretion data to estimate whole body protein turnover. In Nitrogen Metabolism in Man, pp. 323–343 [Waterlow, J. C. and Stephen, J. M. L., editors]. London: Applied Science Publishers.Google Scholar
Jackson, A. A. & Golden, M. H. N. (1980). 15N Glycine metabolism in normal man: the metabolic a-amino- nitrogen pool. Clinical Science 58, 517–522.CrossRefGoogle Scholar
Jensen, E. S. (1991). Evaluation of automated analysis of 15N and total N in plant material and soil. Plant and Soil 133, 83–92.CrossRefGoogle Scholar
Jeevanandam, M., Brennan, M. F., Horowitz, G., Rose, D., Mihranian, M. H., Daly, J. & Lowry, S. F. (1985). Tracer priming in human protein turnover studies with 15N glycine. Biochemical Medicine 34, 214–225.CrossRefGoogle Scholar
Jungas, R. L., Halperin, M. L. & Brosnan, J. T. (1992). Quantitative analysis of amino acid oxidation and related gluconeogenesis in humans. Physiological Reviews 72, 419–448.CrossRefGoogle ScholarPubMed
Matthews, D. E., Conway, J. M., Young, V. R. & Bier, D. M. (1981). Glycine nitrogen metabolism in man. Metabolism 30, 886–893.CrossRefGoogle ScholarPubMed
Miotto, G., Venerando, R., Khurana, K. K., Siliprandi, N. & Mortimore, G. E. (1992). Control of hepatic proteolysis by leucine and isovaleryl-L-carnitine through a common locus. Journal of Biological Chemistry 267, 22066–22012.CrossRefGoogle ScholarPubMed
Mitch, W. E. & Clark, A. S. (1984). Specificity of the effects of leucine and its metabolites on protein degradation in skeletal muscle. Biochemical Journal 222, 579–586.CrossRefGoogle ScholarPubMed
Mortimore, G., Poso, A. & Lardeux, B. R. (1989). Mechanism and regulation of protein degradation in liver. Diabetes Metabolism Reviews 5, 49–70.CrossRefGoogle ScholarPubMed
Nielsen, K., Pedersen, A., Jensen, E. J. & Kondrup, J. (1991). Different proteins have different effects on protein synthesis and degradation. Clinical Nutrition 10 (Suppl. 2), 6.CrossRefGoogle Scholar
Picou, D. & Taylor-Roberts, T. (1969). Measurement of total protein synthesis and catabolism and nitrogen turn-over in infants in different nutritional states and receiving different amounts of dietary protein. Clinical Science 36, 283–296.Google Scholar
Pitts, R. F. (1974). Renal regulation of acid-base balance. In Physiology of the Kidney and Body Fluids, pp. 198–241. Chicago: Year Book Medical Publishers.Google Scholar
Poullain, M. G., Cezard, J. P., Marche, C., Macry, J., Roger, L., Grasset, E. & Broyart, J. P. (1991). Effects of dietary whey proteins, their peptides or amino-acids on the ileal mucosa of normally fed and starved rats. Clinical Nutrition 10, 49–54.CrossRefGoogle ScholarPubMed
Podlain, M. G., Cezard, J. P., Roger, L. & Mendy, F. (1989). Effect of whey proteins, their oligopeptide hydrolysates and free amino acid mixtures on growth and nitrogen retention in fed and starved rats. Journal of Parenteral and Enteral Nutrition 13, 382–386.Google Scholar
Robert, J-J., Bier, D. M., Zhao, X. H., Matthews, D. E. & Young, V. R. (1982). Glucose and insulin effects on de novo amino acid synthesis in young men: studies with stable isotope labeled alanine, glycine, leucine, and lysine. Metabolism 31, 1210–1218.CrossRefGoogle ScholarPubMed
Tsukamoto, H., Reidelberger, R. D., French, S. W. & Largman, C. (1984). Long-term cannulation model for blood sampling and intragastric infusion in the rat. American Journal of Physiology 247, R595–R599.Google ScholarPubMed
Vitti, T. G. & Gaebler, O. H. (1963). Effects of growth hormone on metabolism of nitrogen from several amino acids and ammonia. Archives of Biochemistry and Biophysics 101, 292–298.CrossRefGoogle Scholar
Yu, Y. M., Yang, R. D., Matthews, D. E., Wen, Z. M., Burke, J. F., Bier, D. M. & Young, V. R. (1985). Quantitative aspects of glycine and alanine nitrogen metabolism in postabsorptive young men: effects of level of nitrogen and dispensable amino acid intake. Journal of Nutrition 115, 399–410.CrossRefGoogle ScholarPubMed
Zaloga, G. P., Ward, K. A. & Prielipp, R. C. (1991). Effect of enteral diets on whole body and gut growth in unstressed rats. Journal of Parenteral and Enteral Nutrition 15, 42–47.CrossRefGoogle ScholarPubMed