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Published in: Pathology & Oncology Research 1/2014

01-01-2014 | Review

Xanthine Oxido-Reductase, Free Radicals and Cardiovascular Disease. A Critical Review

Authors: A. M. Robert, L. Robert

Published in: Pathology & Oncology Research | Issue 1/2014

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Abstract

Free radical mediated pathologies occupy a special place in medical semiology and in mechanistic interpretation of diseases. Free radicals, or better reactive oxygen species (ROS) or reactive nitrogen species (RNS) play also an important role in cell signaling. This is the basis of the ambivalent (Jekyll – Hyde) situation of ROS in biology and pathology. Aging itself is attributed by a popular theory to free radicals. A number of ROS – scavenging substances and procedures were described without however reaching credibility for their therapeutic value. An interesting exception is the xanthine oxido - reductase produced ROS and their role in cardiovascular disease. Allopurinol inhibition of xanthine oxido – reductase was shown to be efficient in some cases of cardiovascular diseases. Another important aspect of xanthine oxido – reductase produced ROS is their antibacterial capacity considered to be of importance with newborns fed on milk rich in this enzyme as well as at the gastrointestinal barrier. This ambivalent role of xanthine oxido – reductase justifies this review on the basic enzymatic mechanisms involved, derived ROS production, their role in the above mentioned biological processes and especially the interest of the inhibition of this enzyme as a preventive or curative measure in some cardiovascular pathologies.
Literature
2.
go back to reference Harman D (1955) Aging — a theory based on free radical and information theory U.C.R.L. Publ., 3078, Univ. of Calif. Harman D (1955) Aging — a theory based on free radical and information theory U.C.R.L. Publ., 3078, Univ. of Calif.
3.
go back to reference Comfort A (1979) The biology of senescence, 3rd edn. Churchill Livingstone, Edinburgh & London, 1979 Comfort A (1979) The biology of senescence, 3rd edn. Churchill Livingstone, Edinburgh & London, 1979
4.
go back to reference Emerit I, Eds BC (1992) Free radicals and aging. Birkhäuser Verlag, Basel, 1992CrossRef Emerit I, Eds BC (1992) Free radicals and aging. Birkhäuser Verlag, Basel, 1992CrossRef
5.
go back to reference Edeas M (2009) Anti-oxydants, controverses et perspectives: comment expliquer l’échec des etudes cliniques utilisant des anti-oxydants. J Soc Biol 203:271–280PubMedCrossRef Edeas M (2009) Anti-oxydants, controverses et perspectives: comment expliquer l’échec des etudes cliniques utilisant des anti-oxydants. J Soc Biol 203:271–280PubMedCrossRef
6.
go back to reference Blokhina O, Virolainen E, Fagerstedt KV (2003) Antioxidants, oxidative damage and oxygen deprivation stress: a review. Ann Bot 91:179–194PubMedCrossRef Blokhina O, Virolainen E, Fagerstedt KV (2003) Antioxidants, oxidative damage and oxygen deprivation stress: a review. Ann Bot 91:179–194PubMedCrossRef
7.
go back to reference Martin HM, Hancock JT, Salisbury V, Harrison R (2004) Mini-review. Role of xanthine oxydoreductase as an antimicrobial agent. Infect Immun 72:4933–4939PubMedCentralPubMedCrossRef Martin HM, Hancock JT, Salisbury V, Harrison R (2004) Mini-review. Role of xanthine oxydoreductase as an antimicrobial agent. Infect Immun 72:4933–4939PubMedCentralPubMedCrossRef
8.
9.
go back to reference Garattini E, Mendel R, Romao MJ, Wright R, Terao M (2003) Review article. Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372:15–32PubMedCrossRef Garattini E, Mendel R, Romao MJ, Wright R, Terao M (2003) Review article. Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372:15–32PubMedCrossRef
10.
go back to reference Drury AN, Szent-Györgyi A (1929) The physiological activity of adenine compounds with especial reference to their action upon the mammalian heart. J Physiol 68:213–237PubMed Drury AN, Szent-Györgyi A (1929) The physiological activity of adenine compounds with especial reference to their action upon the mammalian heart. J Physiol 68:213–237PubMed
12.
13.
go back to reference Dowben RM, Brunner JR, Philpott DE (1967) Studies on milk fat globule membranes. Biochim Biophys Acta 135:1–10PubMedCrossRef Dowben RM, Brunner JR, Philpott DE (1967) Studies on milk fat globule membranes. Biochim Biophys Acta 135:1–10PubMedCrossRef
14.
go back to reference Polonovski M, Robert M, Robert L (1950) Cinétique de la révélation de la xanthinedéhydrase du lait de vache. Bull Soc Chim Biol 32:862–867PubMed Polonovski M, Robert M, Robert L (1950) Cinétique de la révélation de la xanthinedéhydrase du lait de vache. Bull Soc Chim Biol 32:862–867PubMed
15.
go back to reference Polonovski M, Baudu L, Robert M, Robert L (1950) Données nouvelles sur la révélation de la xanthine-déhydrase du lait par les agents chimiques. Bull Soc Chim Biol 32:855–861PubMed Polonovski M, Baudu L, Robert M, Robert L (1950) Données nouvelles sur la révélation de la xanthine-déhydrase du lait par les agents chimiques. Bull Soc Chim Biol 32:855–861PubMed
16.
go back to reference Polonovski M, Robert L, Robert M (1950) Une nouvelle méthode d’extraction et de purification de la xanthine déhydrase du lait. Bull Soc Chim Biol 32:868–871PubMed Polonovski M, Robert L, Robert M (1950) Une nouvelle méthode d’extraction et de purification de la xanthine déhydrase du lait. Bull Soc Chim Biol 32:868–871PubMed
17.
go back to reference Robert L, Basset J (1953) Action des hautes pressions sur la xanthinedéhydrase du lait. Bull Soc Chim Biol 35:1375–1380PubMed Robert L, Basset J (1953) Action des hautes pressions sur la xanthinedéhydrase du lait. Bull Soc Chim Biol 35:1375–1380PubMed
18.
go back to reference Robert L, Nolla N (1953) Action des ultrasons sur la xanthinedéhydrase du lait. Bull Soc Chim Biol 35:1363–1373PubMed Robert L, Nolla N (1953) Action des ultrasons sur la xanthinedéhydrase du lait. Bull Soc Chim Biol 35:1363–1373PubMed
19.
go back to reference Robert L, Polonovski M (1955) Activation and inactivation of milk xanthineoxydase by physicochemical means. In: Discussions of the Faraday Society, N° 20, The Physical Chemistry of Enzymes The Aberdeen University Press Ltd; 6 Upper Kirkgate, Aberdeen, pp 54–65 Robert L, Polonovski M (1955) Activation and inactivation of milk xanthineoxydase by physicochemical means. In: Discussions of the Faraday Society, N° 20, The Physical Chemistry of Enzymes The Aberdeen University Press Ltd; 6 Upper Kirkgate, Aberdeen, pp 54–65
20.
go back to reference Avis PG, Berger F, Bray RC, Shooter KV (1954) A crystalline material with xanthine oxidase activity. Nature 173:1230–1233PubMedCrossRef Avis PG, Berger F, Bray RC, Shooter KV (1954) A crystalline material with xanthine oxidase activity. Nature 173:1230–1233PubMedCrossRef
21.
go back to reference Avis PG, Bergel F, Bray RC (1955) Cellular constituents. The chemistry of xanthine oxidase. Pat I. The preparation of a crystalline xanthine oxidase from cow’s milk. J Chem Soc April 1100–1105 Avis PG, Bergel F, Bray RC (1955) Cellular constituents. The chemistry of xanthine oxidase. Pat I. The preparation of a crystalline xanthine oxidase from cow’s milk. J Chem Soc April 1100–1105
22.
go back to reference Avis PG, Bergel F, Bray RC, James DWF, Shooter KV (1956) Cellular constituents. The chemistry of xanthine oxidase. Part II. The homogeneity of crystalline metalloflavoprotein fractions. J Chem Soc 252:1212–1219CrossRef Avis PG, Bergel F, Bray RC, James DWF, Shooter KV (1956) Cellular constituents. The chemistry of xanthine oxidase. Part II. The homogeneity of crystalline metalloflavoprotein fractions. J Chem Soc 252:1212–1219CrossRef
23.
go back to reference Avis PG, Bergel F, Bray RC (1956) Cellular constituents. The chemistry of xanthine oxidase. Part III. Estimations of the co-factors and the catalytic activities of enzyme fractions from cow’s milk. J Chem Soc 253:1219–1226CrossRef Avis PG, Bergel F, Bray RC (1956) Cellular constituents. The chemistry of xanthine oxidase. Part III. Estimations of the co-factors and the catalytic activities of enzyme fractions from cow’s milk. J Chem Soc 253:1219–1226CrossRef
24.
go back to reference Bergel F, Bray RC (1959) The chemistry of xanthine oxidase. 4. The problems of enzyme inactivation and stabilisation. Biochem J 73:182–192PubMed Bergel F, Bray RC (1959) The chemistry of xanthine oxidase. 4. The problems of enzyme inactivation and stabilisation. Biochem J 73:182–192PubMed
25.
go back to reference Bray RC, Chisholm AJ, Hart LI, Meriwether LS, Watts DC (1966) Studies on the composition and mechanism of action of milk xanthine oxidase. In: Slater EC (ed) Flavins and flavoproteins. Elsevier Publishing Company, Amsterdam, pp 117–132 Bray RC, Chisholm AJ, Hart LI, Meriwether LS, Watts DC (1966) Studies on the composition and mechanism of action of milk xanthine oxidase. In: Slater EC (ed) Flavins and flavoproteins. Elsevier Publishing Company, Amsterdam, pp 117–132
26.
go back to reference Haddow A, de Lamirande G, Bergel F, Bray RC, Gilbert DA (1958) Anti-tumour and biochemical effects of purified bovine xanthine oxidase in C3H and C mice. Nature 182:1144–1146PubMedCrossRef Haddow A, de Lamirande G, Bergel F, Bray RC, Gilbert DA (1958) Anti-tumour and biochemical effects of purified bovine xanthine oxidase in C3H and C mice. Nature 182:1144–1146PubMedCrossRef
27.
go back to reference Mackler B, Mahler HR, Green DE (1954) Studies on metalloflavoproteins. I. Xanthine oxydase. A molybdoflavoprotein. J Biol Chem 210:149–164PubMed Mackler B, Mahler HR, Green DE (1954) Studies on metalloflavoproteins. I. Xanthine oxydase. A molybdoflavoprotein. J Biol Chem 210:149–164PubMed
28.
go back to reference Berry CE, Hare JM (2004) Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. J Physiol 555:589–606PubMedCrossRef Berry CE, Hare JM (2004) Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. J Physiol 555:589–606PubMedCrossRef
29.
go back to reference Granger DN, Rutili G, McCord J (1981) Superoxide radicals in feline intestinal ischemia. Gastroenterology 81:22–29PubMed Granger DN, Rutili G, McCord J (1981) Superoxide radicals in feline intestinal ischemia. Gastroenterology 81:22–29PubMed
30.
31.
go back to reference Harrison R (2002) Structure and function of xanthine oxidoreductase: where are we now? Free Radic Biol Med 33:774–797PubMedCrossRef Harrison R (2002) Structure and function of xanthine oxidoreductase: where are we now? Free Radic Biol Med 33:774–797PubMedCrossRef
32.
go back to reference Granger DN, Rutili G, McCord JM (1981) Superoxide radicals in feline intestinal ischemia. Gastroenterology 81:22–29PubMed Granger DN, Rutili G, McCord JM (1981) Superoxide radicals in feline intestinal ischemia. Gastroenterology 81:22–29PubMed
33.
go back to reference Abadeh S, Killacky J, Benboubetra M, Harrison R (1992) Purification and partial characterization of xanthine oxidase from human milk. Biochim Biophys Acta 1117:25–32PubMedCrossRef Abadeh S, Killacky J, Benboubetra M, Harrison R (1992) Purification and partial characterization of xanthine oxidase from human milk. Biochim Biophys Acta 1117:25–32PubMedCrossRef
34.
go back to reference Vorbach C, Scriven A, Capecchi MR (2002) The housekeeper gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary gland. Genes Dev 16:3223–3235PubMedCrossRef Vorbach C, Scriven A, Capecchi MR (2002) The housekeeper gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary gland. Genes Dev 16:3223–3235PubMedCrossRef
35.
go back to reference Simmonds HA (1994) Purine and pyrimidine disorders. In: Holton JS (ed) The Inherited metabolic diseases, 2nd edn. Churchill Livingstone, New York, pp 297–307 Simmonds HA (1994) Purine and pyrimidine disorders. In: Holton JS (ed) The Inherited metabolic diseases, 2nd edn. Churchill Livingstone, New York, pp 297–307
36.
go back to reference Delbarre F, Cartier P, Auscher C, De Géry A, Hamet M (1970) Gouttes enzymopathiques. Dyspurinies par déficit en Hypoxanthine-Guanine-Phosphoribosyl-Transférase. Fréquence et caractères cliniques de l’anenzymose. Presse Med 78:729–734PubMed Delbarre F, Cartier P, Auscher C, De Géry A, Hamet M (1970) Gouttes enzymopathiques. Dyspurinies par déficit en Hypoxanthine-Guanine-Phosphoribosyl-Transférase. Fréquence et caractères cliniques de l’anenzymose. Presse Med 78:729–734PubMed
37.
go back to reference Ea H-K, Bardin T, Jinnah HA, Aral B, Lioté F, Ceballos - Picot I (2009) Severe Gouty Arthritis and mild neurologic symptoms due to F199C, a newly identified variant of the hypoxanthine guanine phosphoribosyltransferase. Arthritis Rheum 60:2201–2220PubMedCentralPubMedCrossRef Ea H-K, Bardin T, Jinnah HA, Aral B, Lioté F, Ceballos - Picot I (2009) Severe Gouty Arthritis and mild neurologic symptoms due to F199C, a newly identified variant of the hypoxanthine guanine phosphoribosyltransferase. Arthritis Rheum 60:2201–2220PubMedCentralPubMedCrossRef
38.
go back to reference Lewers JC, Ceballos-Picot I, Shirley TL, Mockel L, Egami K, Jinnah HA (2008) Consequences of impaired purine recycling in dopaminergic neurons. Neuroscience 152:761–772PubMedCentralPubMedCrossRef Lewers JC, Ceballos-Picot I, Shirley TL, Mockel L, Egami K, Jinnah HA (2008) Consequences of impaired purine recycling in dopaminergic neurons. Neuroscience 152:761–772PubMedCentralPubMedCrossRef
39.
go back to reference Bollée G, Dollinger C, Boutaud L, Guillemot D, Bensman A, Harambat J, Deteix P, Daudon M, Knebelmann B, Ceballos-Picot I (2010) Phenotype and genotype characterization of adenine phosphoribosyltransfetrase deficiency. J Am Soc Nephrol 4:679–688CrossRef Bollée G, Dollinger C, Boutaud L, Guillemot D, Bensman A, Harambat J, Deteix P, Daudon M, Knebelmann B, Ceballos-Picot I (2010) Phenotype and genotype characterization of adenine phosphoribosyltransfetrase deficiency. J Am Soc Nephrol 4:679–688CrossRef
40.
go back to reference Jinnah HA, Ceballos-Picot I, Torres RJ, Visser JE, Schretlen DJ, Verdu A, Larovere LE, Chen S-J, Cossu A et al (2010) Attenuated variants of Lesch-Nyhan disease. Brain 133:671–689PubMedCrossRef Jinnah HA, Ceballos-Picot I, Torres RJ, Visser JE, Schretlen DJ, Verdu A, Larovere LE, Chen S-J, Cossu A et al (2010) Attenuated variants of Lesch-Nyhan disease. Brain 133:671–689PubMedCrossRef
41.
go back to reference Li H, Samouilov A, Liu X, Zweier JL (2003) Characterization of the magnitude and kinetics of xanthine oxidase – catalysed nitrate reduction: evaluation of its role in nitrite and nitric oxide generation in anoxic tissues. Biochemistry 42:1150–1159PubMedCrossRef Li H, Samouilov A, Liu X, Zweier JL (2003) Characterization of the magnitude and kinetics of xanthine oxidase – catalysed nitrate reduction: evaluation of its role in nitrite and nitric oxide generation in anoxic tissues. Biochemistry 42:1150–1159PubMedCrossRef
42.
go back to reference Kayyali US, Donaldson C, Huang H, Abdelnour R, Hassoun PM (2001) Phosphorylation of xanthine dehydrogenase/oxidase in hypoxia. J Biol Chem 276:14359–14365PubMedCrossRef Kayyali US, Donaldson C, Huang H, Abdelnour R, Hassoun PM (2001) Phosphorylation of xanthine dehydrogenase/oxidase in hypoxia. J Biol Chem 276:14359–14365PubMedCrossRef
43.
go back to reference Adachi T, Fukushima T, Usami Y, Hirano K (1993) Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial cell surface. Biochem J 289:523–527PubMed Adachi T, Fukushima T, Usami Y, Hirano K (1993) Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial cell surface. Biochem J 289:523–527PubMed
44.
go back to reference Brown JM, Terrada LS, Grosso MA, Whitmann GJ, Velasco SE, Patt A, Harken AH, Repine JE (1988) Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated, perfused rat hearts. J Clin Invest 81:1297–1301PubMedCentralPubMedCrossRef Brown JM, Terrada LS, Grosso MA, Whitmann GJ, Velasco SE, Patt A, Harken AH, Repine JE (1988) Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated, perfused rat hearts. J Clin Invest 81:1297–1301PubMedCentralPubMedCrossRef
45.
go back to reference Wang W, Sawicki G, Schulz R (2002) Peroxinitrite – induced myocardial injury is mediated through matrix metalloproteinase-2. Cardiovasc Res 53:165–174PubMedCrossRef Wang W, Sawicki G, Schulz R (2002) Peroxinitrite – induced myocardial injury is mediated through matrix metalloproteinase-2. Cardiovasc Res 53:165–174PubMedCrossRef
46.
go back to reference Wang W, Schulze CJ, Suarez-Pinzon WL, Dyck JRB, Sawicki G, Schulz R (2002) Intracellular action of matrix metalloproteinase - 2 accounts for acute myocardial ischemia and reperfusion injury. Circulation 106:1543–1549PubMedCrossRef Wang W, Schulze CJ, Suarez-Pinzon WL, Dyck JRB, Sawicki G, Schulz R (2002) Intracellular action of matrix metalloproteinase - 2 accounts for acute myocardial ischemia and reperfusion injury. Circulation 106:1543–1549PubMedCrossRef
47.
go back to reference Campbell DL, Stamler JS, Strauss HC (1996) Redox modulation of L-type calcium channels in ferret ventricular myocytes dual mechanism regulation by nitric oxide and S-nitrosothiols. J General Physiol 108:277–293CrossRef Campbell DL, Stamler JS, Strauss HC (1996) Redox modulation of L-type calcium channels in ferret ventricular myocytes dual mechanism regulation by nitric oxide and S-nitrosothiols. J General Physiol 108:277–293CrossRef
48.
50.
go back to reference Truglio JJ, Theis K, Leimkühler S, Rappa R, Rajagopalan KV, Kisker C (2002) Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10:115–125PubMedCrossRef Truglio JJ, Theis K, Leimkühler S, Rappa R, Rajagopalan KV, Kisker C (2002) Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10:115–125PubMedCrossRef
51.
go back to reference Sanders S, Eisenthal RS, Harrison R (1997) NADH oxidase activity of human xanthine oxidoreductase –generation of superoxide anion. Eur J Biochem 245:541–548PubMedCrossRef Sanders S, Eisenthal RS, Harrison R (1997) NADH oxidase activity of human xanthine oxidoreductase –generation of superoxide anion. Eur J Biochem 245:541–548PubMedCrossRef
52.
go back to reference Brown JM, Terada LS, Grosso MA, Whitmann GJ, Velasco SE, Patt A, Harken AH, Repine JE (1988) Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated perfused rat hearts. J Clin Invest 81:1297–1301PubMedCentralPubMedCrossRef Brown JM, Terada LS, Grosso MA, Whitmann GJ, Velasco SE, Patt A, Harken AH, Repine JE (1988) Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated perfused rat hearts. J Clin Invest 81:1297–1301PubMedCentralPubMedCrossRef
53.
go back to reference Grisham MB, Hernandez LA, Granger DN (1986) Xanthine oxidase and neutrophil infiltration in intestinal ischemia. Am J Physiol 251:G567–G574PubMed Grisham MB, Hernandez LA, Granger DN (1986) Xanthine oxidase and neutrophil infiltration in intestinal ischemia. Am J Physiol 251:G567–G574PubMed
54.
go back to reference Gimpel JA, Lahpor JR, van der Molen A, Damen J, Hitchcock JF (1995) Reduction of reperfusion injury of human myocardium by allopurinol: a clinical study. Free Radic Biol Med 19:251–255PubMedCrossRef Gimpel JA, Lahpor JR, van der Molen A, Damen J, Hitchcock JF (1995) Reduction of reperfusion injury of human myocardium by allopurinol: a clinical study. Free Radic Biol Med 19:251–255PubMedCrossRef
55.
go back to reference Guan W, Osanai T, Kamada T, Hanada H, Ishizaka H, Onodera H, Iwasa A, Fujita N, Kudo S, OhkuboT OK (2003) Effect of allopurinol pretreatment on free radical generation after primary coronary angioplasty for acute myocardial infarction. J Cardiovasc Pharmacol 41:699–705PubMedCrossRef Guan W, Osanai T, Kamada T, Hanada H, Ishizaka H, Onodera H, Iwasa A, Fujita N, Kudo S, OhkuboT OK (2003) Effect of allopurinol pretreatment on free radical generation after primary coronary angioplasty for acute myocardial infarction. J Cardiovasc Pharmacol 41:699–705PubMedCrossRef
56.
go back to reference Butler R, Morris AD, Belch JJF, Hill A, Struthers AD (2000) Allopurinol normalizes endothelial dysfunction in type 2 diabetics with mild hypertension. Hypertension 35:746–751PubMedCrossRef Butler R, Morris AD, Belch JJF, Hill A, Struthers AD (2000) Allopurinol normalizes endothelial dysfunction in type 2 diabetics with mild hypertension. Hypertension 35:746–751PubMedCrossRef
57.
go back to reference Nakazono K, Watanabe N, Matsuno K, Sasaki J, Sato T, Iwasaki T (2003) Does superoxide underlie the pathogenesis of hypertension? Proc Natl Acad Sci USA 88:10045–10048CrossRef Nakazono K, Watanabe N, Matsuno K, Sasaki J, Sato T, Iwasaki T (2003) Does superoxide underlie the pathogenesis of hypertension? Proc Natl Acad Sci USA 88:10045–10048CrossRef
58.
go back to reference Kögler H, Fraser H, McCune S, Altschuld R, Marban E (2003) Disproportionate enhancement of myocardial contractility by the xanthine oxidase inhibitor oxypurinol in failing rat myocardium. Cardiovasc Res 59:582–592PubMedCrossRef Kögler H, Fraser H, McCune S, Altschuld R, Marban E (2003) Disproportionate enhancement of myocardial contractility by the xanthine oxidase inhibitor oxypurinol in failing rat myocardium. Cardiovasc Res 59:582–592PubMedCrossRef
59.
go back to reference Cappola TP, Kass DA, Nelson GS, Berger RD, Rosas GO, Kobeissi ZA, Marban E, Hare JM (2001) Allopurinol improves myocardial efficiency in patients with idiopathic dilated cardiomyopathy. Circulation 104:2407–2411PubMedCrossRef Cappola TP, Kass DA, Nelson GS, Berger RD, Rosas GO, Kobeissi ZA, Marban E, Hare JM (2001) Allopurinol improves myocardial efficiency in patients with idiopathic dilated cardiomyopathy. Circulation 104:2407–2411PubMedCrossRef
61.
go back to reference Galiardi AC, Miname MH, Santos RD (2009) Uric acid: a marker of increased cardiovascular risk. Atherosclerosis 202:11–17CrossRef Galiardi AC, Miname MH, Santos RD (2009) Uric acid: a marker of increased cardiovascular risk. Atherosclerosis 202:11–17CrossRef
62.
go back to reference Krishnan E, Baker JF, Furst DE, Schumacher HR (2006) Gout and the risk of acute myocardial infarction. Arthritis Rheum 54:2688–2696PubMedCrossRef Krishnan E, Baker JF, Furst DE, Schumacher HR (2006) Gout and the risk of acute myocardial infarction. Arthritis Rheum 54:2688–2696PubMedCrossRef
63.
go back to reference Krishnan E, Pandya BJ, Lingala B, Hariri A, Dabbous O (2012) Hyperuricemia and untreated gout are poor prognostic markers among those with a recent acute myocardial infarction. Arthritis Res Ther 14:R10PubMedCentralPubMedCrossRef Krishnan E, Pandya BJ, Lingala B, Hariri A, Dabbous O (2012) Hyperuricemia and untreated gout are poor prognostic markers among those with a recent acute myocardial infarction. Arthritis Res Ther 14:R10PubMedCentralPubMedCrossRef
64.
go back to reference Baker JF, Schumacher HR, Krishnan E (2007) Serum uric acid level and risk for peripheral arterial disease: analysis of data from the multiple risk factor intervention trial. Angiology 58:450–457PubMedCrossRef Baker JF, Schumacher HR, Krishnan E (2007) Serum uric acid level and risk for peripheral arterial disease: analysis of data from the multiple risk factor intervention trial. Angiology 58:450–457PubMedCrossRef
65.
go back to reference Krishnan E, Svendsen K, Neaton JD, Grandits G, Kuller RH (2008) Long-term cardiovascular mortality among middle – aged men with gout. Arch Intern Med 168:1104–1110PubMedCrossRef Krishnan E, Svendsen K, Neaton JD, Grandits G, Kuller RH (2008) Long-term cardiovascular mortality among middle – aged men with gout. Arch Intern Med 168:1104–1110PubMedCrossRef
66.
go back to reference Choi HK, Curhan G (2007) Independent impact of gout on mortality and risk for coronary heart disease. Circulation 116:894–900PubMedCrossRef Choi HK, Curhan G (2007) Independent impact of gout on mortality and risk for coronary heart disease. Circulation 116:894–900PubMedCrossRef
67.
go back to reference Hanassoulis G, Brophy JM, Richard H, Pilote L (2010) Gout, allopurinol use and heart failure outcomes. Arch Intern Med 170:1358–1364CrossRef Hanassoulis G, Brophy JM, Richard H, Pilote L (2010) Gout, allopurinol use and heart failure outcomes. Arch Intern Med 170:1358–1364CrossRef
68.
go back to reference Noman A, Ang DS, Ogston S, Lang CC, Struthers AD (2010) Effect of high - dose allopurinol on exercise in patients with chronic stable angina: a randomized, placebo controlled crossover trial. Lancet 375:2161–2167PubMedCentralPubMedCrossRef Noman A, Ang DS, Ogston S, Lang CC, Struthers AD (2010) Effect of high - dose allopurinol on exercise in patients with chronic stable angina: a randomized, placebo controlled crossover trial. Lancet 375:2161–2167PubMedCentralPubMedCrossRef
69.
go back to reference Feig DI, Soletsky B, Johnson RJ (2008) Effect of allopurinol on blood pressure of adolescents with newly diagnosed essential hypertension: a randomized trial. JAMA 300:924–932PubMedCentralPubMedCrossRef Feig DI, Soletsky B, Johnson RJ (2008) Effect of allopurinol on blood pressure of adolescents with newly diagnosed essential hypertension: a randomized trial. JAMA 300:924–932PubMedCentralPubMedCrossRef
70.
Metadata
Title
Xanthine Oxido-Reductase, Free Radicals and Cardiovascular Disease. A Critical Review
Authors
A. M. Robert
L. Robert
Publication date
01-01-2014
Publisher
Springer Netherlands
Published in
Pathology & Oncology Research / Issue 1/2014
Print ISSN: 1219-4956
Electronic ISSN: 1532-2807
DOI
https://doi.org/10.1007/s12253-013-9698-x

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