Quantitative and qualitative aspects of nitrogen supply in enteral nutrition in relation to free amino acids and peptides

Metabolic and Therapeutic Aspects of Amino Acids in Clinical Nutrition, Second Edition

Volumn , Issue , 2003, Pages 529-556

  Grimble, George K ^a  

^a UNIVERSITY OF ROEHAMPTON   (United Kingdom)

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EID: 34249815372     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (189)

1. Althausen, T.L., Uyeyama, K., and Simpson, R.G., Digestion and absorption after massive resection of the small intestine. I. Utilization of food from a “natural” versus a “synthetic” diet and a comparison of intestinal absorption tests with nutritional balance studies in a patient with only 45 cm of small intestine, Gastroenterology, 12, 795, 1949.
2. Silk, D.B.A., Enteral diets: clinical uses and formulation, in Artificial Nutrition Support in Clinical Practice, 2nd ed., Payne-James, J.J., Grimble, G.K., and Silk, D.B.A., Eds., Greenwich Medical Media, London, 2001, p. 303.
3. Loewi, O., Über Eiweisssynthese im Tierkörper [On protein synthesis in the animal body], Arch. Exp. Path. Pharmakol., 48, 303, 1901.
4. Loewi, O., Zur frage nach der bildung von zucker aus fett, Arch. Exp. Path. Pharmakol., 47, 68, 1901.
5. Henriques, V. and Andersen, A.C., Über parenterale Ernährung durch intravenöse Injektion [On parenteral nutrition through intravenous injection], Hoppe Seylers Z. Physiol. Chem., 88, 357, 1913.
6. van Slyke, D.D. and Meyer, G.M., The fate of protein digestion products in the body. III. The absorption of amino acids from the blood by the tissues, J. Biol. Chem., 16, 197, 1913.
7. Elman, R., Parenteral Alimentation in Surgery, with Special Reference to Proteins and Amino Acids, Paul B. Hoeber Inc., New York, 1947.
8. Bunge, C., Lehrbuch Der Physiologischen Und Pathologischen Chemie, in Zwanzig Vorlesungen Für Ärzte Und Studierende, 4th ed., Verlag von F.C.W.Vogel, Leipzig, Germany, 1887, p. 168.
9. Fruton, J.S., Molecules and Life: Historical Essays on the Interplay of Chemistry and Biology, Wiley Interscience, New York, 1972.
10. Grimble, G.K. and Backwell, F.R.C., Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, Portland Press, London, 1997.
11. Botbol, V. and Scornik, O.A., Measurement of instant rates of protein degradation in the livers of intact mice by the accumulation of bestatin-induced peptides, J. Biol. Chem., 266, 2151, 1991.
12. Zhou, X., Thamotharan, M., Gangopadhyay, A., Serdikoff, C., and Adibi, S.A., Characterization of an oligopeptide transporter in renal lysosomes, Biochim. Biophys. Acta, 1466, 372, 2000.
13. Shennan, D.B., Calvert, D.T., Backwell, F.R., and Boyd, C.A.R., Peptide aminonitrogen transport by the lactating rat mammary gland, Biochim. Biophys. Acta, 1373, 252, 1998.
14. MacLarnon, A.M., Martin, R.D., Chivers, D.J., and Hladnik, C.M., Some aspects of gastrointestinal allometry in primates and other mammals, in Definition et Origines de l’Homme, 1st ed., Sakka, M., Ed., CNRS, Paris, 1983, p. 293.
15. O’Connor, T.P., Lam, M.M., and Diamond, J., Magnitude of functional adaptation after intestinal resection, Am. J. Physiol., 276, R1265, 1999.
16. Stoll, B., Burrin, D.G., Henry, J., Yu, H., Jahoor, F., and Reeds, P.J., Substrate oxidation by the portal drained viscera of fed piglets, Am. J. Physiol., 277, E168, 1999.
17. Austgen, T.R., Chen, M.K., Flynn, T.C., and Souba, W.W., The effects of endotoxin on the splanchnic metabolism of glutamine and related substrates, J. Trauma, 31, 742, 1991.
18. Reeds, P.J., Burrin, D.G., Jahoor, F., Wykes, L., Henry, J., and Frazer, E.M., Enteral glutamate is almost completely metabolized in first pass by the gastrointestinal tract of infant pigs, Am. J. Physiol., 270, E413, 1996.
19. Lambert, B.D., Stoll, B., Niinikoski, H., Pierzynowski, S., and Burrin, D.G., Net portal absorption of enterally fed alpha-ketoglutarate is limited in young pigs, J. Nutr., 132, 3383, 2002.
20. Grimble, G., Glutamine, glutamate and pyroglutamate: facts and fantasies, Clin. Nutr., 12, 66, 1993.
21. Stegink, L.D., Shepherd, J.A., Brummel, M.C., and Murray, L.M., Toxicity of protein hydrolysate solutions: correlation of glutamate dose and neuronal necrosis to plasma amino acid levels in young mice, Toxicology, 2, 285, 1974.
22. Marrs, T.C., Salmona, M., Garattini, S., Burston, D., and Matthews, D.M., The absorption by human volunteers of glutamic acid from monosodium glutamate and from a partial enzymic hydrolysate of casein, Toxicology, 11, 101, 1978.
23. Geha, R.S., Beiser, A., Ren, C., Patterson, R., Greenberger, P.A., Grammer, L.C., Ditto, A.M., Harris, K.E., Shaughnessy, M.A., Yarnold, P.R., Corren, J., and Saxon, A., Review of alleged reaction to monosodium glutamate and outcome of a multicenter double-blind placebocontrolled study, J. Nutr., 130, 1058S, 2000.
24. Walker, R. and Lupien, J.R., The safety evaluation of monosodium glutamate, J. Nutr., 130, 1049S, 2000.
25. Rérat, A., Nunes, C.S., Mendy, F., and Roger, L., Amino acid absorption and production of pancreatic hormones in non-anaesthetized pigs after duodenal infusions of a milk enzymic hydrolysate or of free amino acids, Br. J. Nutr., 60, 121, 1988.
26. Wu, G., Borbolla, A.G., and Knabe, D.A., The uptake of glutamine and release of arginine, citrulline and proline by the small intestine of developing pigs, J. Nutr., 124, 2437, 1994.
27. O’Sullivan, D., Brosnan, J.T., and Brosnan, M.E., Hepatic zonation of the catabolism of arginine and ornithine in the perfused rat liver, Biochem. J., 330, 627, 1998.
28. Van Goudoever, J.B., Stoll, B., Henry, J.F., Burrin, D.G., and Reeds, P.J., Adaptive regulation of intestinal lysine metabolism, Proc. Natl. Acad. Sci. U.S.A., 97, 11620, 2000.
29. van der Schoor, S.R., Van Goudoever, J.B., Stoll, B., Henry, J.F., Rosenberger, J.R., Burrin, D.G., and Reeds, P.J., The pattern of intestinal substrate oxidation is altered by protein restriction in pigs, Gastroenterology, 121, 1167, 2001.
30. van der Schoor, S.R., Reeds, P.J., Stoll, B., Henry, J.F., Rosenberger, J.R., Burrin, D.G., and Van Goudoever, J.B., The high metabolic cost of a functional gut, Gastroenterology, 123, 1931, 2002.
31. Bouteloup-Demange, C., Boirie, Y., Déchelotte, P., Gachon, P., and Beaufrère, B., Gut mucosal protein synthesis in fed and fasted humans, Am. J. Physiol., 274, E541, 1998.
32. Heys, S.D., Park, K.G., McNurlan, M.A., Keenan, R.A., Miller, J.D., Eremin, O., and Garlick, P.J., Protein synthesis rates in colon and liver: stimulation by gastrointestinal pathologies, Gut, 33, 976, 1992.
33. Buchman, A.L., Moukarzel, A.A., Bhuta, S., Belle, M., Ament, M.E., Eckhert, C.D., Hollander, D., Gornbein, J., Kopple, J.D., and Vijayaroghavan, S.R., Parenteral nutrition is associated with intestinal morphologic and functional changes in humans, J. Parenter. Enteral. Nutr., 19, 453, 1995.
34. Burrin, D.G., Stoll, B., Jiang, R., Chang, X., Hartmann, B., Holst, J.J., Greeley, G.H., Jr., and Reeds, P.J., Minimal enteral nutrient requirements for intestinal growth in neonatal piglets: how much is enough? Am. J. Clin. Nutr., 71, 1603, 2000.
35. Christensen, H.N., Conjugated amino acids in portal plasma of dogs after protein feeding, Biochem. J., 44, 333, 1949.
36. Gardner, M.L.G., Lindblad, B.S., Burston, D., Matthews, D.M., and Gardner, M.L., Transmucosal passage of intact peptides in the guinea-pig small intestine in vivo: a reappraisal, Clin. Sci., 64, 433, 1983.
37. Seal, C.J. and Parker, D.S., Isolation and characterization of circulating low molecular weight peptides in steer, sheep and rat portal and peripheral blood, Comp. Biochem. Physiol. B Biochem. Mol. Biol., 99, 679, 1991.
38. Christensen, H.N., Decker, D.G., Lynch, E.L., Mackenzie, T.M., and Powers, J.H., The conjugated, non-protein, amino acids of plasma. V. A study of the clinical significance of peptidaemia, J. Clin. Invest., 26, 853, 1947.
39. Gardner, M.L.G., Transmucosal passage of intact peptides, in Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, 1st ed., Grimble, G.K. and Backwell, F.R.C., Eds., Portland Press, London, 1997, p. 11.
40. Backwell, F.R.C., Circulating peptides and their role in milk protein synthesis, in Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, 1st ed., Grimble, G.K. and Backwell, F.R.C., Eds., Portland Press, London, 1997, p. 69.
41. Seal, C.J. and Parker, D.S., Methodological approaches for the quantitation of peptide appearance across the gastrointestinal tract, in Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, 1st ed., Grimble, G.K. and Backwell, F.R.C., Eds., Portland Press, London, 1997, p. 43.
42. Matthews, D.M., Protein Absorption: Development and Present State of the Subject, 1st ed., Wiley-Liss, New York, 1991.
43. Stevens, C.E. and Hume, I.D., Contributions of microbes in vertebrate gastrointestinal tract to production and conservation of nutrients, Physiol. Rev., 78, 393, 1998.
44. Woolf, G.M., Miller, C., Kurian, R., and Jeejeebhoy, K.N., Nutritional absorption in short bowel syndrome: evaluation of fluid, calorie, and divalent cation requirements, Dig. Dis. Sci., 32, 8, 1987.
45. McIntyre, P.B., Fitchew, M., and Lennard-Jones, J.E., Patients with a high jejunostomy do not need a special diet, Gastroenterology, 91, 25, 1986.
46. Kapembwa, M.S., Fleming, S.C., Griffin, G.E., Caun, K., Pinching, A.J., and Harris, J.R., Fat absorption and exocrine pancreatic function in human immunodeficiency virus infection, Q. J. Med., 74, 49, 1990.
47. Jeejeebhoy, K.N., Short bowel syndrome: a nutritional and medical approach, CMAJ, 166, 1297, 2002.
48. Nightingale, J.M.D. and Lennard-Jones, J., Nutrition support in short-bowel syndrome, in Artificial Nutrition Support in Clinical Practice, 2nd ed., Payne-James, J.J., Grimble, G.K., and Silk, D.B.A., Eds., Greenwich Medical Media, London, 2001, p. 701.
49. Booth, C.C., Alldis, D., and Read, A.E., Studies on the site of fat malabsorption. 2. Fat balances after resection of varying amounts of the small intestine in man, Gut, 2, 168, 1961.
50. Ugolev, A.M., Timofeeva, N.M., Smirnova, L.F., Delaey, P., Gruzdkov, A.A., Iezuitova, N.N., Mityushova, N.M., Roshchina, G.M., Gurman, E.G., Gusev, V.M., Tsvetkova, V.A., and Scherbakov, G.G., Membrane and intracellular hydrolysis of peptides: differentiation, role and interrelations with transport, Ciba Found. Symp., 221, 1977.
51. Gardner, M.L., Illingworth, K.M., Kelleher, J., and Wood, D., Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose, J. Physiol. (Lond.), 439, 411, 1991.
52. Druml, W., Lochs, H., Roth, E., Hubl, W., Balcke, P., and Lenz, K., Utilization of tyrosine dipeptides and acetyltyrosine in normal and uremic humans, Am. J. Physiol., 260, E280, 1991.
53. Stehle, P. and Fürst, P., In vitro hydrolysis of glutamine-, tyrosine-and cystine-containing short-chain peptides, Clin. Nutr., 9, 37, 1990.
54. Fruton, J.S., A history of pepsin and related enzymes, Q. Rev. Biol., 77, 127, 2002.
55. Desnuelle, P., Chemistry and enzymology of pancreatic endopeptidases, in Molecular and Cellular Basis of Digestion, Desnuelle, P., Sjöström, H., and Norén, O., Eds., Elsevier Science Publishers B.V., Amsterdam, 1986, p. 195.
56. Puigserver, A., Chapus, C., and Kerfelec, B., Pancreatic exopeptidases, in Molecular and Cellular Basis of Digestion, Desnuelle, P., Sjöström, H., and Norén, O., Eds., Elsevier Science Publishers B.V., Amsterdam, 1986, p. 235.
57. Marcuard, S.P. and Perkins, A.M., Clogging of feeding tubes, J. Parenter. Enteral Nutr., 12, 403, 1988.
58. Turner, J.S., Fyfe, A.R., Kaplan, D.K., and Wardlaw, A.J., Oesophageal obstruction during nasogastric feeding, Intensive Care Med., 17, 302, 1991.
59. Viall, C., Porcelli, K., Teran, J.C., Varma, R.N., and Steffee, W.P., A double-blind clinical trial comparing the gastrointestinal side effects of two enteral feeding formulas, J. Parenter. Enteral Nutr., 14, 265, 1990.
60. Chung, Y.C., Kim, Y.S., Shadchehr, A., Garrido, A., MacGregor, I.L., and Sleisenger, M.H., Protein digestion and absorption in human small intestine, Gastroenterology, 76, 1415, 1979.
61. Adibi, S.A. and Mercer, D.W., Protein digestion in human intestine as reflected in luminal, mucosal, and plasma amino acid concentrations after meals, J. Clin. Invest., 52, 1586, 1973.
62. Triadou, N., Bataille, J., and Schmitz, J., Longitudinal study of the human intestinal brush border membrane proteins: distribution of the main disaccharidases and peptidases, Gastroenterology, 85, 1326, 1983.
63. Darmoul, D., Voisin, T., Couvineau, A., Rouyer-Fessard, C., Salomon, R., Wang, Y., Swallow, D.M., and Laburthe, M., Regional expression of epithelial dipeptidyl peptidase IV in the human intestines, Biochem. Biophys. Res. Commun., 203, 1224, 1994.
64. Nixon, S.E. and Mawer, G.E., The digestion and absorption of protein in man. 1. The site of absorption, Br. J. Nutr., 24, 227, 1970.
65. Marrs, T.C., Addison, J.M., Burston, D., and Matthews, D.M., Changes in plasma amino acid concentrations in man after ingestion of an amino acid mixture simulating casein, and a tryptic hydrolysate of casein, Br. J. Nutr., 34, 259, 1975.
66. Baglieri, A., Mahé, S., Zidi, S., Huneau, J.F., Thuillier, F., Marteau, P., and Tomé, D., Gastrojejunal digestion of soya-bean-milk protein in humans, Br. J. Nutr., 72, 519, 1994.
67. Chacko, A. and Cummings, J.H., Nitrogen losses from the human small bowel: obligatory losses and the effect of physical form of food, Gut, 29, 809, 1988.
68. Rothman, S., Liebow, C., and Isenman, L., Conservation of digestive enzymes, Physiol. Rev., 82, 1, 2002.
69. Mortensen, P.B., The effect of oral-administered lactulose on colonic nitrogen metabolism and excretion, Hepatology, 16, 1350, 1992.
70. MacFarlane, G.T. and Macfarlane, S., Human colonic microbiota: ecology, physiology and metabolic potential of intestinal bacteria, Scand. J. Gastroenterol. Suppl., 222, 3, 1997.
71. Hutter, H.J., Egorova, V.V., Nikitina, A.A., Zvetkova, V.A., and Ugolev, A.M., Proteolytic activities of colonic mucosa, Z. Med. Lab. Diagn., 31, 27, 1990.
72. Grimble, G.K., Colonic fermentation of starch and protein: an end to all resistance? Nutrition, 11, 173, 1995.
73. Ziegler, T.R., Fernandez-Estivariz, C., Gu, L.H., Bazargan, N., Umeakunne, K., Wallace, T.M., Diaz, E.E., Rosado, K.E., Pascal, R.R., Galloway, J.R., Wilcox, J.N., and Leader, L.M., Distribution of the H+/peptide transporter PepT1 in human intestine: up-regulated expression in the colonic mucosa of patients with short-bowel syndrome, Am. J. Clin. Nutr., 75, 922, 2002.
74. Herrera-Ruiz, D., Wang, Q., Gudmundsson, O.S., Cook, T.J., Smith, R.L., Faria, T.N., and Knipp, G.T., Spatial expression patterns of peptide transporters in the human and rat gastrointestinal tracts, Caco-2 in vitro cell culture model, and multiple human tissues, AAPS Pharm. Sci., 3, E9, 2001.
75. Wheeler, R.A., Griffiths, D.M., and Jackson, A.A., Urea kinetics in neonates receiving total parenteral nutrition, Arch. Dis. Child, 69, 24, 1993.
76. Badaloo, A., Boyne, M., Reid, M., Persaud, C., Forrester, T., Millward, D.J., and Jackson, A.A., Dietary protein, growth and urea kinetics in severely malnourished children and during recovery, J. Nutr., 129, 969, 1999.
77. Fomon, S.J., Matthews, D.E., Bier, D.M., Rogers, R.R., Rebouche, C.J., Edwards, B.B., and Nelson, S.E., Bioavailability of dietary urea nitrogen in the infant, J. Pediatr., 111, 221, 1987.
78. Rees, R.G., Cooper, T.M., Beetham, R., Frost, P.G., and Silk, D.B., Influence of energy and nitrogen contents of enteral diets on nitrogen balance: a double blind prospective controlled clinical trial, Gut, 30, 123, 1989.
79. Ferraris, R.P., Kwan, W.W., and Diamond, J., Regulatory signals for intestinal amino acid transporters and peptidases, Am. J. Physiol., 255, G151, 1988.
80. Chillaron, J., Roca, R., Valencia, A., Zorzano, A., and Palacin, M., Heteromeric amino acid transporters: biochemistry, genetics, and physiology, Am. J. Physiol., 281, F995, 2001.
81. Payne-James, J., Grimble, G., Cahill, E., and Silk, D.B.A., Jejunal absorption of ornithineoxoglutarate (OKGA) in man, J. Parenter. Enteral Nutr., 13 (Suppl.), 22S, 1989.
82. Hellier, M.D., Holdsworth, C.D., and Perrett, D., Dibasic amino acid absorption in man, Gastroenterology, 65, 613, 1973.
83. Chillaron, J., Estevez, R., Mora, C., Wagner, C.A., Suessbrich, H., Lang, F., Gelpi, J.L., Testar, X., Busch, A.E., Zorzano, A., and Palacin, M., Obligatory amino acid exchange via systems bo,+-like and y+L-like: a tertiary active transport mechanism for renal reabsorption of cystine and dibasic amino acids, J. Biol. Chem., 271, 17761, 1996.
84. Medina, M.A., Urdiales, J.L., Nunez de Castro, I., and Sánchez Jimenez, F., Diamines interfere with the transport of L-ornithine in Ehrlich-cell plasma-membrane vesicles, Biochem. J., 280, 825, 1991.
85. ter Steege, J.C.A., Buurman, W.A., and Forget, P.P., Spermine induces maturation of the immature intestinal immune system in neonatal mice, J. Pediatr. Gastroenterol. Nutr., 25, 332, 1997.
86. Newey, H. and Smyth, D.H., The intestinal absorption of some dipeptides, J. Physiol. (Lond.), 145, 48, 1959.
87. Prockop, D.J., Keiser, H.R., and Sjoerdsma, A., Gastrointestinal absorption and renal excretion of hydroxyproline peptides, Lancet, 2, 527, 1962.
88. Saunders, S.J. and Isselbacher, K.J., Intestinal absorption of amino acids, Gastroenterology, 50, 586, 1966.
89. Silk, D.B.A., Perrett, D., and Clark, M.L., Jejeunal and ileal absorption of dibasic amino acids and an arginine containing dipeptide in cystinuria, Gastroenterology, 68, 1426, 1975.
90. Ganapathy, V. and Leibach, F.H., Role of pH gradient and membrane potential in dipeptide transport in intestinal and renal brush-border membrane vesicles from the rabbit: studies with L-carnosine and glycyl-L-proline, J. Biol. Chem., 258, 14189, 1983.
91. Daniel, H. and Herget, M., Intestinal and renal transport of peptides at the cellular and molecular level, in Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, 1st ed., Grimble, G.K. and Backwell, F.R.C., Eds., Portland Press, London, 1997, p. 91.
92. +symporter in the renal brush border membrane, J. Biol. Chem., 267, 9565, 1992.
93. Fei, Y.J., Kanai, Y., Nussberger, S., Ganapathy, V., Leibach, F.H., Romero, M.F., Singh, S.K., Boron, W.F., and Hediger, M.A., Expression cloning of a mammalian proton-coupled oligopeptide transporter, Nature, 368, 563, 1994.
94. Brodin, B., Nielsen, C.U., Steffansen, B., and Frokjaer, S., Transport of peptidomimetic drugs by the intestinal di/tri-peptide transporter, PepT1, Pharmacol. Toxicol., 90, 285, 2002.
95. Wells, G.P., Nicholson, J.A., and Peters, T.J., Subcellular localisation of di-and tripeptidases in guinea pig and rat enterocytes, Biochim. Biophys. Acta, 569, 82, 1979.
96. Kottra, G. and Daniel, H., Bidirectional electrogenic transport of peptides by the protoncoupled carrier PEPT1 in Xenopus laevis oocytes: its asymmetry and symmetry, J. Physiol. (Lond.), 536, 495, 2001.
97. Chen, H., Wong, E.A., and Webb, K.E., Jr., Tissue distribution of a peptide transporter mRNA in sheep, dairy cows, pigs, and chickens, J. Anim. Sci., 77, 1277, 1999.
98. Asatoor, A.M., Milne, M.D., and Walshe, J.M., Peptiduria in the Fanconi syndrome, Ciba Found. Symp., 287, 1977.
99. Nam, T.J., Noguchi, T., and Naito, H., Changes in the urinary excretion of acid-soluble peptides in rats injected with streptozotocin or dexamethasone: a trial to estimate the changes in the rate of whole-body protein degradation in those rats, Br. J. Nutr., 65, 37, 1991.
100. Solaas, K.M., Skjeldal, O., Gardner, M.L., Kase, F.B., and Reichelt, K.L., Urinary peptides in Rett syndrome, Autism, 6, 315, 2002.
101. Silk, D.B.A., Clark, M.L., Marrs, T.C., Addison, J.M., Burston, D., Matthews, D.M., and Clegg, K.M., Jejunal absorption of an amino acid mixture simulating casein and an enzymic hydrolysate of casein prepared for oral administration to normal adults, Br. J. Nutr., 33, 95, 1975.
102. Silk, D.B.A., Fairclough, P.D., Clark, M.L., Hegarty, J.E., Marrs, T.C., Addison, J.M., Burston, D., Clegg, K.M., and Matthews, D.M., Use of a peptide rather than free amino acid nitrogen source in chemically defined “elemental” diets, J. Parenter. Enteral Nutr., 4, 548, 1980.
103. Friedrich, M., Noack, J., Proll, J., and Noack, R., Absorption of enzymatic protein hydrolysates and equimolar amino acid mixtures in the perfused small intestine of the rat [Untersuchungen zur Absorption enzymatischer Proteinhydrolysate sowie aquimolarer Aminosauremischungen am perfundierten Dunndarm der Ratte], Biomed. Biochim. Acta, 43, 117, 1984.
104. Keohane, P.P., Grimble, G.K., Brown, B., Spiller, R.C., and Silk, D.B.A., Influence of protein composition and hydrolysis method on intestinal absorption of protein in man, Gut, 26, 907, 1985.
105. Rérat, A., Simoes-Nuñes, C., Lacroix, M., Vaugelade, P., and Vaissade, P., Cinétique comparée d’apparition dans la veine porte de l’azote a-aminé provenant de mélanges de petits peptides ou d’acides aminés libres de même composition introduits dans le duodenum chez le porc éveillé [Comparative kinetics of appearance in the portal vein of a-amino nitrogen from mixtures of small peptides of free amino acids of the same composition introduced in the duodenum of conscious pigs], C. R. Acad. Sci. 3, 300, 293, 1985.
106. Grimble, G.K., Rees, R.G., Keohane, P.P., Cartwright, T., Desreumaux, M., and Silk, D.B.A., The effect of peptide chain-length on absorption of egg-protein hydrolysates in the normal human jejunum, Gastroenterology, 92, 136, 1987.
107. Ehrlein, H. and Haas-Deppe, B., Comparison of absorption of nutrients and secretion of water between oligomeric and polymeric enteral diets in pigs, Br. J. Nutr., 80, 545, 1998.
108. Beaumont, C., Grimble, G.K., and Welham, K.J., A novel method for the identification of peptides in complex mixtures by tandem mass-spectrometry with atmospheric pressure chemical ionization, in Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, 1st ed., Grimble, G.K. and Backwell, F.R.C., Eds., Portland Press, London, 1997, p. 167.
109. Grimble, G.K., Protein hydrolysates as vehicles for the application of di-and tripeptides in clinical nutrition, in Peptides in Mammalian Protein Metabolism: Tissue Utilisation and Clinical Targeting, 1st ed., Grimble, G.K. and Backwell, F.R.C., Eds., Portland Press, London, 1997, p. 119.
110. Grimble, G.K., Keohane, P., Higgins, B.E., Kaminski, M.V., and Silk, D.B.A., Effect of peptide chain-length on amino acid and nitrogen absorption from two lactalbumin hydrolysates in the normal human jejunum, Clin. Sci., 71, 65, 1986.
111. Rees, R.G., Raimundo, A.H., Grimble, G.K., Hunjan, M.K., and Silk, D.B.A., Peptide based nitrogen source of enteral diets: studies with casein hydrolysates in man, J. Parenter. Enteral Nutr., 12 (Suppl.), 21S, 1988.
112. Friedrich, M., Noack, J., Proll, J., and Noack, R., Comparative study of the absorption of enzymatic protein hydrolysates in the small intestine of the rat. 2. The absorption of tryptic, thermitatic and tryptic-thermitatic casein hydrolysates compared with the equimolar composition of free amino acids [Vergleichende Untersuchungen zur Absorption enzymatischer Proteinhydrolysate am Dunndarm der Ratte. Mitt. Die Absorption von tryptischen, thermitatischen und tryptisch-thermitatischen Caseinhydrolysaten im Vergleich zum aquimolaren Gemisch freier Aminosauren], Nahrung, 29, 167, 1985.
113. Chataud, J., Desreumaux, S., and Cartwright, T., French Patent Application, 86 17516, December 15, 1986.
114. Kondrup, J. and Frokjaer, S., Effect of endotoxin on tissue protein synthesis in rats is modified by method of casein hydrolysis, Clin. Nutr., 18 (Suppl.), 41, 1999.
115. Dufrene, C., Berta, J.L., and Poutignat, N., Results of a multicenter study on tolerance of a semi-elemental diet administered enterally, Ann. Gastroenterol. Hepatol., 25, 163, 1989.
116. Guandalini, S. and Rubino, A., Development of dipeptide transport in the intestinal mucosa of rabbits, Pediatr. Res., 16, 99, 1982.
117. Miller, P.M., Burston, D., Brueton, M.J., and Matthews, D.M., Kinetics of uptake of L-leucine and glycylsarcosine into normal and protein malnourished young rat jejunum, Pediatr. Res., 18, 504, 1984.
118. Lis, M.T., Matthews, D.M., and Crampton, R.F., Effects of dietary restriction and protein deprivation on intestinal absorption of protein digestion products in the rat, Br. J. Nutr., 28, 443, 1972.
119. Ogihara, H., Suzuki, T., Nagamachi, Y., Inui, K., and Takata, K., Peptide transporter in the rat small intestine: ultrastructural localization and the effect of starvation and administration of amino acids, Histochem. J., 31, 169, 1999.
120. Cheeseman, C.I., Expression of amino acid and peptide transport systems in rat small intestine, Am. J. Physiol., 251, G636, 1986.
121. Ihara, T., Tsujikawa, T., Fujiyama, Y., Ueyama, H., Ohkubo, I., and Bamba, T., Enhancement of brush border membrane peptidase activity in rat jejunum induced by starvation, Pflugers Arch., 440, 75, 2000.
122. Poullain, M.G., Cézard, J.P., Marche, C., Roger, L., Mendy, F., and Broyart, J.P., Dietary whey proteins and their peptides or amino acids: effects on the jejunal mucosa of starved rats, Am. J. Clin. Nutr., 49, 71, 1989.
123. Inoue, Y., Espat, N.J., Frohnapple, D.J., Epstein, H., Copeland, E.M., and Souba, W.W., Effect of total parenteral nutrition on amino acid and glucose transport by the human small intestine, Ann. Surg., 217, 604, 1993.
124. Salloum, R.M., Copeland, E.M., and Souba, W.W., Brush border transport of glutamine and other substrates during sepsis and endotoxemia, Ann. Surg., 213, 401, 1991.
125. Souba, W.W., Herskowitz, K., Klimberg, V.S., Salloum, R.M., Plumley, D.A., Flynn, T.C., and Copeland, E.M.I., The effects of sepsis and endotoxemia on gut glutamine metabolism, Ann. Surg., 211, 543, 1990.
126. Pastores, S.M., Katz, D.P., and Kvetan, V., Splanchnic ischemia and gut mucosal injury in sepsis and the multiple organ dysfunction syndrome, Am. J. Gastroenterol., 91, 1697, 1996.
127. Vallet, B., Lund, N., Curtis, S.E., Kelly, D., and Cain, S.M., Gut and muscle tissue PO2 in endotoxemic dogs during shock and resuscitation, J. Appl. Physiol., 76, 793, 1994.
128. Cook, G.C., Effect of systemic bacterial infection on absorption rates of L-histidine and glycylglycine from the human jejunum in vivo, Am. J. Clin. Nutr., 30, 1994, 1977.
129. Shu, H.J., Takeda, H., Shinzawa, H., Takahashi, T., and Kawata, S., Effect of lipopolysaccharide on peptide transporter 1 expression in rat small intestine and its attenuation by dexamethasone, Digestion, 65, 21, 2002.
130. Hosoda, T., Bamba, T., and Hosoda, S., Ileal absorption of various amino acids and dipeptides in rats administered cyclophosphamide: using the short-circuit current method, Jpn. J. Gastroenterol., 88, 2837, 1991.
131. Tanaka, H., Miyamoto, K.I., Morita, K., Haga, H., Segawa, H., Shiraga, T., Fujioka, A., Kouda, T., Taketani, Y., Hisano, S., Fukui, Y., Kitagawa, K., and Takeda, E., Regulation of the PepT1 peptide transporter in the rat small intestine in response to 5-fluorouracil-induced injury, Gastroenterology, 114, 714, 1998.
132. Cosnes, J., Carbonnel, F., Beaugerie, L., Ollivier, J.M., Parc, R., Gendre, J.P., and Le Quintrec, Y., Functional adaptation after extensive small bowel resection in humans, Eur. J. Gastroenterol. Hepatol., 6, 197, 1994.
133. Avissar, N.E., Ziegler, T.R., Wang, H.T., Gu, L.H., Miller, J.H., Iannoli, P., Leibach, F.H., Ganapathy, V., and Sax, H.C., Growth factors regulation of rabbit sodium-dependent neutral amino acid transporter ATB0 and oligopeptide transporter 1 mRNAs expression after enterectomy, J. Parenter. Enteral Nutr., 25, 65, 2001.
134. Lavigne, C., Tremblay, F., Asselin, G., Jacques, H., and Marette, A., Prevention of skeletal muscle insulin resistance by dietary cod protein in high fat-fed rats, Am. J. Physiol., 281, E62, 2001.
135. Moriarty, K.J., Hegarty, J.E., Fairclough, P.D., Kelly, M.J., Clark, M.L., and Dawson, A.M., Relative nutritional value of whole protein, hydrolysed protein and free amino acids in man, Gut, 26, 694, 1985.
136. Itoh, H., Kishi, T., and Chibata, I., Comparative effects of casein and amino acid mixture simulating casein on growth and food intake in rats, J. Nutr., 103, 1709, 1973.
137. Grimble, G.K., Preedy, V., Garlick, P., and Silk, D.B.A., Trophic effects of dietary peptides on the rat intestinal tract, J. Parenter. Enteral Nutr., 13 (Suppl.), 6S, 1989.
138. Forsum, E. and Hambraeus, L., Effects of proteins and their corresponding amino acid mixtures on nitrogen balance and body composition in the growing rat, J. Nutr., 108, 1518, 1978.
139. Daenzer, M., Petzke, K.J., Bequette, B.J., and Metges, C.C., Whole-body nitrogen and splanchnic amino acid metabolism differ in rats fed mixed diets containing casein or its corresponding amino acid mixture, J. Nutr., 131, 1965, 2001.
140. Poullain, M.G., Cézard, J.P., Roger, L., and Mendy, F., Effect of whey proteins, their oligopeptide hydrolysates and free amino acid mixtures on growth and nitrogen retention in fed and starved rats, J. Parenter. Enteral Nutr., 13, 382, 1989.
141. Boza, J.J., Martinez Augustin, O., Baro, L., Suarez, M.D., Gil, A., and Martinez-Augustin, O., Protein v. enzymic protein hydrolysates: nitrogen utilization in starved rats, Br. J. Nutr., 73, 65, 1995.
142. Nielsen, K., Kondrup, J., Elsner, P., Juul, A., and Jensen, E.S., Casein and soya-bean protein have different effects on whole body protein turnover at the same nitrogen balance, Br. J. Nutr., 72, 69, 1994.
143. Monchi, M. and Rérat, A.A., Comparison of net protein utilization of milk protein mild enzymatic hydrolysates and free amino acid mixtures with a close pattern in the rat, J. Parenter. Enteral Nutr., 17, 355, 1993.
144. Monchi, M., Vaugelade, P., Vaissade, P., and Rérat, A., Net protein utilisation after duodenal infusion of small peptides or free amino acids in growing rats, Clin. Nutr., 10 (Suppl.), 31, 1991.
145. Collin-Vidal, C., Cayol, M., Obled, C., Ziegler, F., Bommelaer, G., and Beaufrère, B., Leucine kinetics are different during feeding with whole protein or oligopeptides, Am. J. Physiol., 267, E907, 1994.
146. Calbet, J.A.L. and MacLean, D.A., Plasma glucagon and insulin responses depend on the rate of appearance of amino acids after ingestion of different protein solutions in humans, J. Nutr., 132, 2174, 2002.
147. Boirie, Y., Dangin, M., Gachon, P., Vasson, M.P., Maubois, J.L., and Beaufrère, B., Slow and fast dietary proteins differently modulate postprandial protein accretion, Proc. Natl. Acad. Sci. U.S.A., 94, 14930, 1997.
148. Arnal, M.A., Mosoni, L., Boirie, Y., Houlier, M.L., Morin, L., Verdier, E., Ritz, P., Antoine, J.M., Prugnaud, J., Beaufrère, B., and Patureau-Mirand, P., Protein feeding pattern does not affect protein retention in young women, J. Nutr., 130, 1700, 2000.
149. Arnal, M.A., Mosoni, L., Boirie, Y., Houlier, M.L., Morin, L., Verdier, E., Ritz, P., Antoine, J.M., Prugnaud, J., Beaufrère, B., and Patureau-Mirand, P., Protein pulse feeding improves protein retention in elderly women, Am. J. Clin. Nutr., 69, 1202, 1999.
150. Boirie, Y., Gachon, P., Cordat, N., Ritz, P., and Beaufrère, B., Differential insulin sensitivities of glucose, amino acid, and albumin metabolism in elderly men and women, J. Clin. Endocrinol. Metab., 86, 638, 2001.
151. Rees, R.G.P., Hare, W.R., Grimble, G.K., Frost, P.G., and Silk, D.B.A., Do patients with moderately impaired gastrointestinal function requiring enteral nutrition need a predigested nitrogen source? A prospective crossover controlled clinical trial, Gut, 33, 877, 1992.
152. Rees, R.G., Grimble, G., Halliday, D., Ford, C., and Silk, D.B.A., Influence of orally administered amino acids and peptides on protein turnover kinetics in the short-bowel syndrome, Gut, 28, A1397, 1987.
153. Sales, M.G., de Freitas, O., Zucoloto, S., Okano, N., Padovan, G.J., Dos Santos, J.E., and Greene, L.J., Casein, hydrolyzed casein, and amino acids that simulate casein produce the same extent of mucosal adaptation to massive bowel resection in adult rats, Am. J. Clin. Nutr., 62, 87, 1995.
154. Vanderhoof, J.A., Grandjean, C.J., Burkley, K.T., and Antonson, D.L., Effect of casein versus casein hydrolysate on mucosal adaptation following massive bowel resection in infant rats, J. Pediatr. Gastroenterol. Nutr., 3, 262, 1984.
155. Crane, C.W., Studies on the absorption of 15N labelled yeast in normal subjects and patients with malabsorption, in The Role of the Gastrointestinal Tract in Protein Metabolism, Munro, H.N., Ed., F.A. Davis, Philadelphia, 1964, p. 333.
156. Canciani, M. and Mastella, G., Absorption of a new semielemental diet in infants with cystic fibrosis, J. Pediatr. Gastroenterol. Nutr., 4, 735, 1985.
157. Ellis, L., Kalnins, D., Corey, M., Brennan, J., Pencharz, P., and Durie, P., Do infants with cystic fibrosis need a protein hydrolysate formula? A prospective, randomized, comparative study, J. Pediatr., 132, 270, 1998.
158. Steinhardt, H.J., Wolf, A., Jakober, B., Schmuelling, R.M., Langer, K., Brandl, M., Fekl, W.E., and Adibi, S.A., Nitrogen absorption in pancreatectomised patients: protein versus protein hydrolysate as substrate, J. Lab. Clin. Med., 113, 162, 1989.
159. Van den Berghe, G., Wouters, P., Weekers, F., Verwaest, C., Bruyninckx, F., Schetz, M., Vlasselaers, D., Ferdinande, P., Lauwers, P., and Bouillon, R., Intensive insulin therapy in the critically ill patients, N. Engl. J. Med., 345, 1359, 2001.
160. Hart, D.W., Wolf, S.E., Zhang, X.J., Chinkes, D.L., Buffalo, M.C., Matin, S.I., DebRoy, M.A., Wolfe, R.R., and Herndon, D.N., Efficacy of a high-carbohydrate diet in catabolic illness, Crit. Care Med., 29, 1318, 2001.
161. Van den Berghe, G., Novel insights into the neuroendocrinology of critical illness, Eur. J. Endocrinol., 143, 1, 2000.
162. Ziegler, F., Ollivier, J.M., Cynober, L., Masini, J.P., Coudray-Lucas, C., Levy, E., and Giboudeau, J., Efficiency of enteral nitrogen support in surgical patients: small peptides v. non-degraded proteins, Gut, 31, 1277, 1990.
163. Ziegler, F., Nitenberg, G., Coudray-Lucas, C., Lasser, P., Giboudeau, J., and Cynober, L., Pharmacokinetic assessment of an oligopeptide-based enteral formula in abdominal surgery patients, Am. J. Clin. Nutr., 67, 124, 1998.
164. Badetti, C., Cynober, L., Bernini, V., Garabedian, M., and Manelli, J.C., Nutrition proteins and muscular catabolism in severely burnt patients: comparative effects of small peptides or free amino acids, Ann. Fr. Anesth. Reanim., 13, 654, 1994.
165. Lee, Y.H., Food-processing approaches to altering allergenic potential of milk-based formula, J. Pediatr., 121, S47, 1992.
166. Docena, G., Rozenfeld, P., Fernandez, R., and Fossati, C.A., Evaluation of the residual antigenicity and allergenicity of cow’s milk substitutes by in vitro tests, Allergy, 57, 83, 2002.
167. Moro, G.E., Warm, A., Arslanoglu, S., and Miniello, V., Management of bovine protein allergy: new perspectives and nutritional aspects, Ann. Allergy Asthma Immunol., 89, 91, 2002.
168. Terracciano, L., Isoardi, P., Arrigoni, S., Zoja, A., and Martelli, A., Use of hydrolysates in the treatment of cow’s milk allergy, Ann. Allergy Asthma Immunol., 89, 86, 2002.
169. Tolia, V., Lin, C.H., and Kuhns, L.R., Gastric emptying using three different formulas in infants with gastroesophageal reflux, J. Pediatr. Gastroenterol. Nutr., 15, 297, 1992.
170. Szajewska, H., Albrecht, P., Stoitiska, B., Prochowska, A., Gawecka, A., and Laskowska-Klita, T., Extensive and partial protein hydrolysate preterm formulas: the effect on growth rate, protein metabolism indices, and plasma amino acid concentrations, J. Pediatr. Gastroenterol. Nutr., 32, 303, 2001.
171. Mihatsch, W.A., Franz, A.R., Hogel, J., and Pohlandt, F., Hydrolyzed protein accelerates feeding advancement in very low birth weight infants, Pediatrics, 110, 1199, 2002.
172. Lucas, A., Bloom, S.R., and Aynsley-Green, A., Metabolic and endocrine events at the time of the first feed of human milk in preterm and term infants, Arch. Dis. Child, 53, 731, 1978.
173. Dollberg, S., Kuint, J., Mazkereth, R., and Mimouni, F.B., Feeding tolerance in preterm infants: randomized trial of bolus and continuous feeding, J. Am. Coll. Nutr., 19, 797, 2000.
174. Schanler, R.J., Shulman, R.J., Lau, C., Smith, E.O., and Heitkemper, M.M., Feeding strategies for premature infants: randomized trial of gastrointestinal priming and tube-feeding method, Pediatrics, 103, 434, 1999.
175. Cannon, P.R., Steffee, C.H., Frazier, L.J., Rowley, D.A., and Steptoe, R.C., The influence of time on ingestion of essential amino acids upon utilization in tissue synthesis, Fed. Proc., 6, 390, 1947.
176. Grimble, G.K. and Silk, D.B.A., Peptides in human nutrition, Nutr. Res. Rev., 2, 87, 1989.
177. 14C labeled gelatin hydrolysate leads to an accumulation of radioactivity in cartilage of mice (C57/BL), J. Nutr., 129, 1891, 1999.
178. Cowan, D.A., Andersen, J.A., Grimble, G.K., and Jaenicke, T.A., International Application, WO97/13139.5, 1997.
179. Rothenbuhler, E., Waibel, R., and Solms, J., An improved method for the separation of peptides and a-amino acids on copper sephadex, Anal. Biochem., 97, 367, 1979.
180. Rérat, A., Simoes-Nuñes, C., Mendy, F., Vaissade, P., and Vaugelade, P., Splanchnic fluxes of amino acids after duodenal infusion of carbohydrate solutions containing free amino acids or oligopeptides in the non-anaesthetised pig, Br. J. Nutr., 68, 111, 1992.
181. Grimble, G.K., Preedy, V., Garlick, P., and Silk, D.B.A., Trophic effects of dietary peptides on the rat intestinal tract, Gut, 30, A1454, 1989.
182. Cosnes, J., Evard, D., Beaugerie, L., Gendre, J.P., and Le Quintrec, Y., Improvement in protein absorption with a small-peptide-based diet in patients with high jejunostomy, Nutrition, 8, 406, 1992.
183. Ksiazyk, J., Piena, M., Kierkus, J., and Lyszkowska, M., Hydrolyzed versus nonhydrolyzed protein diet in short bowel syndrome in children, J. Pediatr. Gastroenterol. Nutr., 35, 615, 2002.
184. Jorpes, J.E., Magnusson, J.H., and Wretlind, A., Casein hydrolysate; a supplementary food for premature infants, Lancet, 2, 228, 1946.
185. Medjad-Guillou, N., Henocq, A., and Arnaud-Battandier, F., Does the hydrolysis of proteins change the acceptability and the digestive tolerance of milk for infants? The results of a comparative and randomized prospective study, Ann. Pediatr. (Paris), 39, 202, 1992.
186. Vandenplas, Y., Hauser, B., Blecker, U., Suys, B., Peeters, S., Keymolen, K., and Loeb, H., The nutritional value of a whey hydrolysate formula compared with a whey-predominant formula in healthy infants, J. Pediatr. Gastroenterol. Nutr., 17, 92, 1993.
187. Rigo, J., Salle, B.L., Putet, G., and Senterre, J., Nutritional evaluation of various protein hydrolysate formulae in term infants during the first month of life, Acta Paediatr. Suppl., 402, 100, 1994.
188. Rigo, J., Salle, B.L., Picaud, J.C., Putet, G., and Senterre, J., Nutritional evaluation of protein hydrolysate formulas, Eur. J. Clin. Nutr., 49 (Suppl 1), S26, 1995.
189. Zijlstra, R.T., Mies, A.M., McCracken, B.A., Odle, J., Gaskins, H.R., Lien, E.L., and Donovan, S.M., Short-term metabolic responses do not differ between neonatal piglets fed formulas containing hydrolyzed or intact soy proteins, J. Nutr., 126, 913, 1996.