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Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase

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Abstract

Cadmium is known as to be a potent pulmonary carcinogen to human beings and to induce prostate tumor. The sequestration of cadmium, an extremely toxic element to living cells, which is performed by biological ligands such as amino acids, peptides, proteins or enzymes is important to minimize its participation in such deleterious processes. The synthesis of metallothionein is induced by a wide range of metals, in which cadmium is a particularly potent inducer. This protein is usually associated with cadmium exposure in man. Because metallothioneins may act as a detoxification agent for cadmium and chelation involves sulfur donor atoms, we administered only cadmium, cysteine, or methionine to rats and also each of these S-amino acids together with cadmium and measured the production of superoxide radicals derived from the conversion of xanthine dehydrogenase to xanthine oxidase. It could be seen in this work that the presence of cadmium enhances this conversion. However, its inoculation with cysteine or methionine almost completely diminishes this effect and this can be the result of the fact that these amino acids complex Cd(II). Thus, these compounds can be a model of the action of metallothionein, removing cadmium from circulation and preventing its deleterious effect.

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References

  1. S. J. Stohs and D. Bagchi, Oxidative mechanisms in the toxicity of metals ions, Free Radical Biol. Med. 18, 321–326 (1995).

    Article  CAS  Google Scholar 

  2. G. M. N. Araujo, C. B. Silva, and A. Hasson-Voloch, Comparison of inhibitory effect of mercury and cadmium on the creatine kinase from Electrophorus electrus (L.), Int. J. Biochem. Cell. Biol. 28(4), 491–497 (1996).

    Article  PubMed  CAS  Google Scholar 

  3. M. Margoshes and B. L. Vallee, A cadmium protein from equine kidney cortex, J. Am. Chem. Soc. 79, 4813–4814 (1957).

    Article  CAS  Google Scholar 

  4. H. Li and J. D. Otvos, 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein, Biochemistry 35, 13,929–13,936 (1996).

    CAS  Google Scholar 

  5. A. R. Green and M. J. Stillman, Oxidative quenching of luminescence from copper metallothionein, Inorg. Chim. Acta 226, 275–283 (1994).

    Article  CAS  Google Scholar 

  6. P. J. Thornalley and M. Vasak, Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of this reaction with superoxide and hydroxyl radicals, Biochem. Biophys. Acta 827, 36–44 (1985).

    PubMed  CAS  Google Scholar 

  7. M. J. Stillman, F. C. Shaw III, and K. T. Suzuki (eds.), Metallothioneins, VCH, New York (1992).

    Google Scholar 

  8. M. Yoshida, H. Ohta, Y. Yamauchi, Y. Seki, M. Sagi, K. Yamazaki, et al., Age-dependent changes in metallotionein levels in liver and kidney of the japanese, Biol. Trace Element Res. 63, 167–175 (1998).

    CAS  Google Scholar 

  9. J. Hidalgo, L. Campmany, M. Borras, J. S. Garvey, and A. Armario, Metallothionein response to stress in rats: role in free radical scanvenging. Am. J. Physiol. 255, E518-E524 (1988).

    PubMed  CAS  Google Scholar 

  10. M. Friedman, The Chemistry and Biochemistry of the Sulfhydryl Group in Amino Acids Peptides and Proteins, Pergamon, Oxford, UK (1973).

    Google Scholar 

  11. SQUERY, IUPAC. Stability Constants Database, Release 3, Academic Software, Timble, Otley, York, UK (1998).

    Google Scholar 

  12. E. Della Corte and F. Stirpe, The regulation of rat liver xanthine oxidase involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme, Biochem. J. 126, 739–745 (1972).

    PubMed  CAS  Google Scholar 

  13. M. G. Batelli, E. Della Corte, and F. Stirpe, Xanthine oxidase type D (dehydrogenase) in the intestine and other organs of the rat, Biochem. J. 126, 747–749 (1972).

    Google Scholar 

  14. O. R. Affonso, C. V. Ayres de Moura, V. Cavallari, and E. Mitidieri, Serum and liver xanthine oxidase in tumor bearing rats and mice, An. Acad. Bras. Ci. 53, 617–620 (1981).

    CAS  Google Scholar 

  15. S. Tan, Y. Yokoyama, E. Dickens, T. G. Cash, B. A. Freeman, and D. A. Parks, Xanthine oxidase activity in the circulation of rats following hemorrhagic shock, Free Radical Biol. Med. 15, 407–414 (1993).

    Article  CAS  Google Scholar 

  16. F. Stirpe and E. Della Corte, The regulation of rat liver xanthine oxidase conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O). J. Biol. Chem. 244, 3855–3863 (1969).

    PubMed  CAS  Google Scholar 

  17. R. Fried, Colorimetric determination of xanthine dehydrogenase by tetrazolium reduction, Anal. Biochem. 16, 427–432 (1966).

    Article  CAS  Google Scholar 

  18. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, Protein measurement with the Folin phenol reagent, J. Biol. Chem. 193, 265–275 (1951).

    PubMed  CAS  Google Scholar 

  19. D. C. Montgomery, Design and Analysis of Experiments, Wiley, New York (1991).

    Google Scholar 

  20. M. J. Stillman, Metalothioneins, Coord. Chem. Rev. 144, 461–511 (1995).

    Article  CAS  Google Scholar 

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Esteves, A.C., Felcman, J. Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase. Biol Trace Elem Res 76, 19–30 (2000). https://doi.org/10.1385/BTER:76:1:19

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  • DOI: https://doi.org/10.1385/BTER:76:1:19

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