Tryptophan Nutrition and Metabolism: An Overview

  • J. C. Peters
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 294)


Tryptophan (TRP) was the first amino acid to be recognized as being essential for normal growth of young animals when Wilcock and Hopkins (1906) and later Osborne and Mendel (1914) observed its ability to stimulate weight gain in mice and rats when added to low TRP rations. Subsequent studies in a variety of species confirmed that TRP was essential for normal growth and, furthermore, was required for maintenance of nitrogen equilibrium in mature animals. Some years after those early animal studies, Rose and collaborators (1957) demonstrated that TRP was an essential amino acid for human nutrition.


Large Neutral Amino Acid Dietary Protein Level Indispensable Amino Acid Amino Acid Supply Dietary Protein Content 
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  1. Anderson, G.H., 1979, Control of protein and energy intake: role of plasma amino acids and brain neurotransmitters, Can J. Physiol. Pharmacol., 57: 1043–1057.PubMedCrossRefGoogle Scholar
  2. Anderson, H.L., Beneverga, N.J., and Harper, A.E., 1968, Associations among food and protein intake, serine dehydratase, and plasma amino acids, Am. J. Physiol., 214: 1008–1013.PubMedGoogle Scholar
  3. Ashley, D.V.M., and Anderson, G.H., 1975, Correlation between the plasma tryptophan to neutral amino acid ratio and protein intake in the selfselecting weanling rat, J. Nutr., 105: 1412–1421.PubMedGoogle Scholar
  4. Badawy, A.A.-B., 1977, The functions and regulation of tryptophan pyrrolase, Life Sci., 21: 755–768.PubMedCrossRefGoogle Scholar
  5. Bender, D.A., 1982, Biochemistry of tryptophan in health and disease, Molec. Aspects Med., 6: 101–197.CrossRefGoogle Scholar
  6. Blazek, R., and Shaw, D.M., 1978, Tryptophan availability and brain protein synthesis, Proc. Brit. Assoc. Psychophannacol., 17: 1065–1068.Google Scholar
  7. Block, R.J., and Weiss, K.W., 1956, “Amino Acid Handbook”, The Ryerson Press, Toronto.Google Scholar
  8. Bloxam, D.L., Tricklebank, M.D., Patel, A.J., and Curzon, G., 1980, Effects of albumin, amino acids, and clofibrate on the uptake of tryptophan by the rat brain, J. Neurochem., 34: 43–49.PubMedCrossRefGoogle Scholar
  9. Blundell, J.E., 1977, Is there a role for serotonin (5-hydroxytryptamine) in feeding?, Int. J. Obes., 1: 15–42.PubMedGoogle Scholar
  10. Bosnan, T., 1978, Serotonin metabolism, in: “Serotonin in Health and Disease”, Vol. 1, Essman, W.B., ed., SP Medical and Scientific Books, New York, pp. 181–300.Google Scholar
  11. Evans, G.W., and Johnson, E.C., 1980, Zinc absorption in rats fed a low protein diet and a low protein diet supplemented with tryptophan or picolinic acid, J. Nutr., 110: 1076–1080.PubMedGoogle Scholar
  12. Fernstrom, J.D., 1981, Dietary precursors and brain neurotransmitter formation, Ann. Rev. Med., 32: 413–425.PubMedCrossRefGoogle Scholar
  13. Fernstrom, J.D., and Faller, D.V., 1978, Neutral amino acids in the brain: Changes in response to food ingestion, J. Neurochem., 30: 1531–1538.PubMedCrossRefGoogle Scholar
  14. Fernstrom, J.D., Hirsch, M.J., Madras, B.K., and Sudarsky, L., 1975, Effects of skim milk, whole milk and light cream on serum tryptophan binding and brain tryptophan concentrations, J. Nutr., 105: 1359–1362.PubMedGoogle Scholar
  15. Fernstrom, J.D., and Wurtman, R.J., 1971a, Brain serotonin content: Physiological dependence on plasma tryptophan levels, Science, 173: 149–152.PubMedCrossRefGoogle Scholar
  16. Fernstrom, J.D., and Wurtman, R.J., 1971b, Brain serotonin content: Increase following ingestion of a carbohydrate diet, Science, 174: 1023–1025.PubMedCrossRefGoogle Scholar
  17. Fernstrom, J.D., and Wurtman, R.J., 1972, Brain serotonin content: Physiological regulation by plasma neutral amino acids, Science, 178: 414–416.PubMedCrossRefGoogle Scholar
  18. Gál, E.M., and Drewes, P.A., 1962, Studies on the metabolism of 5-hydroxytryptamine (serotonin). II. Effect of tryptophan deficiency in rats, Proc. Soc. Exptl. Biol. Med., 110: 368–371.Google Scholar
  19. Greengard, O., and Feigelson, P., 1961, The activation and induction of rat liver tryptophan pyrrolase in vivo by its substrate, J. Biol. Chem., 236: 58–161.Google Scholar
  20. Hayaishi, O., 1980, Newer aspects of tryptophan metabolism, in: “Biochemical and Medical Aspects of Tryptophan Metabolism”, Hayaishi, O., Ishimura, Y., and Kido, R., eds., Elsevier/North-Holland, Amsterdam, pp. 15–30.Google Scholar
  21. Harper, A.E., 1974, Control mechanisms in amino acid metabolism, in: “The Control of Metabolism”, Sink, J.D., ed., The Pennsylvania State University Press, University Park, pp. 49–71.Google Scholar
  22. Harper, A.E., 1977, Human amino acid and nitrogen requirements as the basis for evaluation of nutritional quality of protein, in: “Food Proteins”, Whitaker, J.R., and Tannenbaum, S.R., eds., Avi Publishing Co., Inc., Westport, pp. 363–386.Google Scholar
  23. Harper, A.E., Benevenga, N.J., and Wohlhueter, R.M., 1970, Effects of ingestion of disproportionate amounts of amino acids, Physiol. Rev., 50: 428–558.PubMedGoogle Scholar
  24. Harper, A.E., Miller, R.H., and Block, K.P., 1984, Branched chain amino acid metabolism, Ann. Rev. Nutr., 4: 409–454.CrossRefGoogle Scholar
  25. Harper, A.E., and Peters, J.C., 1989, Protein intake, brain amino acids and serotonin and protein self-selection, J. Nutr., 119: 677–689.PubMedGoogle Scholar
  26. Horwitt, M.K., Harvey, C.C., Rothwell, W.S., Cutler, J.L., and Haffron, D., 1956, Tryptophan-niacin relationship in man, J. Nutr., 60: 1–43.Google Scholar
  27. Ikeda, M., Tsuji, H., Nakamura, S., Ichiyama, A., Nishizuka, Y., and Hayaishi, O., 1965, Studies on the biosynthesis of nicotinamide adenine dinucleotide: (ii) a role of picolinic carboxylase in the biosynthesis of nicotinamide adenine dinucleotide from tryptophan in mammals, J. Biol. Chem., 240: 1395–1401.PubMedGoogle Scholar
  28. Ip, C.Y., and Harper, A.E., 1974, Liver polysome profiles and protein synthesis in rats fed a threonine-imbalanced diet, J. Nutr., 104: 252–263.PubMedGoogle Scholar
  29. Kaufman, S., 1974, Properties of pterin-dependent aromatic amino acid hydroxylases, in: “Aromatic Amino Acids in the Brain”, Wolstenholme, G.E.W., and Fitzsimons, D.W., eds., Elsevier/North-Holland, Amsterdam, pp. 85–108.Google Scholar
  30. Knox, W.E., and Mehler, A.H., 1951, The adaptive increase of the tryptophan peroxidase-oxidase system of liver, Science, 113: 237–240.PubMedCrossRefGoogle Scholar
  31. Krebs, H.A., 1972, Some aspects of the regulation of fuel supply in omnivorous animals, Adv. Enz. Regul., 10: 397–420.CrossRefGoogle Scholar
  32. Lin, F.D., Smith, T.K., and Bayley, H.S., 1988, A role for tryptophan in regulation of protein synthesis in porcine muscle, J. Nutr., 118: 445–449.PubMedGoogle Scholar
  33. McMenamy, R.H., 1965, The binding of indole analogues to human serum albumin: effects of fatty acids, J. Biol. Chem., 240: 4235–4243.PubMedGoogle Scholar
  34. McMenamy, R.H., and Oncley, J.L., 1958, The specific binding of L-tryptophan to serum albumin, J. Biol. Chem., 233: 1436–1447.PubMedGoogle Scholar
  35. Miller, L.L., 1962, The role of liver and the non-hepatic tissues in the regulation of free amino acid levels in the blood, in: “Amino Acid Pools”, Holden, J.T., ed., Elsevier, New York, pp. 708–721.Google Scholar
  36. Munro, H.N., 1970, Free amino acid pools and their role in regulation, in: “Mammalian Protein Metabolism”, Vol. 4, Munro, H.N., ed., Academic Press, New York, pp. 299–386.Google Scholar
  37. Munro, H.N., Hubert, C., and Baliga, B.S., 1975, Regulation of protein synthesis in relation to amino acid supply — a review, in: “Alcohol and Abnormal Protein Biosynthesis”, Rothschild, M.A., Oratz, M., and Schreiber, S.S., eds., Pergamon Press, New York, pp. 33–66.Google Scholar
  38. Nakagawa, I., Takahashi, T., Suzuki, T., and Masana, Y., 1969, Effect in man of the addition of tryptophan or niacin to the diet on the excretion of their metabolites, J. Nutr., 99: 325–330.PubMedGoogle Scholar
  39. Osborne, T.B., and Mendel, L.B., 1914, Amino acids in nutrition and growth, J. Biol. Chem., 17: 325–349.Google Scholar
  40. Pardridge, W.M., 1977, Kinetics of competitive inhibition of neutral amino acid transport across the blood-brain barrier, J. Neurochem., 28: 103–108.PubMedCrossRefGoogle Scholar
  41. Patterson, J.I., Brown, R.R., Linkswiler, H., and Harper, A.E., 1980, Excretion of tryptophan-niacin metabolites by young men: effects of tryptophan, leucine, and vitamin B6 intakes, Am. J. Clin. Nutr., 33: 2157–2167.PubMedGoogle Scholar
  42. Peters, J.C., and Harper, A.E., 1985, Adaption of rats to diets containing different levels of protein: effects on food intake, plasma and brain amino acid concentrations and brain neurotransmitter metabolism, J. Nutr., 115: 382–398.PubMedGoogle Scholar
  43. Peters, J.C., and Harper, A.E., 1987a, Acute effects of dietary protein on food intake, tissue amino acids, and brain serotonin, Am. J. Physiol., 252: R902–R914.PubMedGoogle Scholar
  44. Peters, J.C., and Harper, A.E., 1987b, A skeptical view of the role of central serotonin in the selection and intake of protein, Appetite, 8: 206–210.PubMedCrossRefGoogle Scholar
  45. Pronczuk, A.W., Baliga, B.S., Triant, J.W., and Munro, H.N., 1968, Comparison of the effect of amino acid supply on hepatic polysome profiles in vivo and in vitro. Biochim. Biophys. Acta, 157: 204–206.Google Scholar
  46. Pronczuk, A.W., Rogers, Q.R., and Munro, H.N., 1970, Liver polysome patterns of rats fed amino acid imbalanced diets, J. Nutr., 100: 1249–1258.PubMedGoogle Scholar
  47. Rogers, Q.R., 1976, The nutritional and metabolic effects of amino acid imbalances, in: “Protein Metabolism and Nutrition”, Cole, D.J.A., ed., Butterworths, London.Google Scholar
  48. Rose, W.C., 1957, The amino acid requirements of adult man, Nutr. Abstr. Rev., 27: 631–647.Google Scholar
  49. Schimke, R.T., Sweeney, E.W., and Berlin, C.M., 1964, An analysis of the kinetics of rat liver tryptophan pyrrolase induction: the significance of both enzyme synthesis and degradation, Biochem. Biophys. Res. Comm., 15: 214–219.PubMedCrossRefGoogle Scholar
  50. Schimke, R.T., Sweeney, E.W., and Berlin, C.M., 1965, The roles of synthesis and degradation in the control of rat liver tryptophan pyrrolase, J. Biol. Chem., 240: 322–331.PubMedGoogle Scholar
  51. Sidransky, H., Murty, C.N., and Verney, E., 1984, Nutritional control of protein synthesis: studies relating to tryptophan-induced stimulation of nucleocytoplasmic translocation of mRNA in rat liver, Am. J. Pathol., 117: 298–309.PubMedGoogle Scholar
  52. Sidransky, H., Verney, E., and Sarma, D.S.R., 1971, Effect of tryptophan on polyribosomes and protein synthesis in liver, Am. J. Clin. Nutr., 24: 779–785.PubMedGoogle Scholar
  53. Smith, S.A., and Pogson, C.I., 1980, The metabolism of L-tryptophan by isolated rat liver cells: effect of albumin binding and amino acid competition on oxidation of tryptophan by tryptophan 2,3-dioxygenase, Biochem. J., 186: 977–986.PubMedGoogle Scholar
  54. Spiller, G.A., Jensen, C.D., Patterson, T.S., Chuck, C.S., Whittam, J.H., and Scala, J., 1987, Effect of protein dose on serum glucose and insulin response to sugars, Am. J. Clin. Nutr., 46: 474–480.PubMedGoogle Scholar
  55. Sved, A.F., 1983, Precursor control of the function of monoaminergic neurons, in: “Nutrition and the Brain”, Vol. 6, Wurtman, R.J., and Wurtman, J.J., eds., Raven Press, New York, pp. 223–275.Google Scholar
  56. Udenfriend, S., Titus, E., and Weissbach, H., 1955, The identification of 5-hydroxy-3-indoleacetic acid in normal urine and a method for its assay, J. Biol. Chem., 216: 499–505.PubMedGoogle Scholar
  57. Veneziale, C.M., Walter, P., Kneer, N., and Lardy, H.A., 1967, Influence of L-tryptophan and its metabolites on gluconeogenesis in the isolated perfused liver, Biochemistry, 6: 2129–2138.PubMedCrossRefGoogle Scholar
  58. Willcock, E.G., and Hopkins, F.G., 1906, The importance of individual amino acids in metabolism; observations on the effect of adding tryptophan to a diet in which zein is the sole nitrogenous constituent, J. Physiol. (London), 35: 88–102.Google Scholar
  59. Young, V.R., Munro, H.N., Matthews, D.E., and Bier, D.M., 1983, Relationship in energy metabolism to protein metabolism, in: “New Aspects of Clinical Nutrition”, Kleinberger, G., and Deutsch, E., eds., Karger, Basel, pp. 44–73.Google Scholar

Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • J. C. Peters
    • 1
  1. 1.The Procter & Gamble CompanyMiami Valley LaboratoriesOhioUSA

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