Abstract
Taurine (2-aminoethane sulfonic acid) is a sulfur containing amino acid that is present in mammalian tissues in millimolar concentrations10. Taurine is involved in a diverse array of biological functions which include: osmoregulation, membrane stabilization, neuromodulation, bile salt conjugation, and calcium modulation10. A role for taurine in cellular antioxidant defense mechanisms has been observed under a number of conditions3,17,21,25. Although taurine appears to have little intrinsic reactivity with oxidizing species1, its high concentration may still allow it to directly scavenge free radicals. Furthermore, taurine may bind reactive quinones involved in redox cycling and indirectly inhibit free radical formation11,22. Taurine could also moderate the effects of free radical damage by blunting the ability of prooxidants to increase intracellular free calcium10. The biosynthesis of taurine generates intermediates (hypotaurine and cysteamine) that also have free radical scavenging properties1,10,25. The synthesis of taurine also utilizes cysteine which is an excitatory amino acid that undergoes autoxidation reactions13. Taurine is present in tissues that contain high concentrations of catecholamines which are known to be cytotoxic and increase oxidative stress8,9,16,20. Taurine content declines in brain and peripheral tissues in aged rodents4. The age-related decline in tissue taurine content could increase the susceptibility of cells to free radical-mediated damage. Catecholamines are known to undergo autoxidation reactions to generate free radicals (H2O2, hydroxyl, superoxide) and cytotoxic quinones8,11,22. The oxidation of catecholamines is catalyzed by metals such as iron13. Iron-stimulated autoxidation of catecholamines is thought to play a role in neurodegenerative diseases26. One study has reported that chronic treatment with l-dopa caused a 13% decline in brain taurine content23. At present, it is unclear whether taurine under in vivo conditions serves as a scavenger for reactive quinones and free radicals derived from catecholamine autoxidation.
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
Aruoma, O.I., Halliwell, B., Hoey, B.M., and Butler, J., 1988, The antioxidant action of taurine, hypotaurine and their metabolic precursors, Biochem. J., 256:251–255.
Carney, J.M., Starke-Reed, P.E., Oliver, C.N., Landum, R.W., Cheng, M.S., Wu, J.F., and Floyd, R.A., 1991, Reversal of age-related increases in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tertbutyl-α-phenylnitrone, Proc. Natl. Acad. Sci., 88:3633–3636.
Cozzi, R., Ricordy, R., Bartolini, Ramadori, L., Perticone, P., and De Salvia, R., 1995, Taurine and ellagic acid: two differently-acting natural antioxidants, Environ. Mol. Mutagen., 26:248–254.
Dawson, R. and Wallace, D.R., 1992, Taurine content in tissues from aged Fischer 344 rats, Age, 15:73–81.
Dawson, R., Felheim, R. and Phillips, M.I., 1994, Characterization of the synthesis and release of dopamine in LLC-PK1 cells, Renal Physiol. Biochem., 17:85–100.
Dawson, R., Eppler, B., Patterson, T.A., Shih, D., and Liu, S., 1996, The effects of taurine in a rodent model of aging, in Adv. Exp. Med. Biol. “Taurine 2 Basic and Clinical Aspects”, Huxtable, R.J., Azuma, J., Kuriyama, K., Nakagawa, M., and Baba, A., eds., Plenum Press, Vol. 403, pp. 37-50.
Dean, R.T., Gieseg, S., and Davies, R.T., 1993, Reactive species and their accumulation on radical damaged proteins, Trends Biochem. Sci., 18:437–441.
Graham, D.G., Tiffany, S.M., Bell, W.R., and Gutknecht, W.F., 1978, Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro, Mol. Pharmacol., 14:644–653.
Han, S-K., Mytilineou, C., and Cohen, G., 1996, L-DOPA up-regulates glutathione and protects mesencephalic cultures against oxidative stress, J. Neurochem., 66:501–510.
Huxtable, R.J., 1992, Physiological actions of taurine, Physiol. Rev., 72:101–163.
Kalyanaraman, B., Premovic, P.I., and Sealy, R.C., 1987, Semiquinone anion radicals from addition of amino acids, peptides, and proteins to quinones derived from oxidation of catechols and catecholamines, J. Biol. Chem., 262:11080–11087.
Levine, R.L, Garland, D., Oliver, C.N., Amici, A.A., Climent, I., Lenz, A., Ahn, B., Shaltiel, S., and Stadtman, E.R., 1990, Determination of carbonyl content in oxidatively modified proteins, Meth. Enzymol., 186:464–478.
Miller, D.M., Buettner, G.R., and Aust, S.D., 1990, Transition metals as catalysts of “autoxidation” reactions, Free Rad. Biol. Med., 8:95–108.
Monks, T.J. and Lau, S.S., 1992, Toxicology of quinone-thioethers, Crit. Rev. Toxicol., 22:243–270.
Mosmann, T., 1983, Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays, J. Immunol. Meth., 65:55–63.
Pardo, B., Mena, M.A., Casarejos, M.J., Paino, C.L., and De Yebenes, J.G., 1995, Toxic effects of l-dopa on mesencephalic cell cultures: protection with antioxidants, Brain Res., 682:133–143.
Pasantes-Morales, H., Wright, C.E., and Gaull, G.E., 1985, Taurine protection of lymphoblastoid cells from iron-ascorbate induced damage, Biochem. Pharmacol., 34:2205–2207.
Spencer, J.P.E., Jenner, A., Aruoma, O.I., Evans, P.J., Kaur, H., Dexter, D.T., Jenner, P., Lees, A.J., Marsden, D.C., and Halliwell, B., 1994, Intense oxidative DNA damage promoted by l-dopa and its metabolites implications for neurodegenerative disease, FEBS Lett., 353:246–250.
Stadtman, E.R. and Oliver, C.N., 1991, Metal-catalyzed oxidation of proteins, J. Biol. Chem., 266:2005–2008.
Tanaka, M., Sotomatsu, A., Kanai, H., and Hirai, S., 1991, Dopa and dopamine cause cultured neuronal death in the presence of iron, J. Neurol. Sci., 101:198–203.
Trachtman, H., Futterwiet, S., and Bienkowski, R.S., 1993, Taurine prevents glucose-induced lipid peroxidation and increased collagen production in cultured rat mesangial cells, Biochem. Biophys. Res. Comm., 191:759–765.
Tse, D.C.S., McCreery, R.L., and Adams, R., 1976, Potential oxidative pathways of brain catecholamines, J. Med. Chem., 19:37–40.
Tyce, G.M. and Owen, C.A., 1973, The effect of L-3,4-dihydroxyphenylalanine administration on glucose metabolism in brain, J. Neurochem., 20:1563–1573.
Wills, E.D., 1987, Evaluation of lipid peroxidation in lipids and biological membranes, in “Biochemical Toxicology a Practical Approach” Snell, K. and Mullock, B., eds., IRL Press, Oxford, pp. 127–152.
Wright, C.E., Tallan, H.H., Lin, Y.Y., and Gaull, G.E., 1986, Taurine: biological update, Ann. Rev. Biochem., 55:427–453.
Youdim, M.B.H., Ben-Shachar, D., Eshel, G., Finberg, J.P.M., and Riederer, P., 1993, The neurotoxicity of iron and nitric oxide relevance to the etiology of Parkinson’s disease, Adv. Neurol., 60:259–265.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Dawson, R. et al. (1998). Taurine Inhibition of Iron-Stimulated Catecholamine Oxidation. In: Schaffer, S., Lombardini, J.B., Huxtable, R.J. (eds) Taurine 3. Advances in Experimental Medicine and Biology, vol 442. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0117-0_20
Download citation
DOI: https://doi.org/10.1007/978-1-4899-0117-0_20
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-0119-4
Online ISBN: 978-1-4899-0117-0
eBook Packages: Springer Book Archive