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Serum proteinase inhibitors and other serum proteins in protein-energy malnutrition

Published online by Cambridge University Press:  24 October 2018

F. P. Schelp ,
P. Migasena ,
Praneet Pongpaew ,
W. H. P. Schreurs  and
Venus Supawan
F. P. Schelp
Affiliation:
Department of Tropical Nutrition and Food Science, Faculty of Tropical Medicine, Mahidol University, Bangkok 4, Thailand
P. Migasena
Affiliation:
Department of Tropical Nutrition and Food Science, Faculty of Tropical Medicine, Mahidol University, Bangkok 4, Thailand
Praneet Pongpaew
Affiliation:
Department of Tropical Nutrition and Food Science, Faculty of Tropical Medicine, Mahidol University, Bangkok 4, Thailand
W. H. P. Schreurs
Affiliation:
Department of Tropical Nutrition and Food Science, Faculty of Tropical Medicine, Mahidol University, Bangkok 4, Thailand
Venus Supawan
Affiliation:
Department of Tropical Nutrition and Food Science, Faculty of Tropical Medicine, Mahidol University, Bangkok 4, Thailand
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Abstract

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  1. 1. The concentrations of serum protein albumin, prealbumin and transferrin were determined in twentyeight cases of protein-energy malnutrition (PEM) with infection, together with the levels of serum proteinase inhibitors (PI), α1-antitrypsin (AT), α1-antichymotrypsin (Ach), α2-macroglobulin (α2M) and inter-α-trypsin inhibitor (IαI).

  2. 2. Albumin, prealbumin and transferrin concentrations, as well as the levels of PI, IαI and α2M were found to be lower in cases of PEM associated with infection than the corresponding values for a group of healthy Thai preschool children and a group of newborn Thai children, but despite starvation AT and Ach values generally were increased.

  3. 3. The results provide support for the hypothesis that PI, especially AT and Ach might limit the synthesis of albumin, prealbumin and transferrin in PEM associated with infection, via the inhibition of the mobilization of body's own protein.

Type
Papers of direct relevance to Clinical and Human Nutrition
Information
British Journal of Nutrition , Volume 38 , Issue 1 , July 1977 , pp. 31 - 38
Copyright
Copyright © The Nutrition Society 1977

References

Alper, C. A. (1974). New Engl. J. Med. 219, 287.CrossRefGoogle Scholar
Aronsen, K. F., Ekelund, G., Kindmark, C. O. & Laurell, C. B. (1972). Scand. J. din. Lab. Invest. 29, Suppl. 124, 127.CrossRefGoogle Scholar
Beisel, W. R. (1972). Am. J. din. Nutr. 25, 1254.CrossRefGoogle Scholar
Campbell, R. C. (1967). Statistics for Biologists. London: Cambridge University Press.Google Scholar
Dugdale, A. E. (1971). Am. J. din. Nutr. 24, 174.CrossRefGoogle Scholar
Farrow, S. P. & Baar, S. (1973). Clinica chim. Acta 46, 39.CrossRefGoogle Scholar
Hoffmeister, H. & Schuett, K. H. (1972). Dt. med. Wschr. 97, 1464.CrossRefGoogle Scholar
Ingenbleek, Y., De Visscher, M. & De Nayer, Ph. (1972). Lancet 11, 106.CrossRefGoogle Scholar
Ingenbleek, Y., Van den Schrieck, H. G., De Nayer, Ph. & De Visscher, M. (1975). Clinica chim. Acta 63, 61.CrossRefGoogle Scholar
Johansson, B. G., Kindmark, C. O., Trell, E. Y. & Wollheim, F. A. (1972). Scand. J. din. Lab. Invest. 29, Suppl. 124, 117.CrossRefGoogle Scholar
Kueppers, F. (1971). Humangenetik 11, 117.Google Scholar
Laurell, C. B. (1972). Scand. J. din. Lab. Invest. 29, Suppl. 124, 21.CrossRefGoogle Scholar
Ohlsson, K. (1971). Scand. J. din. Lab. Invest. 28, 251.CrossRefGoogle Scholar
Ohlsson, K. V. (1974). In Proteinase Inhibitors, p. 96 [H. Fritz, H. Tschesche, L. J. Greene and E. Truscheit, editors]. Berlin, Heidelberg and New York: Springer Verlag.Google Scholar
Orell, S. R. & Mazodier, P. (1972). In Pulmonary Emphysema and Proteolysis, p. 69 [C. Mittman, editor]. New York: Academic Press.Google Scholar
Pongpaew, P., Migasena, P. & Schelp, F. P. (1975). J. med. Ass. Thailand. 58, 15.Google Scholar
Razban, S. Z., Olusi, S. O., Ade-Serrano, M. A., Osunkoya, B. O., Adeshina, H. A. & McFarlane, H. (1975). J. trop. Med. Hyg. 78, 264.Google Scholar
Scrimshaw, N. S., Taylor, C. E. & Gordon, J. E. (1968). W.H.O. Monogr. Ser. no. 57.Google Scholar
Steinbuch, M. & Audran, R. (1974). In Proteinase Inhibitors, p. 78 [H. Fritz, H. Tschesche, L. J. Greene and E. Truscheit, editors]. Berlin, Heidelberg and New York: Springer Verlag.Google Scholar
Stuart, H. C. & Stevenson, S. S. (1959). In Textbook of Paediatrics, 7th ed., p. 12 [W. E. Nelson, editor]. Philadelphia: W. Saunders & Co.Google Scholar
Sveger, T. & Ekelund, H. (1975). ActaPaediat. scand. 64, 763.Google Scholar
Vahlquist, A., Rask, L., Peterson, P. A. & Berg, T. (1975). Scand. J. din. Lab. Invest. 35, 569.CrossRefGoogle Scholar
Waterlow, J. C. (1972). Br. med. J. iii, 566.CrossRefGoogle Scholar
Whitehead, R. G. & Alleyne, G. A. O. (1972). Br. med. Bull. 28, 72.CrossRefGoogle Scholar
Whitehead, R. G., Coward, W. A. & Lunn, P. G. (1973). Lancet 1, 63. Google Scholar
Weidermann, O., Wiedermannova, A. P., Vaerman, J. P. & Heremans, J. F. (1970). J. infect. Dis. 121, 74.CrossRefGoogle Scholar
Weidermann, O., Wiedermannova, A. P., Vaerman, J. P. & Heremans, J. F. (1970). J. infect. Dis. 121, 74.CrossRefGoogle Scholar