Extracellular superoxide dismutase, uric acid, and atherosclerosis

Cold Spring Harbor Symposia on Quantitative Biology

Volumn 67, Issue , 2002, Pages 483-490

  Hink, H U ^a,b   Fukai, T ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOCOPHEROL; COPPER; EXTRACELLULAR SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; URIC ACID; ZINC; APOLIPOPROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; PEROXIDASE; PEROXYNITRITE;

ATHEROGENESIS; ATHEROSCLEROSIS; CARDIOVASCULAR DISEASE; CLINICAL TRIAL; CONFERENCE PAPER; CYTOSOL; ENZYME ACTIVITY; HUMAN; LIPID PEROXIDATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; ARTICLE; ENZYME INACTIVATION; NEUROLOGIC DISEASE; OXIDATION REDUCTION POTENTIAL;

EID: 0038801198     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.2002.67.483     Document Type: Conference Paper

References (63)

1. Alderman M.H., Cohen H., Madhavan S., and Kivlighn S. 1999. Serum uric acid and cardiovascular events in successfully treated hypertensive patients (comments). Hypertension 34: 144.
2. Ames B.N., Cathcart R., Schwiers E., and Hochstein P. 1981. Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: A hypothesis. Proc. Natl. Acad. Sci. 78: 6858.
3. Beyer W., Imlay J., and Fridovich I. 1991. Superoxide dismutases. Prog. Nucleic Acid Res. Mol. Biol. 40: 221.
4. Brand F.N., McGee D.L., Kannel W.B., Stokes J., III, and Castelli W.P. 1985. Hyperuricemia as a risk factor of coronary heart disease: The Framingham Study. Am. J. Epidemiol. 121: 11.
5. Cominacini L., Garbin U., Pasini A.F., Davoli A., Campagnola M., Contessi G.B., Pastorino A.M., and Lo Cascio V. 1997. Antioxidants inhibit the expression of intercellular cell adhesion molecule-1 and vascular cell adhesion molecule-1 induced by oxidized LDL on human umbilical vein endothelial cells. Free Radic. Biol. Med. 22: 117.
6. Culleton B.F., Larson M.G., Kannel W.B., and Levy D. 1999. Serum uric acid and risk for cardiovascular disease and death: The Framingham Heart Study. Ann. Intern. Med. 131: 7.
7. Davies K.J., Sevanian A., Muakkassah-Kelly S.F., and Hochstein P. 1986. Uric acid-iron ion complexes. A new aspect of the antioxidant functions of uric acid. Biochem. J. 235: 747.
8. Freedman D.S., Williamson D.F., Gunter E.W., and Byers T. 1995. Relation of serum uric acid to mortality and ischemic heart disease. The NHANES I Epidemiologic Follow-up Study. Am. J. Epidemiol. 141: 637.
9. Fridovich I. 1965. The competitive inhibition of uricase by oxonate and related derivatives of s-triazines. J. Biol. Chem. 240: 2491.
10. -. 1997. Superoxide anion radical (O2-.), superoxide dismutases, and related matters. J. Biol. Chem. 272: 18515.
11. Fukai T., Folz R.J., Landmesser U., and Harrison D.G. 2002. Extracellular superoxide dismutase and cardiovascular disease. Cardiovasc. Res. 55: 239.
12. Fukai T., Galis Z.S., Meng X.P., Parthasarathy S., and Harrison D.G. 1998. Vascular expression of extracellular superoxide dismutase in atherosclerosis. J. Clin. Invest. 101: 2101.
13. Fukai T., Siegfried M.R., Ushio-Fukai M., Cheng Y., Kojda G., and Harrison D.G. 2000. Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training. J. Clin. Invest. 105: 1631.
14. Gertler M.M., Garn S.M., and Levine S.A. 1951. Serum uric acid in relation to age and physique in health and in coronary artery disease. Ann. Intern. Med. 34: 1421.
15. Ginsberg M.H., Kozin F., O'Malley M., and McCarty D.J. 1977. Release of platelet constituents by monosodium urate crystals. J. Clin. Invest. 60: 999.
16. Goss S.P., Singh R.J., and Kalyanaraman B. 1999. Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical. J. Biol. Chem. 274: 28233.
17. Griendling K.K., Sorescu D., and Ushio-Fukai M. 2000. NAD(P)H oxidase: Role in cardiovascular biology and disease. Circ. Res. 86: 494.
18. Hink H.U., Santanam N., Dikalov S., McCann L., Nguyen A.D., Parthasarathy S., Harrison D.G., and Fukai T. 2002. Peroxidase properties of extracellular superoxide dismutase. Role of uric acid in modulating in vivo activity. Arterioscler. Thromb. Vasc. Biol. 22: 1402.
19. Hjalmarsson K., Marklund S.L., Engstrom A., and Edlund T. 1987. Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc. Natl. Acad. Sci. 84: 6340.
20. Hodgson E.K. and Fridovich I. 1975. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme. Biochemistry 14: 5294.
21. 2. Free Radic. Biol. Med. 26: 905.
22. Karlsson K. and Marklund S.L. 1987. Heparin-induced release of extracellular superoxide dismutase to human blood plasma. Biochem. J. 242: 55.
23. Kojda G. and Harrison D. 1999. Interactions between NO and reactive oxygen species: Pathophysiological importance in atherosclerosis, hypertension, diabetes and heart failure. Cardiovasc. Res. 43: 562.
24. Landmesser U., Merten R., Spiekermann S., Buttner K., Drexler H., and Hornig B. 2000. Vascular extracellular superoxide dismutase activity in patients with coronary artery disease: Relation to endothelium-dependent vasodilation. Circulation 101: 2264.
25. Laukkanen M.O., Lehtolainen P., Turunen P., Aittomaki S., Oikari P., Marklund S.L., and Yla-Herttuala S. 2000. Rabbit extracellular superoxide dismutase: Expression and effect on LDL oxidation. Gene 254: 173.
26. Lehto S., Niskanen L., Ronnemaa T., and Laakso M. 1998. Serum uric acid is a strong predictor of stroke in patients with non-insulin-dependent diabetes mellitus. Stroke 29: 635.
27. Liese A.D., Hense H.W., Lowel H., Doring A., Tietze M., and Keil U. 1999. Association of serum uric acid with all-cause and cardiovascular disease mortality and incident myocardial infarction in the MONICA Augsburg cohort. World Health Organization Monitoring Trends and Determinants in Cardiovascular Diseases. Epidemiology 10: 391.
28. Liochev S.I. and Fridovich I. 1999. On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase. Free Radic. Biol. Med. 27: 1444.
29. Luoma J.S., Stralin P., Marklund S.L., Hiltunen T.P., Sarkioja T., and Yla-Herttuala S. 1998. Expression of extracellular SOD and iNOS in macrophages and smooth muscle cells in human and rabbit atherosclerotic lesions: Colocalization with epitopes characteristic of oxidized LDL and peroxynitrite-modified proteins. Arterioscler. Thromb. Vasc. Biol. 18: 157.
30. Maples K.R. and Mason R.P. 1988. Free radical metabolite of uric acid. J. Biol. Chem. 263: 1709.
31. Marchioli R. 1999. Antioxidant vitamins and prevention of cardiovascular disease: Laboratory, epidemiological and clinical trial data. Pharmacol. Res. 40: 227.
32. Marklund S.L. 1982. Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. 79: 7634.
33. -. 1984. Properties of extracellular superoxide dismutase from human lung. Biochem. J. 220: 269.
34. -. 1990. Expression of extracellular superoxide dismutase by human cell lines. Biochem. J. 266: 213.
35. Marklund S.L., Bjelle A., and Elmqvist L.G. 1986. Superoxide dismutase isoenzymes of the synovial fluid in rheumatoid arthritis and in reactive arthritides. Ann. Rheum. Dis. 45: 847.
36. Marklund S.L., Holme E., and Hellner L. 1982. Superoxide dismutase in extracellular fluids. Clin. Chim. Acta 126: 41.
37. Marui N., Offermann M.K., Swerlick R., Kunsch C., Rosen C.A., Ahmad M., Alexander R.W., and Medford R.M. 1993. Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells. J. Clin. Invest. 92: 1866.
38. Moriarity J.T., Folsom A.R., Iribarren C., Nieto F.J., and Rosamond W.D. 2000. Serum uric acid and risk of coronary heart disease: Atherosclerosis Risk in Communities (ARIC) Study. Ann. Epidemiol. 10: 136.
39. Moshage H., Kok B., Huizenga J.R., and Jansen P.L. 1995. Nitrite and nitrate determinations in plasma: A critical evaluation. Clin. Chem. 41: 892.
40. Nelson S.K., Bose S.K., and McCord J.M. 1994. The toxicity of high-dose superoxide dismutase suggests that superoxide can both initiate and terminate lipid peroxidation in the reperfused heart. Free Radic. Biol. Med. 16: 195.
41. Ohta H., Adachi T., and Hirano K. 1994. Internalization of human extracellular-superoxide dismutase by bovine aortic endothelial cells. Free Radic. Biol. Med. 16: 501.
42. Oury T.D., Day B.J., and Crapo J.D. 1996a. Extracellular superoxide dismutase: A regulator of nitric oxide bioavailability. Lab. Invest. 75: 617.
43. Oury T.D., Crapo J.D., Valnickova Z., and Enghild J.J. 1996b. Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: A simplified, high-yield purification of extracellular superoxide dismutase. Biochem. J. 317: 51.
44. Rao G.N. and Berk B.C. 1992. Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression. Circ. Res. 70: 593.
45. Rao G.N., Corson M.A., and Berk B.C. 1991. Uric acid stimulates vascular smooth muscle cell proliferation by increasing platelet-derived growth factor A-chain expression. J. Biol. Chem. 266:8604.
46. Sandstrom J., Carlsson L., Marklund S.L., and Edlund T. 1992. The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity. J. Biol. Chem. 267: 18205.
47. Sankarapandi S. and Zweier J.L. 1999. Bicarbonate is required for the peroxidase function of Cu, Zn-superoxide dismutase at physiological pH. J. Biol. Chem. 274: 1226.
48. Scott M.D., Meshnick S.R., and Eaton J.W. 1987. Superoxide dismutase-rich bacteria. Paradoxical increase in oxidant toxicity. J. Biol. Chem. 262: 3640.
49. Sentman M.L., Brannstrom T., Westerlund S., Laukkanen M.O., Yla-Herttuala S., Basu S., and Marklund S.L. 2001. Extracellular superoxide dismutase deficiency and atherosclerosis in mice. Arterioscler. Thromb. Vasc. Biol. 21: 1477.
50. 2/NO2-: Role of nitrogen dioxide free radical. Proc. Natl. Acad. Sci. 95: 12912.
51. Steinberg D. 1997. Low density lipoprotein oxidation and its pathobiological significance. J. Biol. Chem. 272: 20963.
52. Strålin P., Karlsson K., Johansson B.O., and Markland S.L. 1995. The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase. Arterioscler. Thromb. Vasc. Biol. 15: 2032.
53. Tainer J.A., Getzoff E.D., Richardson J.S., and Richardson D.C. 1983. Structure and mechanism of copper, zinc superoxide dismutase. Nature 306: 284.
54. Takatsu H., Tasaki H., Kim H.N., Ueda S., Tsutsui M., Yamashita K., Toyokawa T., Morimoto Y., Nakashima Y., and Adachi T. 2001. Overexpression of EC-SOD suppresses endothelial-cell-mediated LDL oxidation. Biochem. Biophys. Res. Commun. 285: 84.
55. Tribble D.L., Gong E.L., Leeuwenburgh C., Heinecke J.W., Carlson E.L., Verstuyft J.G., and Epstein C.J. 1997. Fatty streak formation in fat-fed mice expressing human copper-zinc superoxide dismutase (erratum in Arterioscler. Thromb. Vasc. Biol. [1997] 17: 3363). Arterioscler. Thromb. Vasc. Biol. 17: 1734.
56. Wannamethee S.G., Shaper A.G., and Whincup P.H. 1997. Serum urate and the risk of major coronary heart disease events. Heart 78: 147.
57. Whiteman M. and Halliwell B. 1996. Protection against peroxynirite-dependent tyrosine nitration and alpha 1-antiproteinase inactivation by ascorbic acid. A comparison with other biological antioxidants. Free Radic. Res. 25: 275.
58. Wiedau-Pazos M., Goto J.J., Rabizadeh S., Gralla E.B., Roe J.A., Lee M.K., Valentine J.S., and Bredesen D.E. 1996. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis (comments). Science 271: 515.
59. Witztum J.L. and Steinberg D. 2001. The oxidative modification hypothesis of atherosclerosis: Does it hold for humans? Trends Cardiovasc. Med. 11: 93.
60. Wu X.W., Lee C.C., Muzny D.M., and Caskey C.T. 1989. Urate oxidase: Primary structure and evolutionary implications. Proc. Natl. Acad. Sci. 86: 9412.
61. Wung B.S., Cheng J.J., Hsieh H.J., Shyy Y.J., and Wang D.L. 1997. Cyclic strain-induced monocyte chemotactic protein-1 gene expression in endothelial cells involves reactive oxygen species activation of activator protein 1. Circ. Res. 81: 1.
62. Zelko I.N., Mariani T.J., and Folz R.J. 2002. Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD 1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 33: 337.
63. Zhang H., Joseph J., Felix C., and Kalyanaraman B. 2000. Bicarbonate enhances the hydroxylation, nitration, and peroxidation reactions catalyzed by copper, zinc superoxide dismutase. Intermediacy of carbonate anion radical. J. Biol. Chem. 275: 14038.