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Protein quantity, not protein quality, accelerates whole-body leucine kinetics and the acute-phase response during acute infection in marasmic Malawian children

Published online by Cambridge University Press:  09 March 2007

M. J. Manary ,
K. E. Yarasheski ,
S. Smith ,
E. T. Abrams  and
C. A. Hart
M. J. Manary*
Affiliation:
College of Medicine, University of Malawi, Private Bag 360, Blantyre 3, Malawi Departments of Pediatrics and Internal Medicine, Washington University School of Medicine, St Louis, MO 63110, USA
K. E. Yarasheski
Affiliation:
Departments of Pediatrics and Internal Medicine, Washington University School of Medicine, St Louis, MO 63110, USA
S. Smith
Affiliation:
Departments of Pediatrics and Internal Medicine, Washington University School of Medicine, St Louis, MO 63110, USA
E. T. Abrams
Affiliation:
Department of Anthropology, University of Michigan, Ann Arbor, MI 48109, USA
C. A. Hart
Affiliation:
Department of Medical Microbiology, University of Liverpool, Liverpool, L69 3GA, UK
*
*Corresponding author: Dr Mark J. Manary, fax +1 314 454 4345, email manary@kids.wustl.edu
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Abstract

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The present study compared leucine kinetics and acute-phase-protein concentrations in three groups of marasmic, acutely infected Malawian children fed one of three isoenergetic diets. These were: an enhanced-protein-quality diet (egg-white+tryptophan, providing 1.2 g protein/kg per d; n 14); an increased-protein-content diet (egg-white+tryptophan, providing 1·8 g protein/kg per d; n 14); a standard-protein diet (1·2 g milk protein/kg per d; n 25). The hypotheses tested were that children receiving a diet with more protein would have greater rates of non-oxidative leucine disposal and that children receiving an isonitrogenous diet with a higher protein quality would have lower rates of leucine oxidation. The children were studied after 24 h of therapy using standard [13C]leucine stable-isotope tracer techniques. The children receiving the higher-protein-content diet had greater leucine kinetic rates than those receiving the standard-protein-content diet; non-oxidative leucine disposal was 170 (SD 52) v. 122 (SD 30) μmol leucine/kg per h (P<0·01). Leucine oxidation was less in the children receiving the enhanced-protein-quality diet than in those receiving the standard-protein-quality diet; 34 (SD 12) v. 45 (SD 13) μmol leucine/kg per h (P<0·05). The children receiving the high-protein-content diet increased their serum concentration for five of six acute-phase proteins 24 h after starting therapy, while those receiving the standard-protein-content diet did not. These data suggest that there was greater whole-body protein synthesis, and a more vigorous acute-phase response associated with the higher-protein-content diet. The clinical benefits associated with a higher protein intake in marasmic, acutely infected children need further study.

Keywords

MalnutritionTherapyProteinAcute-phase response
Type
Research Article
Information
British Journal of Nutrition , Volume 92 , Issue 4 , October 2004 , pp. 589 - 595
Copyright
Copyright © The Nutrition Society 2004

References

Anonymous (1970) Classification of infantile malnutrition. Lancet ii, 302–303.Google Scholar
Bodamer, OA, Leonard, JV, Tasker, RC, Hoffmann, GF & Halliday, D (1997) Protein turnover in critically ill children. Eur J Pediatr 156, S59–S61.CrossRefGoogle ScholarPubMed
Bresson, JL, Mariotti, A, Narcy, P, Ricour, C, Sachs, C & Rey, J (1990) Recovery of [ 13 C]bicarbonate as respiratory 13 CO 2 in parenterally fed infants. Eur J Clin Nutr 44, 3–9.Google Scholar
Burger, GCE, Sandstead, HR & Drummond, J (1945) Starvation in Western Holland. Lancet ii, 282–283.CrossRefGoogle Scholar
Collins, S, Myatt, M & Golden, B (1998) Dietary treatment of severe malnutrition in adults. Am J Clin Nutr 68, 193–199.CrossRefGoogle ScholarPubMed
Gabay, C & Kushner, I (1999) Acute-phase proteins and other systemic responses to inflammation. N Engl J Med 340, 448–454.CrossRefGoogle ScholarPubMed
Garlick, PJ, McNurlan, MA & Ballmer, PE (1991) Influence of dietary protein intake on whole-body protein turnover in humans. Diabetes Care 14, 1189–1198.CrossRefGoogle ScholarPubMed
Golden, MHN (2002) The development of concepts of malnutrition. J Nutr 132 2117S – 2122S.CrossRefGoogle ScholarPubMed
Hasselgren, PO (2000) Catabolic response to stress and injury: implications for regulation. World J Surg 24, 1452–1459.CrossRefGoogle ScholarPubMed
Hoerr, RA, Yu, YM, Wagner, DA, Burke, JF & Young, VR (1989) Recovery of 13 C in breath from NaH 13 CO 3 infused by gut and vein: effect of feeding. Am J Physiol 257, E426–E438.Google Scholar
Jackson, AA, Golden, MH, Byfield, R, Jahoor, F, Royes, J & Soutter, L (1983) Whole-body protein turnover and nitrogen balance in young children at intakes of protein and energy in the region of maintenance. Human Nutr Clin Nutr 37, 433–446.Google ScholarPubMed
Jahoor, F, Gazzard, B, Phillips, G, Sharpstone, D, Delrosario, M, Fraser, ME, Heird, W, Smith, R & Jackson, A (1999) The acute phase protein response to human immunodeficiency virus in human subjects. Am J Physiol 276, E1092–E1098.Google ScholarPubMed
Kadowaki, M & Kanazawa, T (2003) Amino acids as regulators of proteolysis. J Nutr 133 2052S – 2056S.CrossRefGoogle ScholarPubMed
Kee, AJ, Combaret, L, Tilignac, T, Souweine, B, Aurousseau, E, Dalle, M, Taillandier, D & Attaix, D (2003) Ubiquitin-proteasome-dependent muscle proteolysis responds slowly to insulin release and refeeding in starved rats. J Physiol 546, 765–776.CrossRefGoogle ScholarPubMed
Kien, CL & McClead, RE (1996) Estimation of CO 2 production in enterally fed preterm infants using an isotope dilution stable tracer technique. J Parenter Enteral Nutr 20, 389–393.CrossRefGoogle Scholar
Lipscomb, FM (1945) Medical aspects of Belsen concentration camp. Lancet ii, 313–315.CrossRefGoogle Scholar
Long, CL, Jeevanandam, M, Kim, BM & Kinney, JM (1977) Whole body protein synthesis and catabolism in septic man. Am J Clin Nutr 30, 1340–1344.CrossRefGoogle ScholarPubMed
Manary, MJ, Brewster, DR, Broadhead, RL, Graham, SM, Hart, CA, Crowley, JR, Fjeld, CR & Yarasheski, KE (1997) Whole-body protein kinetics in children with kwashiorkor and infection: a comparison of egg white and milk as dietary sources of protein. Am J Clin Nutr 66, 643–648.CrossRefGoogle ScholarPubMed
Manary, MJ, Broadhead, RL & Yarasheski, K (1998) Whole-body protein kinetics in marasmus and kwashiorkor during acute infection. Am J Clin Nutr 67, 1205–1209.CrossRefGoogle ScholarPubMed
Manary, MJ, Yarasheski, KE, Berger, R, Abrams, ET, Hart, CA & Broadhead, RL (2004) Whole-body leucine kinetics and the acute phase response during acute infection in marasmic Malawian children. Pediatr Res 55, 940–956.CrossRefGoogle ScholarPubMed
Manary, MJ, Yarasheski, KE, Berger, R & Broadhead, RL (2003) CO 2 production during acute infection in malnourished Malawian children. Eur J Clin Nutr 58, 116–120.CrossRefGoogle Scholar
Manary, MJ, Yarasheski, KE & Broadhead, RL (2002) Urea production and leucine oxidation in malnourished children with and without infection. Metabolism 51, 1418–1422.CrossRefGoogle Scholar
Martin, SAM, Blaney, S, Bowman, AS & Houlihan, DF (2002) Ubiquitin-proteosome-dependent proteolysis in rainbow trout ( Oncorhynchus mykiss ): effect of food deprivation. Pflugers Arch 445, 257–266.Google Scholar
Matthews, DE, Motil, KJ, Rohrbaugh, DK, Burke, JF, Young, VR & Bier, DM (1980) Measurement of leucine metabolism in man from a primed, continuous infusion of L-[1- 13 C]leucine. Am J Physiol 238, E474–E479.Google Scholar
Reeds, PR, Fjeld, CR & Jahoor, F (1994) Do the differences between the amino acid compositions of acute-phase and muscle proteins have a bearing on nitrogen loss in traumatic stress?. J Nutr 124, 906–910.CrossRefGoogle Scholar
Scrimshaw, NS & SanGiovanni, J (1997) Synergism of nutrition, infection and immunity: an overview. Am J Clin Nutr 66 464S – 477S.CrossRefGoogle ScholarPubMed
Soares, MJ, Piers, LS, Shetty, PS, Jackson, AA & Waterlow, JC (1994) Whole body protein turnover in chronically undernourished individuals. Clin Sci 86, 441–446.CrossRefGoogle ScholarPubMed
Spear, ML, Darmaun, D, Sager, BK, Parsons, WR & Haymond, MW (1995) Use of [ 13 C]bicarbonate for measurement of CO 2 production. Am J Physiol 268, E1123–E1127.Google Scholar
Szalai, AJ, Briles, DE & Volanakis, JE (1995) Human C-reactive protein is protective against fatal Streptococcus pneumoniae infection in transgenic mice. J Immunol 155, 2557–2563.CrossRefGoogle ScholarPubMed
Tissot, S, Delafosse, B, Normand, S, Bouffard, Y, Annat, G, Viale, JP, Pachiaudi, C, Riou, JP & Motin, J (1993) Recovery of [ 13 C]bicarbonate as respiratory 13 CO 2 in mechanically ventilated patients. Am J Clin Nutr 57, 202–206.CrossRefGoogle Scholar
Waterlow, JC (1992) Protein-energy Malnutrition, London: Edward Arnold.Google Scholar
World Health OrganizationWorld Health Organization (1999) Management of Severe Malnutrition: a Manual for Physicians and Other Senior Health Workers. Geneva: WHO.Google Scholar