Advances in Clinical and Experimental Medicine

Title abbreviation: Adv Clin Exp Med
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Advances in Clinical and Experimental Medicine

2014, vol. 23, nr 3, May-June, p. 423–431

Publication type: original article

Language: English

Is Additional Enrichment of Diet in Branched-Chain Amino Acids or Glutamine Beneficial for Patients Receiving Total Parenteral Nutrition after Gastrointestinal Cancer Surgery?

Maria Szpetnar1,A,C,D, Przemysław Matras2,A,B, Anna Boguszewska-Czubara1,C,D, Małgorzata Kiełczykowska1,B,D, Sławomir Rudzki2,E,F, Irena Musik1,E,F

1 Chair and Cepartment of Medical chemistry, Medical University of Lublin, Lublin, Poland

2 1st Chair and Department of General and Transplant Surgery and Nutritional Treatment, Medical University of Lublin, Lublin, Poland

Abstract

Objectives. Total Parenteral Nutrition (TPN) is necessary in patients unable to receive oral or enteral feeding for a period of at least 7 days. branched-chain amino acids (bcaa): valine (Val), leucine (Leu), and isoleucine (Ile) are essential amino acids, which are important regulators in protein metabolism. They are also the main nitrogen source for glutamine synthesis in muscles. In this process they undergo irreversible degradation and cannot be reutilised for protein synthesis. In catabolic states, like cancers, glutamine demand increases and therefore also its utilisation, which can decrease the level of bcaa required for Gln synthesis. The purpose of this study was to evaluate the necessity of bcaa or glutamine-enriched TPN in patients after gastrointestinal cancers surgery.
Material and Methods. Our aim was to investigate changes of plasma bcaa and glutamine concentrations in patients operated for colorectal, small intestine or pancreatic cancer and who are either receiving TPN or not in the postoperative period. free amino acids plasma concentrations were determined by the ion-exchange chromatography.
Results. Surgery in the control group caused a decrease in Val, Ile and Leu concentrations in the postoperative period. In TPN patients this depression was inhibited beginning from the third day after surgery, except for Val and Leu in colorectal cancer group. In control and TPN patient groups, Gln concentration decreased after the surgery and subsequently increased beginning from the third day after the operation.
Conclusion. Gastrointestinal cancer patients’ surgery results in decrease in bcaa concentrations. Standard TPN exerts a beneficial effect on the bcaa level in patients with pancreatic and small intestine cancer. In colorectal cancer such TPN should be enriched with Leu and Val.

Key words

branched-chain amino acids, glutamine, postoperative TPN, gastrointestinal cancer; surgical stress.

References (36)

  1. Evans WJ, Morley JE, Argiles J: cachexia: a new definition. clin Nutr 2008, 27, 793–799.
  2. Mantovani G, Madeddu C: cancer cachexia: medical management. Support care cancer 2009, doi: 10.1007/ s00520-009-0722-3.
  3. Argiles JM: cancer-associated malnutrition. eur J Oncol Nurs 2005, 9, Suppl, 39–50.
  4. Noblett SE, Watson DS, Huong H, Davison B, Hainsworth PJ, Horgan AF: Pre-operative oral carbohydrate loading in colorectal surgery: a randomized controlled trial. colorectal dis 2006, 8, 563–569.
  5. Braga M, Ljungqvist O, Soeters P, Weimann A, Bozetti F: eSPeN guidelines on Parenteral Nutrition: surgery. clin Nutr 2009, 28, 378–386.
  6. Weimann A, Braga M, Harsanyi L: eSPeN Guidelines on enteral Nutrition: Surgery including organ transplantation. clin Nutr 2006, 25, 224–244.
  7. Kuhn SK, Muscaritoli M, Wischmeyer P, Stehle P: Glutamine as indispensable nutrient in oncology: experimental and clinical evidence. eur J Nutr 2009, doi: 10.1007/s00394-009-0082-2.
  8. Zaloga GP: Parenteral nutrition in adult patients with functioning gastrointestinal tracts: assessment of outcomes. Lancet 2006, 367, 1101–1111.
  9. Marchesini G, Bianchi G, Merli M, Amodio P, Panellea C, Loguercio C, Rossi Fanelli F, Abbiati R: Nutritional supplementation with branched-chain amino acids in advanced cirrhosis: a double-blind, randomized trial. Gastroenterology 2003, 124, 1792–1801.
  10. Moore S, Spackman DD, Stein WH: chromatography of amino acids on sulfonated polystyrene resins. ann chem 1958, 30, 1185–1189.
  11. Lai HS, Lee JC, Lee PH, Wang ST, Chen WJ: Plasma free amino acid profile in cancer patients. Semin cancer biol 2005, 15, 267–276.
  12. Curi R, Lagranha CJ, Doi SQ, Sellitti DF, Procopio J, Pithon-Curi TC: Glutamine-dependent changes in gene expression and protein activity. cell biochem funct 2005, 23, 77–84.
  13. Lee JC, Chen MJ, Chang CH, Tiai YF, Lin P., Lai HS, Wang ST: Plasma amino acid levels in patients with colorectal cancers and liver cirrhosis with hepatocellular carcinoma. Hepatogastroenterology 2003, 50, 1269–1273.
  14. Soeters PB, Van De Poll MC, Van De Gemert WG, Dejong CH: amino acid adequacy in pathophysiological states. J Nutr 2004, 134 (6 Suppl.), 1575–1582.
  15. Wang XY, Li N, Gu J, Li WQ, Li JS: The effects of the formula of amino acids enriched bcaa on nutritional support in traumatic patients. World J Gastroenterol 2003, 9, 599–602.
  16. Biolo G, De Cicco M, Dal Mas V, Lorenzon S, Antonione R, Ciocchi B, Brazzoni R, Zanetti M, Dore F, Guarnieri G: Response of muscle protein and glutamine kinetics to branched-chain-enriched amino acids in intensive care patients after radical cancer. Nutrition 2006, 22, 475–482.
  17. Moriwaki H, Miwa Y, Tajika M, Kato M, Fukushima H, Shiraki M: branched-chain amino acids as a proteinand energy-source in liver cirrhosis. biochem biophys Res commun 2004, 313, 405–409.
  18. Kawaguchi T, Izumi N, Charlton MR, Sata M: branched-chain amino acids as pharmacological nutrients in chronic liver disease. Hepatology 2011, 54, 1063–1070.
  19. Charlton M: branched-chain amino acid enriched supplements as therapy for liver disease. J Nutr 2006, 136(1 Suppl.), 295–298.
  20. Khanna S, Gopalan S: Role of branched-chain amino acids in liver disease: the evidence for and against. curr Opin clin Nutr Metab care 2007, 10, 297–303.
  21. Holecek M, Muthny T, Kovarik M, Sispera L: Simultaneous infusion of glutamine and branched-chain amino acids (bcaa) to septic rats does not have more favourable effect on protein synthesis in muscle, liver and small intestine than separate infusions. JPeN 2006, 30, 467–473.
  22. Xue H, Sawyer MB, Wischmeyer PE, Baracos VE: Nutrition modulation of gastrointestinal toxicity related to cancer chemotherapy: from preclinical findings to clinical strategy. JPeN 2011, 35, 74–90.
  23. Kaufmann Y, Kornbluth J, Feng Z, Fahr M, Schaefer RF, Klimberg VS: effect of glutamine on the initiation and promotion phases of dMba-induced mammary tumor development. JPeN 2003, 27, 411–418.
  24. Barlett DL, Charland S, Torosian MH: effect of glutamine on tumor and host growth. ann Surg Oncol 1995, 2, 71–76.
  25. Cano NJ, Fouque D, Leverve XM: application of branched-chain amino acids in human pathological states: renal failure. J Nutr 2006, 136 (1 Suppl.), 299–307.
  26. Sun LC, Shih YL, Lu CY, Hsieh JS, Chuang JF, Chen FM, Ma CJ, Wang JY: Randomised, controlled study of branched chain amino-acid-enriched total parenteral nutrition in malnourished patients with gastrointestinal cancer undergoing surgery. am Surg 2008, 74, 237–242.
  27. Kimball SR, Jefferson LS: Signaling pathways and molecular mechanisms through which branched – chain amino acids mediate translational control of protein synthesis. J Nutr 2006, 136 (1 Suppl.), 227–231.
  28. Suryawan A, O’Connor PM, Bush JA, Nguyen HV, Davis TA: differential regulation of protein synthesis by amino acids and insulin in peripheral and visceral tissues of neonatal pigs. amino acids 2009, 37, 97–104.
  29. Meyer C, Woerle HJ, Gerich J: Paradoxical changes of muscle glutamine release during hyperinsulinemia, euglycemia and hypoglycemia in humans: further evidence for the glucose-glutamine cycle. Metabolism 2004, 53, 1208–1214.
  30. Holecek M: Three targets of branched-chain amino acid supplementation in the treatment of liver disease. Nutrition 2010, 26, 482–490.
  31. Biolo G, De Cicco M, Dal Mas V, Lorenzon S, Antonione R, Ciocchi B, Barazzoni R, Zanetti M, Dore F, Guarnieri G: Response of muscle protein and glutamine kinetics to branched-chain-enriched amino acids in intensive care patients after radical cancer surgery. Nutrition 2006, 11, 475–482.
  32. Yoshizawa F: Regulation of protein synthesis by branched-chain amino acids in vivo. biochem biophys Res commun 2004, 313, 417–422.
  33. Wu G: amino acids: metabolism, functions, and nutrition. amino acids 2009, 37, 1–17.
  34. Murata K, Moriyama M: Isoleucine, an essential amino acid, prevents liver metastases of colon cancer by antiangiogenesis. cancer Res 2007, 67, 3263–3268.
  35. Lynch CJ, Hutson SM, Patson BJ, Vaval A, Vary TC: Tissue-specific effects of chronic dietary leucine and norleucine supplementation on protein synthesis in rats. am J Physiol endocrinol Metab 2002, 283, 824–835.
  36. Szpetnar M, Matras P, Kiełczykowska M, Horecka A, Bartoszewska L, Pasternak K, Rudzki S: antioxidants in patients receiving total parenteral nutrition after gastrointestinal cancer surgery. Cell Biochem Funct 2012, 30, 211–216.
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