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Published in: Intensive Care Medicine 10/2003

01-10-2003 | Original

Efficiency of a cysteine-taurine-threonine-serine supplemented parenteral nutrition in an experimental model of acute inflammation

Authors: Sylwia Osowska, Jean-Pascal De Bandt, Samira Chaïb, Nathalie Neveux, Marie-Pierre Bérard, Luc Cynober

Published in: Intensive Care Medicine | Issue 10/2003

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Abstract

Objective

As is the case with glutamine, requirements for amino acids such as cysteine, taurine, and serine may be increased in stress situations. This study evaluated the potential usefulness of supplementation of total parenteral nutrition with a cysteine, taurine, threonine, and serine mixture (SEAS), with or without glutamine, in an experimental model of turpentine-induced acute inflammation.

Design and setting

Prospective, controlled animal study in male Sprague-Dawley rats.

Interventions

Twenty-seven rats received isonitrogenous, isocaloric total parenteral nutrition (260 kcal/kg, 2 gN/kg per day) for 5 days. They were divided into three groups according to the composition of the amino acid admixture: standard amino acids (control, n=9), standard amino acids partly substituted with SEAS (n=10) or with SEAS and glutamine (n=8). All rats received two subcutaneous turpentine injections (0.5 ml/100 g) 24 h (day 2) and 72 h (day 4) after the initiation of parenteral nutrition and were killed on day 5.

Measurements and results

Nitrogen balance was significantly increased (control 53±29, SEAS 153±21, SEAS+Gln 187±32 mg/24 h) and urinary 3-methylhistidine/creatinine ratio decreased (control 55±4, SEAS 43±4, SEAS+Gln 38±3 µmol/mmol) on day 5 in the two SEAS-treated groups. Hepatic and extensor digitorum longus muscle protein contents were significantly higher in the SEAS+Gln-treated group than in the other two groups. In addition to slight differences in liver amino acid content, other parameters including liver glutathione did not differ significantly between groups.

Conclusions

Improved nitrogen balance and reduction in urinary 3-methylhistidine suggest that SEAS supplementation improves nitrogen homeostasis in an experimental model of acute inflammation. Glutamine addition further improves protein status.
Literature
1.
go back to reference Obled C, Papet I, Breuillé D (2002) Metabolic bases of amino acid requirements in acute diseases. Curr Opin Clin Nutr Metab Care 5:189–197CrossRefPubMed Obled C, Papet I, Breuillé D (2002) Metabolic bases of amino acid requirements in acute diseases. Curr Opin Clin Nutr Metab Care 5:189–197CrossRefPubMed
2.
go back to reference Malmezat T, Breuillé D, Pouyet C, Patureau-Mirand P, Obled C (1998) Metabolism of cysteine is modified during the acute phase of sepsis in rats. J Nutr 128:97–105PubMed Malmezat T, Breuillé D, Pouyet C, Patureau-Mirand P, Obled C (1998) Metabolism of cysteine is modified during the acute phase of sepsis in rats. J Nutr 128:97–105PubMed
3.
go back to reference Malmezat T, Breuillé D, Capitan P, Mirand PP, Obled C (2000) Glutathione turnover is increased during the acute phase of sepsis in rats. J Nutr 130:1239–1246PubMed Malmezat T, Breuillé D, Capitan P, Mirand PP, Obled C (2000) Glutathione turnover is increased during the acute phase of sepsis in rats. J Nutr 130:1239–1246PubMed
4.
go back to reference Haussinger D, Roth E, Lang F, Gerok W (1993) Cellular hydration state: an important determinant of protein catabolism in health and disease. Lancet 341:1330–1332PubMed Haussinger D, Roth E, Lang F, Gerok W (1993) Cellular hydration state: an important determinant of protein catabolism in health and disease. Lancet 341:1330–1332PubMed
5.
go back to reference Schaffer S, Takahashi K, Azuma J (2000) Role of osmoregulation in the actions of taurine. Amino Acids 19:527–546CrossRefPubMed Schaffer S, Takahashi K, Azuma J (2000) Role of osmoregulation in the actions of taurine. Amino Acids 19:527–546CrossRefPubMed
6.
go back to reference Gregory JF 3rd, Cuskelly GJ, Shane B, Toth JP, Baumgartner TG, Stacpoole PW (2000) Primed, constant infusion with [2H3]serine allows in vivo kinetic measurement of serine turnover, homocysteine remethylation, and transsulfuration processes in human one-carbon metabolism. Am J Clin Nutr 72:1535–1541PubMed Gregory JF 3rd, Cuskelly GJ, Shane B, Toth JP, Baumgartner TG, Stacpoole PW (2000) Primed, constant infusion with [2H3]serine allows in vivo kinetic measurement of serine turnover, homocysteine remethylation, and transsulfuration processes in human one-carbon metabolism. Am J Clin Nutr 72:1535–1541PubMed
7.
go back to reference Laurichesse H, Tauveron I, Gourdon F, Cormerais L, Champredon C, Charrier S, Rochon C, Lamain S, Bayle G, Laveran H, Thieblot P, Beytout J, Grizard J (1998) Threonine and methionine are limiting amino acids for protein synthesis in patients with AIDS. J Nutr 128:1342–1348PubMed Laurichesse H, Tauveron I, Gourdon F, Cormerais L, Champredon C, Charrier S, Rochon C, Lamain S, Bayle G, Laveran H, Thieblot P, Beytout J, Grizard J (1998) Threonine and methionine are limiting amino acids for protein synthesis in patients with AIDS. J Nutr 128:1342–1348PubMed
8.
go back to reference Kelly D, Wischmeyer PE (2003) Role of L-glutamine in critical illness: new insights. Curr Opin Clin Nutr Metab Care 6:217–222CrossRefPubMed Kelly D, Wischmeyer PE (2003) Role of L-glutamine in critical illness: new insights. Curr Opin Clin Nutr Metab Care 6:217–222CrossRefPubMed
9.
go back to reference De Bandt JP, Cynober L (1998) Amino acids with anabolic properties. Curr Opin Clin Nutr Metab Care 1:263–272CrossRefPubMed De Bandt JP, Cynober L (1998) Amino acids with anabolic properties. Curr Opin Clin Nutr Metab Care 1:263–272CrossRefPubMed
10.
go back to reference Roth E, Oehler R, Manhart N, Exner R, Wessner B, Strasser E, Spittler A (2002) Regulative potential of glutamine-relation to glutathione metabolism. Nutrition 18:217–221CrossRefPubMed Roth E, Oehler R, Manhart N, Exner R, Wessner B, Strasser E, Spittler A (2002) Regulative potential of glutamine-relation to glutathione metabolism. Nutrition 18:217–221CrossRefPubMed
11.
go back to reference Wusteman M, Hayes A, Stirling D, Elia M (1994) Changes in protein distribution in the rat during prolonged "systemic injury." J Surg Res 56:331–337 Wusteman M, Hayes A, Stirling D, Elia M (1994) Changes in protein distribution in the rat during prolonged "systemic injury." J Surg Res 56:331–337
12.
go back to reference Wusteman M, Wight DG, Elia M (1990) Protein metabolism after injury with turpentine: a rat model for clinical trauma. Am J Physiol 259:E763–E769PubMed Wusteman M, Wight DG, Elia M (1990) Protein metabolism after injury with turpentine: a rat model for clinical trauma. Am J Physiol 259:E763–E769PubMed
13.
go back to reference Gornall AG, Bardawil CJ, David MM (1949) Determination of serum protein by means of the biuret reaction. J Biol Chem 177:751–766 Gornall AG, Bardawil CJ, David MM (1949) Determination of serum protein by means of the biuret reaction. J Biol Chem 177:751–766
14.
go back to reference Powanda MC, Cockerell GL, Pekarek RS (1973) Amino acid and zinc movement in relation to protein synthesis early in inflammation. Am J Physiol 225:399–401PubMed Powanda MC, Cockerell GL, Pekarek RS (1973) Amino acid and zinc movement in relation to protein synthesis early in inflammation. Am J Physiol 225:399–401PubMed
15.
go back to reference Saadane A, Neveux N, Feldmann G, Lardeux B, Bleiberg-Daniel F (1996) Inhibition of liver RNA breakdown during acute inflammation in the rat. Biochem J 317:907–912PubMed Saadane A, Neveux N, Feldmann G, Lardeux B, Bleiberg-Daniel F (1996) Inhibition of liver RNA breakdown during acute inflammation in the rat. Biochem J 317:907–912PubMed
16.
go back to reference Rennie MJ, MacLennan PA, Hundal HS, Weryk B, Smith K, Taylor PM, Egan C, Watt PW (1989) Skeletal muscle glutamine transport, intramuscular glutamine concentration and muscle protein turnover. Metabolism 38:47–51PubMed Rennie MJ, MacLennan PA, Hundal HS, Weryk B, Smith K, Taylor PM, Egan C, Watt PW (1989) Skeletal muscle glutamine transport, intramuscular glutamine concentration and muscle protein turnover. Metabolism 38:47–51PubMed
17.
go back to reference Hallbrucker C, Vom Dahl S, Lang F, Haussinger D (1991) Control of hepatic proteolysis by amino acids. The role of cell volume. Eur J Biochem 197:717–724PubMed Hallbrucker C, Vom Dahl S, Lang F, Haussinger D (1991) Control of hepatic proteolysis by amino acids. The role of cell volume. Eur J Biochem 197:717–724PubMed
18.
19.
go back to reference Hunter EA, Grimble RF (1997) Dietary sulphur amino acid adequacy influences glutathione synthesis and glutathione-dependent enzymes during the inflammatory response to endotoxin and tumour necrosis factor-alpha in rats. Clin Sci (Lond) 92:297–305 Hunter EA, Grimble RF (1997) Dietary sulphur amino acid adequacy influences glutathione synthesis and glutathione-dependent enzymes during the inflammatory response to endotoxin and tumour necrosis factor-alpha in rats. Clin Sci (Lond) 92:297–305
20.
go back to reference Jahoor F, Wykes LJ, Reeds PJ, Henry JF, del Rosario MP, Frazer ME (1995) Protein-deficient pigs cannot maintain reduced glutathione homeostasis when subjected to the stress of inflammation. J Nutr 125:1462–1472PubMed Jahoor F, Wykes LJ, Reeds PJ, Henry JF, del Rosario MP, Frazer ME (1995) Protein-deficient pigs cannot maintain reduced glutathione homeostasis when subjected to the stress of inflammation. J Nutr 125:1462–1472PubMed
Metadata
Title
Efficiency of a cysteine-taurine-threonine-serine supplemented parenteral nutrition in an experimental model of acute inflammation
Authors
Sylwia Osowska
Jean-Pascal De Bandt
Samira Chaïb
Nathalie Neveux
Marie-Pierre Bérard
Luc Cynober
Publication date
01-10-2003
Publisher
Springer-Verlag
Published in
Intensive Care Medicine / Issue 10/2003
Print ISSN: 0342-4642
Electronic ISSN: 1432-1238
DOI
https://doi.org/10.1007/s00134-003-1878-9

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