Publication Cover
Redox Report
Communications in Free Radical Research
Volume 9, 2004 - Issue 2
232
Views
11
CrossRef citations to date
0
Altmetric
Review Article

Vascular physiology and pathology of circulating xanthine oxidoreductase: from nucleotide sequence to functional enzyme

, &
Pages 71-79 | Published online: 19 Jul 2013

REFERENCES

  • Kunst F, Ogasawara N, Moszer I et al. The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 1997; 390: 249–256.
  • Schultz AC, Nygaard P, Saxild HH. Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J Bacteriol 2001; 183: 3293–3302.
  • Ichida K, Amaya Y, Noda K et al. Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene 1993; 133: 279–284.
  • Xu P, Zhu XL, Huecksteadt TP, Brothman AR, Hoidal JR. Assignment of human xanthine dehydrogenase gene to chromosome 2p22. Genomics 1994; 23: 289–291.
  • Xu P, Huecksteadt TP, Hoidal JR. Molecular cloning and characterization of the human xanthine dehydrogenase gene (xdh). Genomics 1996; 34: 173–180.
  • Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE. cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci USA 1993; 90: 10690–10694.
  • Martelin E, Palvimo JJ, Lapatto R, Raivio KO. Nuclear factor Y activates the human xanthine oxidoreductase gene promoter. FEBS Lett 2000; 480: 84–88.
  • Xu P, LaVallee P, Hoidal JR. Repressed expression of the humanxanthine oxidoreductase gene. E-box and TATA-like elements restrict ground state transcriptional activity. J Biol Chem 2000; 275: 5918–5926.
  • Moriwaki Y, Yamamoto T, Suda M et al. Purification and immunohistochemical tissue localization of human xanthine oxidase. Biochim Biophys Acta 1993; 1164: 327–330.
  • Massey V, Brumby PE, Komai H. Studies on milk xanthine oxidase. Some spectral and kinetic properties. J Biol Chem 1969; 244: 1682–1691.
  • Kisker C, Schindelin H, Rees DC. Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu Rev Biochem 1997; 66: 233–267.
  • Reiss J, Johnson JL. Mutations in the molybdenum cofactor biosynthetic genes MOCS I, MOCS2, and GEPH. Hum Mutat 2003; 21: 569–576.
  • Rajagopalan KV. Biosynthesis and processing of the molybdenum cofactors. Biochem Soc Trans 1997; 25: 757–761.
  • Wang J, Van Praagh A, Hamilton E et al. Serum xanthine oxidase: origin, regulation, and contribution to control of trypanosome parasitemia. Antioxid Redox Signal 2002; 4: 161–178.
  • Frazzon J, Fick JR, Dean DR. Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem Soc Trans 2002; 30: 680–685.
  • Nishino T, Okamoto K. The role of the [2Fe-2s] cluster centers in xanthine oxidoreductase. J Inorg Biochem 2000; 82: 43–49.
  • Martelin E, Lapatto R, Raivio KO. Regulation of xanthine oxidoreductase by intracellular iron. Am J Physiol 2002; 283: CI722–C1728.
  • Ghio AJ, Kennedy TP, Stonehuerner J et al. Iron regulates xanthine oxidase activity in the lung. Am J Physiol 2002; 283: L563–L572.
  • Huang YT, Ghio AJ, Nozik-Grayck E, Piantadosi CA. Vascular release of nonheme iron in perfused rabbit lungs. Am J Physiol 2001; 280: L474-L481.
  • Stryer L. Biosynthesis of nucleotides. In: Biochemistry, 4th edn. New York, W. H. Freeman, 1995; 739-762.
  • Edmondson DE, Newton-Vinson P. The covalent FAD of monoamine oxidase: structural and functional role and mechanism of the flavinylation reaction. Antioxid Redox Signal 2001; 3: 789–806.
  • Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A. Structural analysis of flavinylation in vanillyl-alcohol oxidase. J Biol Chem 2000; 275: 38654–38658.
  • Brizio C, Barile M, Brandsch R. Flavinylation of the precursor of mitochondrial dimethylglycine dehydrogenase by intact and solubilised mitochondria. FEBS Lett 2002; 522: 141–146.
  • Stirpe F, Della CE. 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 1969; 244: 3855–3863.
  • Corte ED, Stirpe F. 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 0) and purification of the enzyme. Biochem J1972; 126: 739-745.
  • McManaman JL, Bain DL. Structural and conformational analysis of the oxidase to dehydrogenase conversion of xanthine oxidoreductase. J Biol Chem 2002; 277: 21261–21268.
  • Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc Natl Acad Sci USA 2000; 97: 10723–10728.
  • Kuppusamy P. Zweier JL. Characterization of free radical generation by xanthine oxidase. Evidence for hydroxyl radical generation. J Biol Chem 1989; 264: 9880–9884.
  • Millar TM, Stevens CR, Benjamin N, Eisenthal R, Harrison R, Blake DR. Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions. FEBS Lett 1998; 427: 225–228.
  • Godber BL, Doel JJ, Durgan J, Eisenthal R, Harrison R. A new route to peroxynitrite: a role for xanthine oxidoreductase. FEBS Lett 2000; 475: 93–96.
  • Porras AG, Olson JS, Palmer G. The reaction of reduced xanthine oxidase with oxygen. Kinetics of peroxide and superoxide formation. J Biol Chem 1981; 256: 9096–9103.
  • Millar TM, Kanczler JM, Bodamyali T, Blake DR, Stevens CR. Xanthine oxidase is a peroxynitrite synthase: newly identified roles for a very old enzyme. Redox Report 2002; 7: 65–70.
  • Abadeh S, Killacky J, Benboubetra M, Harrison R. Purification and partial characterization of xanthine oxidase from human milk. Biochim Biophys Acta 1992; 1117: 25–32.
  • Al-Khalidi UAS, Chaglassian TH. The species distribution of xanthine oxidase. Biochem J 1965; 97: 3183–3200.
  • Battelli MG, Musiani S, Valgimigli M et al. Serum xanthine oxidase in human liver disease. Am J Gastroenterol 2001; 96: 1194–1199.
  • Kristensen SR. Mechanisms of cell damage and enzyme release. Dan Med Bull 1994; 41: 423–433.
  • Folch E, Salas A, Prats Net al. H(2)0(2) and PARS mediate lung P-selectin upregulation in acute pancreatitis. Free Radic Biol Med 2000; 28: 1286–1294.
  • Partridge CA, Blumenstock FA, Malik AB. Pulmonary micro-vascular endothelial cells constitutively release xanthine oxidase. Arch Biochem Biophys 1992; 294: 184–187.
  • Ichida K, Amaya Y, Kamatani N, Nishino T, Hosoya T, Sakai O. Identification of two mutations in human xanthine dehydro-genase gene responsible for classical type I xanthinuria. J Clin Invest 1997; 99: 2391–2397.
  • Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T. Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun 2001; 282: 1194–1200.
  • Quinlan GJ, Lamb NJ, Tilley R, Evans TW, Gutteridge JM. Plasma hypoxanthine levels in ARDS: implications for oxidative stress, morbidity, and mortality. Am J Respir Crit Care Med 1997; 155: 479–484.
  • Adachi T, Fukushima T, Usami Y, Hirano K. Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial-cell surface. Biochem J 1993; 289: 523–527.
  • Houston M, Estevez A, Chumley P et al. Binding of xanthine oxidase to vascular endothelium. Kinetic characterization and oxidative impairment of nitric oxide-dependent signaling. J Biol Chem 1999; 274: 4985–4994.
  • Takeyama N, Shoji Y, Ohashi K, Tanaka T. Role of reactive oxygen intermediates in lipopolysaccharide-mediated hepatic injury in the rat. J Surg Res 1996; 60: 258–262.
  • Roberts IS. The biochemistry and genetics of capsular polysaccharide production in bacteria. Annu Rev Microbiol 1996; 50: 285–315.
  • Stevens CR, Millar TM, Clinch JG, Kanczler JM, Bodamyali T, Blake DR. Antibacterial properties of xanthine oxidase in human milk. Lancet 2000; 356: 829–830.
  • Hancock JT, Salisbury V, Ovejero-Boglione MC et al. Antimicrobial properties of milk: dependence on presence of xanthine oxidase and nitrite. Antimicrob Agents Chem other 2002; 46: 3308–3310.
  • Nathan C, Xie QW. Nitric oxide synthases: roles, tolls, and controls. Cell 1994; 78: 915–918.
  • McCord JM. Oxygen-derived free radicals in postischemic tissue injury. N Engl J Med 1985; 312: 159–163.
  • Harrison R. Human xanthine oxidoreductase: in search of a function. Biochem Soc Trans 1997; 25: 786–791.
  • Kinugasa Y, Ogino K, Furuse Yet al. Allopurinol improves cardiac dysfunction after ischemia-reperfusion via reduction of oxidative stress in isolated perfused rat hearts. Circ J2003; 67: 781–787.
  • Maulik N. Redox signaling of angiogenesis. Antioxid Redox Signal 2002; 4: 805–815.
  • Allen RG, Tresini M. Oxidative stress and gene regulation. Free Radic Biol Med 2000; 28: 463–499.
  • Willemer S, Feddersen CO, Karges W, Adler G. Lung injury in acute experimental pancreatitis in rats. I. Morphological studies. Int J Pancreatol 1991; 8: 305–321.
  • Folch E, Salas A, Panes J et al. Role of P-selectin and ICAM-1 in pancreatitis-induced lung inflammation in rats: significance of oxidative stress. Ann Surg 1999; 230: 792–798.
  • Zingarelli B, Salzman AL, Szabo C. Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury. Circ Res 1998; 83: 85–94.
  • Sanders SA, Eisenthal R, Harrison R. NADH oxidase activity of human xanthine oxidoreductase - generation of superoxide anion. Eur J Biochem 1997; 245: 541–548.
  • Harris CM, Massey V. The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radical. J Biol Chem 1997; 272: 8370–8379.
  • Hunt J, Massey V. Studies of the reductive half-reaction of milk xanthine dehydrogenase. J Biol Chem 1994; 269: 18904–18914.
  • Doel JJ, Godber BL, Eisenthal R, Harrison R. Reduction of organic nitrates catalysed by xanthine oxidoreductase under anaerobic conditions. Biochim Biophys Acta 2001; 1527: 81–87.
  • Huie RE, Padmaja S. The reaction of NO with superoxide. Free Radic Res Commun 1993; 18: 195–199.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.