Skip to main content
SpringerLink
Log in
Book cover

The Role of Oxygen Radicals in Cardiovascular Diseases pp 51–69Cite as

Conversion of Rat Xanthine Dehydrogenase to Xanthine Oxidase during Oxidative Stress

  • Chapter

Abstract

The enzyme “xanthine oxidase” is one of the best characterized sources of superoxide anion and hydrogen peroxide. “In vivo” it mainly acts as a dehydrogenase which, by reducing NAD+, appears to be the physiologic form. Nevertheless under a variety of conditions the enzyme can undergo a conversion to an oxidase which delivers the electrons to oxygen to form superoxide and hydrogen peroxide. The transformation xanthine dehydrogenase→xanthine oxidase is irreversible when it is induced by a proteolytic attack or reversible when the SH groups of the enzyme have been oxidized.

This is a preview of subscription content, log in via an institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Adkinson, D., Höllwart, M.E., Benoit, J.N., Parks, D.A., McCord, J.M. and Granger, D.N., 1986. Role of free radicals in i senemia-reperfusion injury to liver. Acta Physiol. Scand., Suppl. 548: 101–107.

    Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Battelli, M.G., Lorenzoni, E. and Stirpe, F., 1973. Milk xanthine oxidase type D (dehydrogenase) and type 0 (oxidase) purification, interconversion and some properties. Biochem. J., 131: 191–198.

    PubMed  CAS  Google Scholar 

  • Battelli, M.G. and Lorenzoni, E., 1982. Purification and properties of a new glutathione-dependent thiol: disulfide oxidoreductase from rat liver. Biochem. J., 207: 133–138.

    PubMed  CAS  Google Scholar 

  • Clare, D.A., Blakistone, B.A., Swaisgood, H.E. and Horton, H.R., 1981. Sulfhydryl oxidase-catalyzed conversion of xanthine dehydrogenase to xanthine oxidase. Arch. Biochem. Biophys., 211: 44–47.

    Article  PubMed  CAS  Google Scholar 

  • Delia Corte, E. and Stirpe, F., 1972. The regulation of xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type 0) and purification of the enzyme. Biochem. J., 126: 739–745.

    Google Scholar 

  • Fridovich, I., 1970. Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J. Biol. Chem., 245: 4053–4057.

    PubMed  CAS  Google Scholar 

  • Gornall, A.G., Bardawill, C.J. and David, M.M., 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751–766.

    PubMed  CAS  Google Scholar 

  • Granger, D.N., Rutili, G. and McCord, J.M., 1981. Superoxide radicals in feline intestinal ischemia. Gastroenterology, 78: 474–480.

    Google Scholar 

  • Granger, D.N., Hollwarth, M.E. and Parks, D.A., 1986. Ischemia-reperfusion injury: role of oxygen-derived free radicals. Acta Physiol. Scand, Suppl. 548: 47–63.

    CAS  Google Scholar 

  • Guarnieri, C, Ferrari, R., Visioli, O., Caldarera, CM. and Nayler, W.G., 1978. Effect of α-tocopherol on hypoxic-perfused and reoxyge-nated rabbit heart muscle. J. Mol. Cell. Card., 10: 893–906.

    Article  CAS  Google Scholar 

  • Hansson, R.O., Jonsson, O., Lundstam, S., Petterson, S. and Schersten, T., 1983. Effects of free radical scavengers on renal circulation after ischemia in the rabbit. Clin. Sci. 65: 605–610.

    PubMed  CAS  Google Scholar 

  • Haerse, D.J., Manning, A.S., Downey, J.M. and Yellon, D.M., 1986. Xanthine oxidase: a critical mediator of myocardial injury during ischemia and reperfusion? Acta Physiol. Scand., Suppl. 548: 65–78.

    Google Scholar 

  • Jarasch, E.D., Grund, C, Bruder, G., Heid, H.W., Keenan, T.W. and Franke, W.W., 1981. Localization of xanthine oxidase in mammary gland epithelium and capillary endothelium. Cell, 25: 67–82.

    Article  PubMed  CAS  Google Scholar 

  • Jolly, S.R., Kane, W.J., Bailie, M.B., Abrams, G.D. and Lucchesi, B.R., 1984. Canine myocardial reperfusion injury. Its reduction by the combined administration of superoxide dismutase and catalase. Circ. Res., 54: 277–285.

    PubMed  CAS  Google Scholar 

  • Kaminski, Z.W. and Jezewska, M.M., 1979. Intermediate dehydrogenase-oxi- dase form of xanthine oxidoreductase in rat liver. Biochem. J., 181: 177–182.

    PubMed  CAS  Google Scholar 

  • Krenitsky, T.A., Tutle, J.V., Cattau, E.L. and Wang, P., 1974. A comparison of the distribution and electron acceptor specificities of xanthine oxidase and aldehyde oxidase. Comp. Biochem. Physiol., 49B: 687–703.

    Google Scholar 

  • Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J., 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193: 265–293.

    PubMed  CAS  Google Scholar 

  • Mannervik, B., Axelsson, K., Sundewall, A.C. and Holmgren, A., 1983. Relative contribution of thioltransferase — and thioredoxin — dependent systems in reduction of low molecular mass and protein disulphi-des. Biochem. J., 213: 519–523.

    PubMed  CAS  Google Scholar 

  • Manning, A.S., Coltart, D.J. and Hearse, D.J., 1984. Ischemia and reper-fusion-induced arrhythmias in the rat. Effect of xanthine oxidase inhibition with allopurinol. Circ. Res., 55: 545–548.

    PubMed  CAS  Google Scholar 

  • Olson, J.S., Ballou, D.P., Palmer, G. and Massey, V., 1974. The mechanism of action of xanthine oxidase. J. Biol. Chem., 249: 4363–4382.

    PubMed  CAS  Google Scholar 

  • Parks, D.A. and Granger, D.N., 1986. Xanthine oxidase: biochemistry, distribution and physiology. Acta Physiol. Scand., Suppl. 548: 87–99.

    CAS  Google Scholar 

  • Ramboer, C.R.H., 1969. A sensitive and nonradioactive assay for serum and tissue xanthine oxidase. J. Lab. Clin. Med., 74: 828–829.

    PubMed  CAS  Google Scholar 

  • Schousten, B., De Jong, J.W., Harmsen, E., De Tombe, P.P. and Achterberg, P.W., 1983. Myocardial xanthine oxidase/dehydrogenase. Biochim. Biophys. Acta, 762: 519–544.

    Article  Google Scholar 

  • Stirpe, F. and Delia Corte, E., 1969. The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type 0). J. Biol. Chem., 244: 3855–3863.

    PubMed  CAS  Google Scholar 

  • Tietze, F., 1969. Enzymatic method for quantitative determination of nanograms amounts of total and oxidized glutathione. Anal. Biochem. 27: 502–522.

    Article  PubMed  CAS  Google Scholar 

  • Ursini, F., Maiorino, M. and Gregolin, C, 1985. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta, 839: 62–70.

    PubMed  CAS  Google Scholar 

  • Waud, W.R. and Rajagopalan, K.V., 1976. The mechanism of conversion of rat liver xanthine dehydrogenase from a NAD+ -dependent form (type D) to an 02 dependent form (type D). Arch. Biochem. Biophys., 172: 365–379.

    Article  PubMed  CAS  Google Scholar 

  • Xia, Y., Hill, K.E. and Burk, R.F., 1985. Effect of selenium-deficiency on hydroperoxide-induced glutathione from the isolated perfused rat heart. J. Nutr., 115: 733–742.

    PubMed  CAS  Google Scholar 

  • Yagi, K., 1984. Malondialdehyde assay for blood plasma or serum. Methods Enzymol., 105: 328–331.

    Article  PubMed  CAS  Google Scholar 

  • Zimmer, H.G., Ibel, H., Suchner, U. and Schad, H., 1984. Ribose intervention in the cardiac pentose phosphate pathway is not species-specific. Science, 233: 712–714.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Centro Studio Fisiologia Mitocondriale, C.N.R. and Istituto di Chimica Biologica, Via F. Marzolo 3, 35131, Padova, Italy

    A. Bindoli, L. Cavallini, M. P. Rigobello, M. Coassin & F. Di Lisa

Authors
  1. A. Bindoli
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. L. Cavallini
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. M. P. Rigobello
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. M. Coassin
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. F. Di Lisa
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Institute of Clinical Physiology, CNR, Pisa, Italy

    A. L’Abbate

  2. Institute of Biochemistry, Padova, Italy

    F. Ursini

Rights and permissions

Reprints and permissions

Copyright information

© 1988 ECSC, EEC, EAEC, Brussels and Luxembourg

About this chapter

Cite this chapter

Bindoli, A., Cavallini, L., Rigobello, M.P., Coassin, M., Di Lisa, F. (1988). Conversion of Rat Xanthine Dehydrogenase to Xanthine Oxidase during Oxidative Stress. In: L’Abbate, A., Ursini, F. (eds) The Role of Oxygen Radicals in Cardiovascular Diseases. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-2697-4_6

Download citation

  • DOI: https://doi.org/10.1007/978-94-009-2697-4_6

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-7716-3

  • Online ISBN: 978-94-009-2697-4

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation