Taurine 3 pp 9-15 | Cite as

In Vitro Evaluation of Hypotaurine Activity on Oxidized LDL

  • Silvestro Dupré
  • Alberto Macone
  • Roberta Masella
  • Daniela Modesti
  • Claudio Giovannini
  • Alfredo Cantafora
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 442)


Recent reports on the antioxidant activity of hypotaurine indicate that it behaves as a hydroxyl radical scavenger7. In vitro experiments have shown excellent reactivity with ·OH and HOCl based on rate constants calculated for these reactions2. Cystamine-α-disulfone has been proposed as a product of the radical reaction12, as demonstrated by the isolation of this compound following an in vitro reaction of hypotaurine with Fenton’s reagent8. Notably cystamine-α-disulfone has been also isolated from male sexual tissues8. Hypotaurine affects the initiation, propagation and termination phases of lipid peroxidation15. In a recent review9 the antioxidant role of hypotaurine in the regenerating liver and male reproductive system, tissues in which hypotaurine is present in mM concentrations, has been discussed. In other tissues hypotaurine is present in such a minute amount (micromolar or less) as to cast doubts about its real capacity to act as an in vivo antioxidant. Target molecules for possible oxidation by highly reactive oxygen species (ROS, reactive oxygen species) are, among others, membrane lipids, protein structures and nucleic acids. A general protective effect of hypotaurine on membrane lipid structure is likely, in view of the protective action of hypotaurine on sperm motility1 and capacitation11.


Caffeic Acid Male Reproductive System Conjugate Diene Formation Excellent Reactivity Membrane Lipid Structure 
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.


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  1. 1.
    Alvarez, J.G. and Storey, B.T., 1983, Taurine, hypotaurine, epinephrine and albumin inhibit lipid peroxidation in rabbit spermatozoa and protect against loss of motility, Biol. Reprod., 29:548–555.PubMedCrossRefGoogle Scholar
  2. 2.
    Aruoma O.L., Halliwell B., Hoey B.M., and Butler J., 1988, The antioxidant action of taurine, hypotaurine and their metabolic precursors, Biochem. J., 256:251–255.PubMedGoogle Scholar
  3. 3.
    Baker, H.W., Brindle, J., Irvine, D.S., and Aitken, R.J., 1996, Protective effect of antioxidants on the impairment of sperm motility by activated polymorphonuclear leukocytes, Fertil. Steril, 65:411–419.PubMedGoogle Scholar
  4. 4.
    Beuge, J.A and Aust, S.D., 1978, Microsomal lipid peroxidation, in Methods Enzymol. “Biomembranes”, Fleischer, S. and Packer, L., eds., 52:308.Google Scholar
  5. 5.
    Bradford, M., 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding, Anal. Biochem., 72:248–254.PubMedCrossRefGoogle Scholar
  6. 6.
    Esterbauer, H., Gebicki, J., Puhl, H., and Jürgens, G., 1992, The role of lipid peroxidation and antioxidants in oxidative modification of LDL, Free Rad. Biol. and Med., 13:341–390.CrossRefGoogle Scholar
  7. 7.
    Fellman, J.H. and Roth, E.S., 1985, The biological oxidation of hypotaurine to taurine: hypotaurine as an antioxidant, in Progr. Clin. Biol. Res. “Taurine: Biological actions and clinical Perspectives”, Oja, S.S., Ahtee, L., Kontro, P., and Paasonen, M.K., eds., Alan R. Liss, Inc., New York, vol. 179, pp. 71–82.Google Scholar
  8. 8.
    Fellman, J.H., Green, T.R., and Eicher, A.L., 1987, The oxidation of hypotaurine to taurine: bis-aminoethyl-α-disulfone, a metabolic intermediate in mammalian tissue, in Adv. Exp. Med. Biol. “The Biology of Taurine: Methods and Mechanism”, Huxtable, R.J., Franconi, F., and Giotti, A., eds., Plenum Press, New York, Vol. 217, pp. 39–48.Google Scholar
  9. 9.
    Huxtable, R.J., 1992, Physiological actions of taurine, Physiol. Reviews, 72:101–163.Google Scholar
  10. 10.
    Lindgren, F.T., 1975, Preparative ultracentrifugal laboratory procedures and suggestions for lipoprotein analysis, in: “Analysis of lipids and lipoproteins”, Perkins E.G., ed., AOCS, Campaign 111., pp. 204–224.Google Scholar
  11. 11.
    Meizel, S., Lui, C.W., Working, P.K., and Mrsny, R.J., 1980, Taurine and hypotaurine: their effects on motility, capacitation and the acrosome reaction of hamster sperm in vitro and their presence in sperm and reproductive tract fluids of several mammals, Dev. Growth Differ., 22:483–494.CrossRefGoogle Scholar
  12. 12.
    Ricci, G., Duprè, S., Federici, G., Spoto, G., Matarese, R.M., and Cavallini, D., 1978, Oxidation of hypotaurine to taurine by ultraviolet irradiation, Physiol Chem. & Phys., 10:435–441.Google Scholar
  13. 13.
    Schnitzer, E., Pinchuk, I., Fainaru, M., Schafer, Z., and Lichtenberg, 1995, Copper-induced lipid oxidation in unfractioned plasma:the lag phase preceding oxidation as a measure of oxidation resistance, Biochem. Biophys. Res. Commun., 216:854–861.PubMedCrossRefGoogle Scholar
  14. 14.
    Schnitzer, E., Pinchuk, I., Bor, A., Fainaru, M., and Lichtenberg, D., 1997, The effect of albumin on copper-induced LDL oxidation, Biochim. Biophys. Acta, 1344:300–311.PubMedCrossRefGoogle Scholar
  15. 15.
    Tadolini, B., Pintus, G., Pinna, G.G., Bennardini, F., and Franconi, F., 1995, Effects of taurine and hypotaurine on lipid peroxidation, Biochem. Biophys. Res. Commun., 213:820–826.PubMedCrossRefGoogle Scholar
  16. 16.
    Wakayama, T., Suto, J.K., Imamura, K., Toyoda, Y., Kurohmaru, M., and Hayashi, Y., 1996, Effect of hypotaurine on in vitro fertilization and production of term offspring from in vitro-fertilized ova of the Japanese fiels vole, Microtus montebelli, Biol Reprod., 54:625–630.CrossRefGoogle Scholar
  17. 17.
    Witting, P.K., Upston, J.M., and Stocker, R., 1997, Role of α-tocopheroxyl radical in the initiation of lipid peroxidation in human low-density lipoprotein exposed to horse radish peroxidase, Biochemistry, 36:1251–1258.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Silvestro Dupré
    • 1
  • Alberto Macone
    • 1
  • Roberta Masella
    • 2
  • Daniela Modesti
    • 2
  • Claudio Giovannini
    • 2
  • Alfredo Cantafora
    • 2
  1. 1.Dipartimento di Scienze Biochimiche and Centro di Biologia Molecolare del C.N.R.Università di Roma “La Sapienza”RomaItaly
  2. 2.Laboratorio di Metabolismo e Biochimica PatologicaIstituto Superiore di SanitàRomaItaly

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