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A sulfur amino acid deficiency changes the amino acid composition of body protein in piglets

Published online by Cambridge University Press:  04 March 2010

J. A. Conde-Aguilera ,
R. Barea ,
N. Le Floc’h ,
L. Lefaucheur  and
J. van Milgen
J. A. Conde-Aguilera
Affiliation:
INRA, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35000 Rennes, France Institute of Animal Nutrition (IFNA), Estación Experimental del Zaidín (CSIC), Cno. del Jueves s/n, 18100 Armilla, Granada, Spain
R. Barea
Affiliation:
INRA, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35000 Rennes, France
N. Le Floc’h
Affiliation:
INRA, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35000 Rennes, France
L. Lefaucheur
Affiliation:
INRA, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35000 Rennes, France
J. van Milgen*
Affiliation:
INRA, UMR1079 Systèmes d’Elevage Nutrition Animale et Humaine, F-35590 Saint-Gilles, France
*
†E-mail: jaap.vanmilgen@rennes.inra.fr
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Abstract

Experiments carried out to determine the amino acid requirement in growing animals are often based on the premise that the amino acid composition of body protein is constant. However, there are indications that this assumption may not be correct. The objective of this study was to test the effect of feeding piglets a diet deficient or not in total sulfur amino acids (TSAA; Met + Cys) on nitrogen retention and amino acid composition of proteins in different body compartments. Six blocks of three pigs each were used in a combined comparative slaughter and nitrogen balance study. One piglet in each block was slaughtered at 42 days of age, whereas the other piglets received a diet deficient or not in TSAA for 19 days and were slaughtered thereafter. Two diets were formulated to provide either 0.20% Met and 0.45% TSAA (on a standardized ileal digestible basis) or 0.46% Met and 0.70% TSAA. Diets were offered approximately 25% below ad libitum intake. At slaughter, the whole animal was divided into carcass, blood, intestines, liver, and the combined head, tail, feet and other organs (HFTO), which were analyzed for nitrogen and amino acid contents. Samples of the longissimus muscle (LM) were analyzed for myosin heavy chain (MyHC) and actin contents. Nitrogen retention was 20% lower in piglets receiving the TSAA-deficient diet (P < 0.01). In these piglets, the nitrogen content in tissue gain was lower in the empty body, carcass, LM and blood (P < 0.05) or tended to be lower in HFTO (P < 0.10), but was not different in the intestines and liver. The Met content in retained protein was lower in the empty body, LM and blood (P < 0.05), and tended to be lower in the carcass (P < 0.10). The Cys content was lower in LM, but higher in blood of piglets receiving the TSAA-deficient diet (P < 0.05). Skeletal muscle appeared to be affected most by the TSAA deficiency. In LM, the Met content in retained protein was reduced by 12% and total Met retention by more than 60%. The MyHC and actin contents in LM were not affected by the TSAA content of the diet. These results show that a deficient TSAA supply affects the amino acid composition of different body proteins. This questions the use of a constant ideal amino acid profile to express dietary amino acid requirements, but also illustrates the plasticity of the animal to cope with nutritional challenges.

Keywords

amino acidbody compositionpigmethioninecysteine
Type
Full Paper
Information
animal , Volume 4 , Issue 8 , August 2010 , pp. 1349 - 1358
Copyright
Copyright © The Animal Consortium 2010

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Footnotes

a

Supported by a research visitor grant from the Ministry of Education and Science (Spain).

b

Supported by a Postdoctoral/Fulbright grant from the Ministry of Education and Science (Spain). Present address: Institute of Animal Nutrition (IFNA), Estación Experimental del Zaidín (CSIC), Cno. del Jueves s/n, 18100 Armilla, Granada, Spain.

References

Batterham, ES, Andersen, LM, Baigent, DR, White, E 1990. Utilization of ileal digestible amino acids by growing pigs: effect of dietary lysine concentration on efficiency of lysine retention. The British Journal of Nutrition 64, 81–94.CrossRefGoogle ScholarPubMed
Bikker, P, Verstegen, MWA, Bosch, MW 1994. Amino acid composition of growing pigs is affected by protein and energy intake. The Journal of Nutrition 124, 1961–1969.CrossRefGoogle ScholarPubMed
Bunce, GE, King, KW 1969. Amino acid retention and balance in the young rat fed varying levels of lactalbumin. The Journal of Nutrition 98, 159–167.CrossRefGoogle Scholar
Campbell, RG, Taverner, MR, Rayner, CJ 1988. The tissue and dietary protein and amino acid requirements of pigs from 8 to 20 kg live weight. Animal Production 46, 283–290.Google Scholar
Candiano, G, Bruschi, M, Musante, L, Santucci, L, Ghiggeri, GM, Carnemolla, B, Orecchia, P, Zardi, L, Righetti, PG 2004. Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25, 1327–1333.CrossRefGoogle Scholar
Chung, TK, Baker, DH 1992a. Maximal portion of the young pig’s sulfur amino acid requirement that can be furnished by cystine. Journal of Animal Science 70, 1182–1187.CrossRefGoogle Scholar
Chung, TK, Baker, DH 1992b. Efficiency of dietary methionine utilization by young pigs. The Journal of Nutrition 122, 1862–1869.CrossRefGoogle ScholarPubMed
Ebner, S, Schoknecht, P, Reeds, P, Burrin, D 1994. Growth and metabolism of gastrointestinal and skeletal muscle tissues in protein-malnourished neonatal pigs. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology 266, R1736–R1743.CrossRefGoogle ScholarPubMed
Gahl, MJ, Crenshaw, TD, Benevenga, NJ 1995. Diminishing returns in weight, nitrogen, and lysine gain of pigs fed six levels of lysine from three supplemental sources. Journal of Animal Science 73, 3177–3187.Google Scholar
Gahl, MJ, Finke, MD, Crenshaw, TD, Benevenga, NJ 1996. Efficiency of lysine or threonine retention in growing rats fed diets limiting in either lysine or threonine. The Journal of Nutrition 126, 3090–3099.CrossRefGoogle ScholarPubMed
Hamard, A, Sève, B, Le Floc’h, N 2007. Intestinal development and growth performance of early-weaned piglets fed a low-threonine diet. Animal 1, 1134–1142.Google Scholar
Hamard, A, Sève, B, Le Floc’h, N 2009. A moderate threonine deficiency differently affects protein metabolism in tissues of early-weaned piglets. Comparative Biochemistry and Physiology. Part A, Comparative Physiology 152, 491–497.CrossRefGoogle ScholarPubMed
Harris, CI, Milne, G 1981. The inadequacy of urinary Nτ-methyl histidine excretion in the pig as a measure of muscle protein breakdown. The British Journal of Nutrition 45, 423–429.Google Scholar
Henry, Y 1993. Affinement du concept de la protéine idéale pour le porc en croissance. INRA Productions Animales 6, 199–212.Google Scholar
Kyriazakis, I, Emmans, GC, McDaniel, R 1993. Whole body amino acid composition of the growing pig. Journal of the Science of Food and Agriculture 62, 29–33.CrossRefGoogle Scholar
Le Bellego, L, Noblet, J 2002. Performance and utilization of dietary energy and amino acids in piglets fed low protein diets. Livestock Production Science 76, 45–58.Google Scholar
Lefaucheur, L, Ecolan, P, Lossec, G, Gabillard, JC, Butler-Browne, G, Herpin, P 2001. Influence of early postnatal cold exposure on myofiber maturation in pig skeletal muscle. Journal of Muscle Research and Cell Motility 22, 439–452.CrossRefGoogle ScholarPubMed
Mahan, DC, JrShields, RG 1998. Essential and nonessential amino acid composition of pigs from birth to 145 kilograms of body weight, and comparison to other studies. Journal of Animal Science 76, 513–521.CrossRefGoogle ScholarPubMed
Martinez-Ramirez, HR, Jeaurond, EA, de Lange, CFM 2008. Dynamics of body protein deposition and changes in body composition following sudden changes in amino acid intake: I. Barrows. Journal of Animal Science 86, 2156–2167.CrossRefGoogle Scholar
Noblet, J, Fortune, H, Shi, XS, Dubois, S 1994. Prediction of net energy value of feeds for growing pigs. Journal of Animal Science 72, 344–354.CrossRefGoogle ScholarPubMed
NRC 1998. Nutrient requirements of swine, 10th revised edition. National Academy Press, Washington, DC, USA.Google Scholar
Pearson, AM, Young, RB 1989. Muscle and meat biochemistry. Academic Press, London, UK.Google Scholar
Purchas, RW, Morel, PCH, Janz, JAM, Wilkinson, BHP 2009. Chemical composition characteristics of the longissimus and semimembranosus muscles for pigs from New Zealand and Singapore. Meat Science 81, 540–548.Google Scholar
Richie, JP, Komninou, D, Leutzinger, Y, Kleinman, W, Orentreich, N, Malloy, V, Zimmerman, JA 2004. Tissue glutathione and cysteine levels in methionine-restricted rats. Nutrition 20, 800–805.CrossRefGoogle ScholarPubMed
Riley, DA, Bain, JLW, Thompson, JL, Fitts, RH, Widrick, JJ, Trappe, SW, Trappe, TA, Costill, DL 2000. Decreased thin filament density and length in human atrophic soleus muscle fibers after spaceflight. Journal of Applied Physiology 88, 567–572.CrossRefGoogle ScholarPubMed
Sauvant, D, Perez, J-M, Tran, G 2004. Tables of composition and nutritional value of feed materials. Pigs, poultry, cattle, sheep, goats, rabbits, horses, fish. INRA Editions, Paris, France.CrossRefGoogle Scholar
Sève, B, Le Floc’h, N 1998. Valorisation mutuelle du L-tryptophane et de la L-thréonine supplémentaires dans l’aliment deuxième âge du porcelet. Rôle de la thréonine déshydrogénase hépatique. Journées de la Recherche Porcine en France 30, 209–216.Google Scholar
Stibler, H, Edström, L, Ahlbeck, K, Remahl, S, Ansved, T 2003. Electrophoretic determination of the myosin/actin ratio in the diagnosis of critical illness myopathy. Intensive Care Medicine 29, 1515–1527.CrossRefGoogle ScholarPubMed
van Milgen, J, Brossard, L, Le Floc’h, N, Rademacher, M 2007. Dietary methionine supply affects the amino acid composition of body proteins. In 2nd International symposium on energy and protein metabolism and nutrition, Vichy, France (ed. I Ortigues-Marty), pp. 93–94. Wageningen Academic Publishers, Wageningen, the Netherlands.Google Scholar
Wei, H-W, Fuller, M 2006. Dietary deficiencies of single amino acids: whole-body amino acid composition of adult rats. Archives of Animal Nutrition 60, 119–130.CrossRefGoogle ScholarPubMed