Taurine 2 pp 73-84 | Cite as

High Levels of Dietary Protein or Methionine have Different Effects on Cysteine Metabolism in Rat Hepatocytes

  • Deborah L. Bella
  • Martha H. Stipanuk
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 403)


Cysteine catabolism in mammalian liver can occur by both cysteine sulfinate-dependent and cysteine sulfinate-independent pathways. Both pathways lead to the production of pyruvate and sulfate, but only the cysteine sulfinate-dependent pathway leads to taurine production. Cysteine dioxygenase (CDO; EC catalyzes the first reaction in the cysteine sulfinate-dependent catabolic pathway, by which cysteine is oxidized to cysteine sulfinate. Cysteine sulfinate has two possible catabolic fates. It can be transaminated by aspartate aminotransferase (AAT; EC which ultimately yields pyruvate and sulfate, or it can be decarboxylated by cysteine sulfinate decarboxylase (CSAD; EC to hypotaurine. Hypotaurine is then presumably non-enzymatically oxidized to taurine. Both taurine and sulfate are important metabolites required by the body for essential functions as well as being end-products of cysteine catabolism that are excreted in the urine.


High Protein Diet Sulfur Amino Acid Cysteine Sulfinate Decarboxylase Cysteine Metabolism Cysteine Dioxygenase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    AIN Ad Hoc Committee on Standards for Nutrition Studies. Report of the AIN ad hoc committee on standards for nutritional studies. J. Nutr. 107:1340-1348, 1977.Google Scholar
  2. 2.
    Bagley, P. J., and M. H. Stipanuk. The activities of hepatic cysteine dioxygenase and cysteinesulfinate decarboxylase are regulated in a reciprocal manner in response to dietary casein level in rats. J. Nutr. 124:2410–2421, 1994.Google Scholar
  3. 3.
    Bagley, P. J., and M. H. Stipanuk. Rats fed a low protein diet supplemented with sulfur amino acids have increased cysteine dioxygenase activity and increased taurine production in hepatocytes. J. Nutr. 125: 933–940, 1995.Google Scholar
  4. 4.
    Bella, D. L., and M. H. Stipanuk. Comparison of effects of excess dietary protein, methionine or chloride on acid-base balance and on cysteine catabolism to taurine versus sulfate. Am. J. Physiol., 1995, in press.Google Scholar
  5. 5.
    Bergmeyer, H. U., and Bernt, E. Glutamate-oxaloacetate transaminawe. In: Methods in Enzymatic Analysis, edited by H. U. Bergmeyer, New York: Academic Press, Inc., vol. 2, 1974, p. 727–744.CrossRefGoogle Scholar
  6. 6.
    Berry, M. N., A. M. Edwards, and G. J. Borritt. Isolated Hepatocytes: Preparation, Properties and Applications. Elsevier, New York, 1991, p.16–32, 56-57.Google Scholar
  7. 7.
    Claus, T. H., C. R. Park, and S. J. Pilkis. Glucagon and gluconeogenesis. In: Glucagon I, edited by P. Lefebvre, Berlin, Germany: Springer-Verlag, 1983, p. 361–382Google Scholar
  8. 8.
    Coloso, R. M., M. R. Drake, and M. H. Stipanuk. Effect of bathocuproine disulfonate, a copper chelator, on cyst(e)ine metabolism in freshly isolated rat hepatocytes. Am. J. Physiol. 259:E443–E450, 1990.Google Scholar
  9. 9.
    Coloso, R. M., and M. H. Stipanuk]. Metabolism of cyst(e)ine in rat enterocytes. J. Nutr. 119:1914–1924, 1Google Scholar
  10. 10.
    Daniels, K. M., and M. H. Stipanuk. The effect of dietary cysteine level on cysteine metabolism in rats. J. Nutr. 112(11):2130–2141, 1982.Google Scholar
  11. 11.
    Fariss, M. W., and D. J. Reed. High-performance liquid chromatography of thiols and disulfides: dinitrophenyl derivatives. Methods Enzymol. 143:101–109, 1987.CrossRefGoogle Scholar
  12. 12.
    Gaull, G. E., D. K. Rassin, N.C.R. Raiha, and K. Heinonen. Milk protein quantity and quality in low-birth-weight infants. III. Effects on sulfur amino acids in plasma and urine. J. Pediat. 90:348–355, 19CrossRefGoogle Scholar
  13. 13.
    Hardison, W.G.M., C. A. Wood, and J. H. Proffitt. Quantification of taurine synthesis in the intact rat and cat liver. Proc. Soc. Exp. Biol. Med. 155:55–58, 1977.CrossRefGoogle Scholar
  14. 14.
    Hosokawa, Y., S. Nizeki, H. Tojo, I. Sato, and K. Yamaguchi. Hepatic cysteine dioxygenase activity and sulfur amino acid metabolism in rats: possible indicators in the evaluation of protein quality. J. Nutr. 118:456–461, 1988.Google Scholar
  15. 15.
    Hosokawa, Y., K. Yamaguchi, N. Kohashi, Y. Kori, and I. Ueda. Decrease of rat liver cysteine dioxygenase (cysteine oxidase) activity mediated by glucagon. J. Biochem. 84:419–424, 1978.Google Scholar
  16. 16.
    Jacobsen, J. G., and L. H. Smith, Jr. Comparison of decarboxylation of cysteine sulflnic acid-l-14C and cysteic acid-l-14C by human, dog and rat liver and brain. Nature 200:575–577, 1963.CrossRefGoogle Scholar
  17. 17.
    Jacobsen, J. G., L. L. Thomas, and L. Smith. Properties and distribution of mammalian L-cysteine sulfinate carboxylyases. Biochim. Biophys. Acta 85:103–116, 1964.Google Scholar
  18. 18.
    Jerkins, A. A., L. E. Bobroff, and R. D. Steele. Hepatic cysteine sulfinic acid decarboxylase activity in rats fed various levels of dietary casein. J. Nutr. 119:1593–1597, 1989.Google Scholar
  19. 19.
    Jerkins, A. A., and R. D. Steele. Dietary sulfur amino acid modulation of cysteine sulfinic acid decarboxylase. Am. J. Physiol. 261:E551–E555, 1991.Google Scholar
  20. 20.
    Kohashi, N., K. Yamaguchi, Y. Hosokawa, Y. Kori, O. Fuji, and I. Ueda. Dietary control of cysteine dioxygenase in rat liver. J. Biochem. 84:159–168, 1978.Google Scholar
  21. 21.
    Knopf, K., J. A. Sturman, M. Armstrong, and K. C. Hayes. Taurine: an essential nutrient for the cat. J. Nutr. 108:773–778, 1978.Google Scholar
  22. 22.
    Lamprecht, W., and I. Trautschold. ATP determination with hexokinase and glucose-6-phosphate dehy-drogenase. In: Methods of Enzymatic Analysis, edited by H. Bergmeyer. New York: Academic Press, vol. 4, 1974, p. 2101–2110.Google Scholar
  23. 23.
    Lu, S. C., and J-L. Ge. Loss of suppression of GSH synthesis at low cell density in primary cultures of rat hepatocytes. Am. J. Physiol. 263:C1181–C1189, 1992.Google Scholar
  24. 24.
    Markwell, M.A.K., S. M. Haas, L. L. Bieber, and N. E. Tolbert. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87:206–210, 1CrossRefGoogle Scholar
  25. 25.
    Richman, P. G., and A. Meister. Regulation of τ-glutamylcysteine synthetase by nonallosteric feedback inhibition of glutathione. J. Biol. Chem. 216:763–773, 1975.Google Scholar
  26. 26.
    Schimke, R. T. Adaptive characteristics of urea cycle enzymes in the rat. J. Biol. Chem. 237:459–468, 1962.Google Scholar
  27. 27.
    Snodgrass, P. J., R. C. Lin, W. A. Muller, and T. T. Aoki. Induction of urea cycle enzymes of rat liver by glucagon. J. Biol. Chem. 253:2748–2753, 1Google Scholar
  28. 28.
    Steel, R.G.D., and J. H. Torrie. Principles and Procedures of Statistics. New York: McGraw-Hill, 1960, p. 99–160.Google Scholar
  29. 29.
    Stipanuk, M. H. Effect of excess dietary methionine on the catabolism of cysteine in rats. J. Nutr. 109:2126–2139, 1979.Google Scholar
  30. 30.
    Stipanuk, M. H., L. L. Hirschberger, and P. J. Bagley. Anion-exchange HPLC of taurine, cysteinesulfinate and cysteic acid. In: Taurine-Nutritional Value and Mechanisms of Action, edited by J. B. Lombardini, S. W. Schaffer and J. Azurne. New York: Plenum Press, 1992, p. 429–435.Google Scholar
  31. 31.
    Yamaguchi, K., S. Sakakibara, K. Kyoichiro, and U. Iwao. Induction and activation of cysteine oxidase of rat liver I. The effects of cysteine, hydrocortisone and nicotinamide injection on hepatic cysteine oxidase and tyrosine aminotransferase activities of intact and adrenalectomized rats. Biochim. Biophys. Acta 237:502–512, 1971.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • Deborah L. Bella
    • 1
  • Martha H. Stipanuk
    • 1
  1. 1.Division of Nutritional SciencesCornell UniversityIthacaUSA

Personalised recommendations