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The effects of experimental malnutrition on albumin metabolism and distribution in rabbits

Published online by Cambridge University Press:  09 March 2007

S. E. Weidel ,
G. Smith  and
A. Fleck
S. E. Weidel
Affiliation:
Department of Chemical Pathology, Charing Cross and Westminster Medical School, St Dunstan's Road, LondonW6 8RP
G. Smith
Affiliation:
Department of Chemical Pathology, Charing Cross and Westminster Medical School, St Dunstan's Road, LondonW6 8RP
A. Fleck
Affiliation:
Department of Chemical Pathology, Charing Cross and Westminster Medical School, St Dunstan's Road, LondonW6 8RP
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Abstract

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In order to determine the extent to which the concentration of albumin in plasma is maintained at the expense of the extravascular pool during protein-energy malnutrition, the rates of exchange between albumin in plasma (1A) and the extravascular pool (EA) and consequently the distribution of albumin between intravascular and extravascular pools (expressed as EA:IA) were measured in protein-energy-depleted and control rabbits. The fractional rates of synthesis (FSR) and catabolism (FCR), the concentration of albumin and the plasma volume (PV) were also measured. In animals in which protein-energy intake was reduced by 58% the concentration of albumin in plasma remained unchanged, whereas FCR decreased by 38 % and FSR by 30 YO. No significant changes in EA: IA or PV were found. We conclude that albumin concentration during proteirrenergy depletion is not maintained at the expense of extravascular albumin, but by parallel changes in the rates of catabolism and synthesis.

Keywords

Protein-energy malnutritionAlbuminRabbit
Type
Albumin metabolism in malnutrition
Information
British Journal of Nutrition , Volume 72 , Issue 3 , September 1994 , pp. 369 - 384
Copyright
Copyright © The Nutrition Society 1994

References

REFERENCES

Bentdal, Ø. H., Frøland, S. S., Askevold, F., Bjorno, K. & Larson, S. (1988). Nutritional assessment of anorexia nervosa patients - Analysis of anthropometric and biochemical variables to evaluate patients at risk. Clinical Nutrition 7, 93–99.CrossRefGoogle Scholar
Bianchi, R., Mariane, G., Pilo, A. M., Toni, G. & Donato, L. (1973). Short term determination of plasma protein turnover by a two tracer technique using plasma and urine data. In Protein turnover. Ciba Foundation Symposia no. 9, pp. 47–72 [Wolstenholme, G. E. M. and OConnor, M., editors]. London: Elsevier.CrossRefGoogle Scholar
Campbell, R. M., Cnthbertson, D. P., Matthews, C. M. E. & McFarlane, A. S. (1956). Behaviour of 14C- and 131l-labelled plasma proteins in the rat. International Journal of Applied Radiation and Isotopes 1, 66–84.CrossRefGoogle Scholar
Cohen, S. & Hansen, J. D. L. (1962). Metabolism of albumin and gamma-globulin in kwashiorkor. Clinical Science 23, 351–359.Google ScholarPubMed
Edwards, J. S. & Fleck, A. (1992). Selection and comparison of methods for investigating the metabolism and distribution of plasma proteins. In Proceedings of the ACB National Meeting B25, p. 72 [Martin, S. M. and Halloran, S. P., editors]. Cambridge: Piggott Printers Limited.Google Scholar
Fleck, A. (1974). Micro-determination of nitrogen. CRC Critical Review on Analytical Chembtry 4, 141–154.Google Scholar
Fleck, A. (1985). Computer models for metabolic studies on plasma proteins. Annals of Clinical Biochemistry 2, 33–49.CrossRefGoogle Scholar
Fleck, A. (1988). Nutrition, protein metabolism and fluid balance. In Clinical Anaesthesiology, International Practice Research. Fluid Resuscitation, Vol. 2, pp. 625–648 [Kox, W. J. and Gamble, J., editor]. London: Balliere Tindall.Google Scholar
Gersovitz, M., Munro, H. N., Udall, J. & Young, V. R. (1980). Albumin synThesis in young and elderly subjects using a new stable isotope methodology: response to level of protein intake. Metabolism 29, 1075–1086.CrossRefGoogle Scholar
Hoffenberg, R., Black, E. & Brock, J. F. (1966). Albumin and gamma-globulin tracer studies in protein depletion states. Journal of Clinical Investigation 45, 143–151.CrossRefGoogle ScholarPubMed
Hoffenberg, R., Saunders, S., Linder, G. C., Black, E. & Brock, J. F. (1962). l131-albumin metabolism in human adults after experimental protein depletion and repletion. In Protein Metabolism - An International Symposium, pp. 314–325 [Gross, F., editor]. Berlin: Springer-Verlag.CrossRefGoogle Scholar
James, W. P. T. & Hay, A. M. (1968). Albumin metabolism: effect of the nutritional state and the dietary protein intake. Journal of Clinical Investigation 47, 1958–1972.CrossRefGoogle ScholarPubMed
Keys, A., Brozek, J., Henschel, A., Mickelson, O. & Taylor, H. L. (1950). The Biology of Human Starvation. Minneapolis and London: University of Minnesota Press.CrossRefGoogle Scholar
Kingsley, G. R. (1942). The direct biuret method for the determination of serum proteins as applied to photoelectric and visual colorimetry. Journal of Laboratory and Clinical Medicine 27, 840–845.Google Scholar
Koj, A. & McFarlane, A. S. (1968). Effect of endotoxin on plasma albumin and fibrinogen synThesis rates in rabbits as measured by the 14C carbonate method. Biuchemical Journal 108, 137–146.Google ScholarPubMed
McFarlane, A. S. (1956). Labelling of plasma proteins with radioactive iodine. Biochemical Journal 62, 135–143.CrossRefGoogle ScholarPubMed
McFarlane, A. S. (1963). Measurement of synThesis rates of liver-produced plasma proteins. Biochemical Journal 89, 277–290.CrossRefGoogle ScholarPubMed
McFarlane, A. S., Irons, L., Koj, A. & Regoeczi, E. (1965). The measurement of synThesis rates of albumin and fibrinogen in rabbits. Biochemical Journal 95, 536–540.CrossRefGoogle ScholarPubMed
McFarlane, A. S. & Koj, A. (1970). Short-term measurement of catabolic rates using iodine-labelled plasma proteins. Journal of Clinical Investigation 49, 1903–1911.CrossRefGoogle Scholar
Matthews, C. M. E. (1957). The theory of tracer experiments with 131l-labelled plasma proteins. Physics in Medicine and Biology 2, 36–53.CrossRefGoogle Scholar
Matthews, C. M. E. (1961). Effect of plasmapheresis on albumin pools in rabbits. Journal of Clinical Investigation 40, 603–610.CrossRefGoogle ScholarPubMed
Nosslin, B. (1973). Analysis of disappearance time-curves after single injection of labelled proteins. In Protein Turnover. Ciba Foundation Symposia, Vol. 9, pp. 113–130 [Wolstenholme, G. E. M. and O'Connor, M., editors]. Amsterdam: Elsevier.CrossRefGoogle Scholar
Peters, T. Jr, Baimonte, G. T. & Doumas, B. T. (1982). Protein (total protein) in serum, urine, cerebrospinal fluid: albumin in serum. In SeZected Methods of Clinical Chemistry, vol. 9 [Faulkner, w. R. and Meites, S., editors]. Washington, DC: American Association for Clinical Chemistry.Google Scholar
Picou, D. & Waterlow, J. C. (1962). The effect of malnutrition on the metabolism of plasma albumin. Clinical Science 22, 459–468.Google Scholar
Reeve, E. B. & Roberts, J. E. (1959). The kinetics of the distribution and breakdown of I131-albumin in the rabbit. Journal of General Physiology 43, 414–44.Google Scholar
Reeve, E. B., Pearson, J. R. & Martz, D. C. (1963). Plasma protein synThesis in the liver. Science 139, 914–916.CrossRefGoogle ScholarPubMed
Regoeczi, E., Irons, L., Koj, A. & McFarlane, A. S. (1965). Isotopic studies of urea metabolism in rabbits. Biochemical Journal 95, 521–532.CrossRefGoogle ScholarPubMed
Rothschild, M. A., Oratz, M., Evans, C. & Schreiber, S. S. (1964). Alteration in albumin metabolism after serum and albumin infusions. Journal of Clinical Investigation 43, 1874–1880.CrossRefGoogle ScholarPubMed
Rothschild, M. A., Oratz, M., Mongelli, J. & Schreiber, S. S. (1968 a). Effects of a short-term fast on albumin synthesis studied in vivo, in the perfused liver, and on amino acid incorporation by hepatic microsomes. Journal of Clinical Investigation 47, 2591–2599.CrossRefGoogle ScholarPubMed
Rothschild, M. A., Oratz, M. & Schreiber, S. S. (1968 b). The effect of hyperalbuminemia on albumin synthesis studied in rabbits using 14C-carbonate. Journal of Nuclear Biology and Medicine 12, 68–72.Google ScholarPubMed
Rothschild, M. A., Oratz, M. & Schreiber, S. S. (1988). Serum albumin. Hepatology 8, 385–401.CrossRefGoogle ScholarPubMed
Shipley, R. A. & Clark, R. E. (editors) (1972). In Tracer Methods For In Vivo Kinetics. Theory and Application. London: Academic Press.Google Scholar
Smith, G., Weidel, S. E. & Fleck, A. (1994). Albumen catabolic rate and protein-energy depletion. Nutrition (In the Press).Google ScholarPubMed
Tavill, A. S., Craigie, A. & Rosenoer, V. M. (1968). The measurement of the synthetic rate of albumin in man. Clinical Science 34, 1–28.Google ScholarPubMed
Vicra, G. D., Travis, J., Hall, P. K. & Roberts, R. C. (1978). Purification of human alpha-2-macroglobulin by chromatography on Cibacron Blue Sepharose. Analytical Biochemistry 89, 274–278.Google Scholar
Vitek, F., Bianchi, R., Macini, P. & Donato, L. (1969). Deconvolution techniques for the analysis of short-term metabolic studies with radioiodinated albumin. In Physiology and Pathophysiology of Plasma Protein Metabolism, pp. 29–34 [Birke, C., Norberg, R. and Plantin, L. O., editors]. Oxford: Pergamon Press.CrossRefGoogle Scholar
Webster, D. (1977). The immediate reaction between BCG and serum as a measure of albumin content. Clinical Chemistry 23, 663–665.CrossRefGoogle Scholar