Abstract
Arginine is a semiessential dibasic amino acid. It is an essential component of the urea cycle (Fig. 1) and is converted by the enzyme arginase into ornithine and urea (Ratner, 1973) (Fig. 2). By virtue of its position in the urea cycle (Fig. 1), arginine is required for ammonia detoxification and is therefore involved in the intermediary metabolism of other amino acids. A major source of endogenous arginine is derived from the conversion of citrulline to arginine by the kidney (Windmueller and Spaeth, 1981). Hepatic arginase activity is usually very high, so that hepatic arginine levels are low and the liver does not contribute significantly to the maintenance of plasma arginine levels. Arginine is normally present in the Western diet as approximately 5% of dietary protein such that an individual ingesting 100 g of protein will receive 31 mmole (5.4 g) of arginine (Visek, 1986). The normal plasma arginine concentration is O.05 mM and supplementation with amounts of up to 25 g of arginine results in plasmal levels of O.2 to O.3 mM. Arginine is absorbed in the gastrointestinal tract by an active transport mechanism which is both substrate specific and sodium dependent.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Barbul, A., 1990, Arginine and immune function, Nutrition 6: 53–58.
Barbul, A., Wasserkrug, H. L., Sisto, D. A., et al., 1980a, Thymic and immune stimulatory actions of arginine, J. Parent. Ent. Nutr. 4: 446–449.
Barbul, A., Wasserkrug, H. L., Seifter, E., et al., 1980b, Immunostimulatory effects of arginine in normal and injured rats, J. Surg. Res. 29: 228–235.
Barbul, A., Sisto, D. A., Wasserkrug, H. L., et al., 1981, Arginine stimulates lymphocyte immune response in healthy humans, Surgery 90: 244.
Billiar, T. R., Curran, R. D., Stuehr, D. J., West, M. A., Ferrari, F. K., and Simmons, R. L., 1989, Evidence that the activation of Kupffer cells results in the production of L-arginine metabolites that release cell-associated iron and inhibit hepatocyte protein synthesis, Surgery 106: 364.
Cerra, F. B., Holman, R. T., Bankey, P. E., Mazuski, J. F., and Li Cari, J. J., 1991, Omega 3 polyunsaturated fatty acids as modulators of cellular function in the critically ill, Pharmacotherapy 11: 71–76.
Chisari, F. V., Nakamura, M., Milich, D. R., et al., 1985, Production of two distinct and independent hepatic immunoregulatory molecules by the perfused rat liver, Hepatology 5: 735–743.
Choo-Chung, Y. S., Clair, T., Bodwin, J. S., et al., 1980, Arrest of mammary tumor growth in vivo by Larginine: Stimulation of NAD-dependent activation of adenylate cyclase, Biochem. Biophys. Res. Commun. 95: 1306–1313.
Curran, R. D., Billiar, T. R., Stuehr, D. J., et al., 1992, Multiple cytokines are required to induce hepatic nitric oxide production and inhibit total protein synthesis, Ann. Surg. in press.
Daly, J. M., Reynolds, J. V., Thorn, A. K., et al., 1988a, Immune and metabolic effects of arginine in surgical patients, Ann. Surg. 208: 512.
Daly, J. M., Reynolds, J. V., Thorn, A., Kinsley, L., Dietrick-Gallagher, M., Shou, J., and Ruggeri, B., 1988b, Immune and metabolic effects of arginine in the surgical patient, Ann. Surg. 208: 512–523.
Drapier, J. C., and Hibbs, J. B., Jr., 1986, Murine cytotoxic activated macrophages inhibit aconitase in tumor cells, J. Clin. Invest. 78: 790.
Drapier, J. C., and Hibbs, J. B., Jr., 1988, Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells, J. Immunol. 140: 2829.
Droge, W., 1986, Protein kinase C in T cell regulation, Immunol. Today 7: 340–343.
Droge, W., Benninghoff, B., and Lehman, V., 1987, Tumor necrosis factor augments the immunogenicity and the production of L-ornithine by peritoneal macrophages, Lymphokine Res. 92: 359–365.
Eagle, H., 1959, Amino acid metabolism in mammalian cell cultures, Science 130: 432–437.
Gottschlich, M., Jenkins, M., Warden, G., Boumer, T., Havens, P., Snook, J., and Alexander, J. W., 1990, Differential effects of three enterai dietary regimens on selected outcome variables in burn patients, J. Parent. Ent. Nutr. 14: 225–236.
Granger, D., and Lehninger, L., 1982, Site of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells, J. Cell Biol. 95: 527.
Granger, D., Taintor, R., Cook, J., and Hibbs, J. B., Jr., 1980, Injury of neoplastic cells by murine macrophages leads to inhibition of mitochondrial respiration, J. Clin. Invest. 65: 357–370.
Granger, D. L., Hibbs, J. B., Perfect, J. R., and Durack, D. T., 1988, Specific amino acid (L-arginine) requirement for the microbiostatic activity of murine macrophages, J. Clin. Invest. 81: 1129–1136.
Hacker-Shahin, B., and Droge, W., 1986, Putrescine and its biosynthetic precursor L-ornithine augment the in vivo immunization against major histocompatibility antigens and syngeneic tumor cells, Cell. Immunol. 99: 434–443.
Hibbs, J. B., Jr., Vavrin, Z., and Taintor, R. R., 1987, L-Arginine is required for expression of the activated macrophage effector mechanisms causing selective metabolic inhibition in target cells, J. Immunol. 138: 550–565.
Ignarro, L. J., Buga, G. M., Wood, K. S., et al., 1987, Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide, Proc. Natl. Acad. Sci. USA 84: 9265–9269.
Kaplan, S. S., Billiar, T. R., Curran, R. D., Zdziarski, U. E., Simmons, R. L., and Baseford, R. E., 1989, Inhibition of neutrophil chemotaxis with NG monomethyl-L-arginine: A role for cyclic GMP, Blood 74: 1885–1887.
Keller, R., 1973, Cytostatic elimination of syngeneic rat tumor cells in vitro by nonspecifically activated macrophages, J. Exp. Med. 138: 2366–2371.
Keller, R., Geiges, M., and Keist, R., 1990, L-Arginine-dependent reactive nitrogen intermediates as mediators of tumor cell killing by activated macrophages, Cancer Res. 50: 1421–1425.
Knowles, R. G., Palacios, M., Palmer, R. M. J., et al., 1989, Formation of nitric oxide from L-arginine in the central nervous system: A transduction mechanism for stimulation of the soluble guanylate cyclase, Proc. Natl. Acad. Sci. USA 86: 5159–5162.
Merimee, T. J., Lillicrap, D. A., and Rabinowitz, D., 1965, Effect of arginine on serum levels of human growth hormone, Lancet 2: 668–670.
Milner, J. A., and Stepanovitch, L. V., 1979, Inhibitory effects of dietary arginine on growth of Ehrlich ascites tumor cells in mice, J. Nutr. 109: 489–494.
Moss, J., and Vaughan, M., 1977, Mechanism of action of choleragen: Evidence for ADP-ribosyltransferase activity with arginine as an acceptor, J. Biol. Chem. 252: 2455–2465.
Palmer, J. P., Walter, R. M., and Ensick, J. W., 1975, Arginine-stimulated acute phase of insulin and glucagon secretion. I. In normal man, Diabetes 24: 735–740.
Rakoff, J. S., Siver, T. M., Sinha, Y. M., et al., 1973, Prolactin and growth hormone release in response to sequential stimulation by arginine and TRF, J. Clin. Endocrinol. Metab. 37: 641–644.
Ratner, S., 1973, Enzymes of arginine and urea synthesis, Adv. Enzymol. 39: 1–90.
Rettura, G., Padawer, J., Barbul, A., et al., 1979, Supplemental arginine increases thymic cellularity in normal and murine sarcoma virus-inoculated mice and increases the resistance of mice to the murine sarcoma virus tumor, J. Parent. Ent. Nutr. 3: 409–416.
Rettura, G., Levenson, S. M., Barbul, A., et al., 1981, Supplemental arginine and ornithine promote allograft rejection, 183rd Meet. Am. Chem. Soc. AGFD Abstract 11.
Rettura, G., Stratford, F., Levenson, S. M., et al., 1983, Improved wound-healing, anticachectic and thymotrophic effects of supplemental ornithine, 17 th Mid-Atlantic Reg. Meet. Am. Chem. Soc. Abstract 15.
Reynolds, J. V., Thorn, A. K., Ziegler, M., et al., 1987, Arginine, protein calorie malnutrition and cancer, J. Surg. Res. 45: 513.
Reynolds, J. V., Zhang, S. M., Thorn, A. K., et al., 1988, Arginine as an immunomodulator, Surg. Forum 38: 415.
Saito, H., Trochi, O., Wang, S., et al., 1987, Metabolic and immune effects of dietary arginine supplementation after burn, Arch. Surg. 122: 784–789.
Susskind, B. M., and Chandrasekaran, J., 1987, Inhibition of cytolytic T lymphocyte maturation with ornithine, arginine and putrescine, J. Immunol. 139: 905–912.
Tachibana, K., Mukai, K., Hiraoka, I., et al., 1985, Evaluation of the effect of arginine-enriched amino acid solution on tumor growth, J. Parent. Ent. Nutr. 9: 428–434.
Visek, W. J., 1986, Arginine needs, physiological states and usual diets. A reevaluation, J. Nutr. 116: 36–46.
Windmueller, H. G., and Spaeth, A. E., 1981, Source and fate of circulating citrulline, Am. J. Physiol. 241: 473–480.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media New York
About this chapter
Cite this chapter
Redmond, H.P., Daly, J.M. (1993). Arginine. In: Klurfeld, D.M. (eds) Nutrition and Immunology. Human Nutrition. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2900-2_7
Download citation
DOI: https://doi.org/10.1007/978-1-4615-2900-2_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6257-9
Online ISBN: 978-1-4615-2900-2
eBook Packages: Springer Book Archive