Advertisement

Interconversion Pathways of Aldose Reductase Induced by Thiol Compounds

  • Antonella Del Corso
  • Pier Giuseppe Vilardo
  • Catia Barsotti
  • Mario Cappiello
  • Ilaria Cecconi
  • Massimo Dal Monte
  • Isabella Marini
  • Stefania Banditelli
  • Umberto Mura
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 463)

Abstract

The occurrence of protein S-thiolation as a consequence of oxidative stress is widely recognized (Thomas et al., 1990; Lou et at, 1990; Schuppe et al., 1992; Giblin, et al., 1995). However, the role and the relevance of this process are still a matter of debate.

Keywords

Aldose Reductase Native Enzyme Thiol Compound Mixed Disulfide Italian National Research Council 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bhatnagar, A., Liu, S-Q., Petrash, J. M., and Srivastava, S. K. (1992) Mechanism of inhibition of aldose reductase by menadione (Vitamin K3), Molec. Pharmacol, 42, 917–921.Google Scholar
  2. Bohren, K. M., and Gabbay, K. H., (1993) Cys298 is responsible for reversible thiol-induced variation in aldose reductase activity, in “Enzymology and Molecular Biology of Carbonyl Metabolism”(Weiner, H., Ed. ), vol. 4, pp. 267–277, Plenum Press, New York.CrossRefGoogle Scholar
  3. Bradford, M. M., (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72, 248–254.PubMedCrossRefGoogle Scholar
  4. Brigelius, R., (1985) Mixed disulfides: biological functions and increase in oxidative stress in “Oxidative Stress”(Sies H., Ed) pp. 243–271, Academic Press, London.Google Scholar
  5. Cappiello, M., Voltarelli, M., Cecconi, I., Vilardo, P. G., Dal Monte, M., Marini, I., Del Corso, A., Wilson, D. K., Quiocho, F. A., Petrash, J. M., and Mura, U. (1996) Specifically targeted modification of human aldose reductase by physiological disulfides, J. Biol. Chem., 271, 33539–33544.PubMedCrossRefGoogle Scholar
  6. Cappiello, M., Voltarelli, M., Giannessi, M., Cecconi, I., Camici, G., Manao, G., Del Corso, A., and Mura, U., (1994) Glutathione dependent modification of bovine lens aldose reductase, Exp. Eye Res., 58, 491–501.PubMedCrossRefGoogle Scholar
  7. Cappiello, M., Vilardo, P. G., Cecconi, I., Leverenz, V, Giblin, F. J., Del Corso, A., and Mura, U., (1995) Occurrence of glutathione-modified aldose reductase in oxidatively stressed bovine lenses, Biochem. Biophys. Res. Commun. 207, 775–782.PubMedCrossRefGoogle Scholar
  8. Coan, C, Ji, J-H., Hideg, K., and Mehlhorn, R. J., (1992) Protein sulfhydryls are protected from irreversible oxidation by conversion to mixed disulfides, Arch. Biochem. Biophys., 295, 369–378.PubMedCrossRefGoogle Scholar
  9. Del Corso, A., Barsacchi, D., Camici, M., Garland, D., and Mura, U. (1989) Bovine lens aldose reductase: identification of two enzyme forms, Arch. Biochem. Biophys.,270, 604–610.PubMedCrossRefGoogle Scholar
  10. Del Corso, A., Barsacchi, D., Giannessi, M, Tozzi, M. G., Camici, M., Houben, J. L., Zandomeneghi, M., and Mura, U., (1990) Bovine lens aldose reductase: tight binding of the pyridine coenzyme, Arch. Biochem. Biophys, 283, 512–518.PubMedCrossRefGoogle Scholar
  11. Del Corso, A., Cappiello, M., and Mura, U., (1994) Thiol dependent oxidation of enzymes: the last chance against oxidative stress, Int. J. Biochem., 26, 745–750.PubMedCrossRefGoogle Scholar
  12. Del Corso, A., Dal Monte, M., Vilardo, P. G., Cecconi, I., Moschini, R., Banditelli, S., Cappiello, M., Tsai, L., and Mura, U., (1998) Site-specific inactivation of aldose reductase by 4-hydroxynonenal, Arch. Biochem. Bio-phys., 350, 245–248.CrossRefGoogle Scholar
  13. Del Corso, Voltarelli, M., Giannessi, M., Cappiello, M., Barsacchi, D., Zandomeneghi, M., Camici, M., and Mura, U., (1993) Thiol-dependent metal-catalyzed oxidation of bovine lens aldose reductase. II. Proteolytic susceptibility of the modified enzyme form, Arch. Biochem. Biophys. 300, 430–433.CrossRefGoogle Scholar
  14. Eriksson, B., and Eriksson, S. A., (1967) Synthesis and characterization of the L-cysteine-glutathione mixed disul-fide, Acta Chem. Scand., 21, 1304–1312.PubMedCrossRefGoogle Scholar
  15. Giannessi, M., Del Corso, A., Cappiello, M., Voltarelli, M., Marini, I., Barsacchi, D., Garland, D., Camici, M., and Mura, U., Thiol-dependent metal-catalyzed oxidation of bovine lens aldose reductase. I. Studies on the modification process, Arch. Biochem. Biophys., 300, 423–429.Google Scholar
  16. Giblin, F. J., Padgaonkar, V. A., Leverenz, V. R., Lin, L-R., Lou, M. F., Unakar, N. J., Dang, L., Dickerson, J. E. Jr., and Reddy, V. N., (1995) Nuclear light scattering, disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen, Exp. Eye Res. 60, 219–235.PubMedCrossRefGoogle Scholar
  17. Lou, M. F., and Dickerson, J. E. Jr., (1992) Protein-thiol mixed disulfides in human lens, Exp. Eye Res 55, 889–896.PubMedCrossRefGoogle Scholar
  18. Lou, M. F., Dickerson, J. E. Jr., and Garadi, R., (1990) The role of protein thiol mixed disulfide in cataractogenesis, Exp. Eye Res. 50, 819–826.PubMedCrossRefGoogle Scholar
  19. Schuppe, I., Moldeus, P., and Cotgreave, I. A., (1992) Protein-specific S-thiolation in human endothelial cells during oxidative stress, Biochem. Pharmacol. 44, 1757–1764.PubMedCrossRefGoogle Scholar
  20. Thomas, J. A., Park, E. M., Chai, Y. C., Brooks, R., Rokutan, K., and Johnston, R. B. Jr., (1990) S-Thiolation of protein sulfhydryls, in “Biological Reactive Intermediates IV: Molecular and Cellular Effects, and Human Impact” (Witmer, CM., Snyder, R., and Sipes, G., Eds. ) pp. 95–101, Plenum Press, New York.Google Scholar

Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • Antonella Del Corso
    • 1
  • Pier Giuseppe Vilardo
    • 1
  • Catia Barsotti
    • 1
  • Mario Cappiello
    • 1
  • Ilaria Cecconi
    • 1
  • Massimo Dal Monte
    • 1
  • Isabella Marini
    • 1
  • Stefania Banditelli
    • 1
  • Umberto Mura
    • 1
  1. 1.Dipartimento di Fisiologia e BiochimicaUniversità di PisaPisaItaly

Personalised recommendations