Extracellular superoxide dismutase polymorphism in mice: Allele-specific effects on phenotype

Free Radical Biology and Medicine

Volumn 48, Issue 4, 2010, Pages 590-596

  Jun, Sujung ^a   Pierce, Anson ^a   Dory, Ladislav ^a  

^a UNIVERSITY OF NORTH TEXAS HEALTH SCIENCE CENTER   (United States)

Author keywords

129P3 J; Antioxidants; C57BL 6J; Congenic mice; ecSOD; Free radicals; Plasma; Polymorphism; Tissue

Indexed keywords

HEPARIN; MESSENGER RNA; SUPEROXIDE DISMUTASE;

ALLELE; ANIMAL TISSUE; ARTICLE; BACKCROSSING; CONGENIC STRAIN; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME RELEASE; ENZYME SYNTHESIS; FEMALE; GENE EXPRESSION; GENOTYPE; HETEROZYGOTE; HOMOZYGOTE; MALE; MOUSE; MUTATIONAL ANALYSIS; NONHUMAN; OXIDATIVE STRESS; PHENOTYPE; PRIORITY JOURNAL; PROGENY; PROTEIN EXPRESSION; SINGLE NUCLEOTIDE POLYMORPHISM; TISSUE DISTRIBUTION;

3' UNTRANSLATED REGIONS; ALLELES; ANIMALS; CHROMOSOME MAPPING; CROSSES, GENETIC; FEMALE; HEPARIN; MALE; MICE; MICE, INBRED C57BL; MICROSATELLITE REPEATS; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS; PHENOTYPE; POLYMORPHISM, GENETIC; SUPEROXIDE DISMUTASE;

MUS;

EID: 74149092508     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.12.003     Document Type: Article

References (40)

1. Pierce A., Whitlark J., and Dory L. Extracellular superoxide dismutase polymorphism in mice. Arterioscler. Thromb. Vasc. Biol. 23 (2003) 1820-1825
2. Beckman J.S., Beckman T.W., Chen J., Marshall P.A., and Freeman B.A. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87 (1990) 1620-1624
3. Oury T.D., Day B.J., and Crapo J.D. Extracellular superoxide dismutase: a regulator of nitric oxide bioavailability. Lab. Invest. 75 (1996) 617-636
4. Brahmajothi M.V., and Campbell D.L. Heterogeneous basal expression of nitric oxide synthase and superoxide dismutase isoforms in mammalian heart: implications for mechanisms governing indirect and direct nitric oxide-related effects. Circ. Res. 85 (1999) 575-587
5. Ushio-Fukai M. Redox signaling in angiogenesis: role of NADPH oxidase. Cardiovasc. Res. 71 (2006) 226-235
6. Capettini L.S., Cortes S.F., Gomes M.A., Silva G.A., Pesquero J.L., Lopes M.J., Teixeira M.M., and Lemos V.S. Neuronal nitric oxide synthase-derived hydrogen peroxide is a major endothelium-dependent relaxing factor. Am. J. Physiol. Heart Circ. Physiol. 295 (2008) H2503-2511
7. Faraci F.M., and Didion S.P. Vascular protection: superoxide dismutase isoforms in the vessel wall. Arterioscler. Thromb. Vasc. Biol. 24 (2004) 1367-1373
8. Fattman C.L., Tan R.J., Tobolewski J.M., and Oury T.D. Increased sensitivity to asbestos-induced lung injury in mice lacking extracellular superoxide dismutase. Free Radic. Biol. Med. 40 (2006) 601-607
9. Jung O., Marklund S.L., Geiger H., Pedrazzini T., Busse R., and Brandes R.P. Extracellular superoxide dismutase is a major determinant of nitric oxide bioavailability: in vivo and ex vivo evidence from ecSOD-deficient mice. Circ. Res. 93 (2003) 622-629
10. Kim H.W., Lin A., Guldberg R.E., Ushio-Fukai M., and Fukai T. Essential role of extracellular SOD in reparative neovascularization induced by hindlimb ischemia. Circ. Res. 101 (2007) 409-419
11. Sheng H., Kudo M., Mackensen G.B., Pearlstein R.D., Crapo J.D., and Warner D.S. Mice overexpressing extracellular superoxide dismutase have increased resistance to global cerebral ischemia. Exp. Neurol. 163 (2000) 392-398
12. Chen E.P., Bittner H.B., Davis R.D., Folz R.J., and Van Trigt P. Extracellular superoxide dismutase transgene overexpression preserves postischemic myocardial function in isolated murine hearts. Circulation 94 (1996) II412-II417
13. Ghio A.J., Suliman H.B., Carter J.D., Abushamaa A.M., and Folz R.J. Overexpression of extracellular superoxide dismutase decreases lung injury after exposure to oil fly ash. Am. J. Physiol. Lung Cell. Mol. Physiol. 283 (2002) L211-L218
14. Levin E.D. Extracellular superoxide dismutase (EC-SOD) quenches free radicals and attenuates age-related cognitive decline: opportunities for novel drug development in aging. Curr. Alzheimer. Res. 2 (2005) 191-196
15. Gao F., Koenitzer J.R., Tobolewski J.M., Jiang D., Liang J., Noble P.W., and Oury T.D. Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan. J. Biol. Chem. 283 (2008) 6058-6066
16. Kliment C.R., Tobolewski J.M., Manni M.L., Tan R.J., Enghild J., and Oury T.D. Extracellular superoxide dismutase protects against matrix degradation of heparan sulfate in the lung. Antioxid. Redox Signaling 10 (2008) 261-268
17. Kliment C.R., Englert J.M., Gochuico B.R., Yu G., Kaminski N., Rosas I., and Oury T.D. Oxidative stress alters syndecan-1 distribution in lungs with pulmonary fibrosis. J. Biol. Chem. 284 (2009) 3537-3545
18. Sandstrom J., Carlsson L., Marklund S.L., and Edlund T. The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity. J. Biol. Chem. 267 (1992) 18205-18209
19. Karlsson K., Edlund A., Sandstrom J., and Marklund S.L. Proteolytic modification of the heparin-binding affinity of extracellular superoxide dismutase. Biochem. J. 290 Pt 2 (1993) 623-626
20. Petersen S.V., Oury T.D., Ostergaard L., Valnickova Z., Wegrzyn J., Thogersen I.B., Jacobsen C., Bowler R.P., Fattman C.L., Crapo J.D., and Enghild J.J. Extracellular superoxide dismutase (EC-SOD) binds to type I collagen and protects against oxidative fragmentation. J. Biol. Chem. 279 (2004) 13705-13710
21. Sandstrom J., Karlsson L., Edlund T., and Marklund S.L. Heparin-affinity patterns and composition of extracellular superoxide dismutase in human plasma and tissues. Biochem. J. 294 Pt 3 (1993) 853-857
22. Stralin P., Karlsson K., Johansson B.O., and Marklund S.L. The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase. Arterioscler. Thromb. Vasc. Biol. 15 (1995) 2032-2036
23. Karlsson K., Sandstrom J., Edlund A., and Marklund S.L. Turnover of extracellular-superoxide dismutase in tissues. Lab. Invest. 70 (1994) 705-710
24. Oury T.D., Day B.J., and Crapo J.D. Extracellular superoxide dismutase in vessels and airways of humans and baboons. Free Radic. Biol. Med. 20 (1996) 957-965
25. Warshamana G.S., Pociask D.A., Sime P., Schwartz D.A., and Brody A.R. Susceptibility to asbestos-induced and transforming growth factor-beta1-induced fibroproliferative lung disease in two strains of mice. Am. J. Respir. Cell Mol. Biol. 27 (2002) 705-713
26. Fujii M., Hara H., Meng W., Vonsattel J.P., Huang Z., and Moskowitz M.A. Strain-related differences in susceptibility to transient forebrain ischemia in SV-129 and C57black/6 mice. Stroke 28 (1997) 1805-1810 discussion 1811
27. Ward N.L., Moore E., Noon K., Spassil N., Keenan E., Ivanco T.L., and LaManna J.C. Cerebral angiogenic factors, angiogenesis, and physiological response to chronic hypoxia differ among four commonly used mouse strains. J. Appl. Physiol. 102 (2007) 1927-1935
28. Paigen B., Ishida B.Y., Verstuyft J., Winters R.B., and Albee D. Atherosclerosis susceptibility differences among progenitors of recombinant inbred strains of mice. Arteriosclerosis 10 (1990) 316-323
29. Prass K., Wiegand F., Schumann P., Ahrens M., Kapinya K., Harms C., Liao W., Trendelenburg G., Gertz K., Moskowitz M.A., Knapp F., Victorov I.V., Megow D., and Dirnagl U. Hyperbaric oxygenation induced tolerance against focal cerebral ischemia in mice is strain dependent. Brain Res. 871 (2000) 146-150
30. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
31. Marklund S.L. Analysis of extracellular superoxide dismutase in tissue homogenates and extracellular fluids. Methods Enzymol. 186 (1990) 260-265
32. Paoletti F., and Mocali A. Determination of superoxide dismutase activity by purely chemical system based on NAD(P)H oxidation. Methods Enzymol. 186 (1990) 209-220
33. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
34. Folz R.J., Guan J., Seldin M.F., Oury T.D., Enghild J.J., and Crapo J.D. Mouse extracellular superoxide dismutase: primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization. Am. J. Respir. Cell Mol. Biol. 17 (1997) 393-403
35. Karlsson K., and Marklund S.L. Heparin-induced release of extracellular superoxide dismutase to human blood plasma. Biochem. J. 242 (1987) 55-59
36. Mirossay A., Jun S., and Dory L. Cloning and characterization of two alleles of the murine extracellular superoxide dismutase gene. Biochem. Biophys. Res. Commun. 352 (2007) 739-743
37. Folz R.J., and Gordon J.I. Computer-assisted predictions of signal peptidase processing sites. Biochem. Biophys. Res. Commun. 146 (1987) 870-877
38. Fukai T., Galis Z.S., Meng X.P., Parthasarathy S., and Harrison D.G. Vascular expression of extracellular superoxide dismutase in atherosclerosis. J. Clin. Invest. 101 (1998) 2101-2111
39. Ganguly K., Stoeger T., Wesselkamper S.C., Reinhard C., Sartor M.A., Medvedovic M., Tomlinson C.R., Bolle I., Mason J.M., Leikauf G.D., and Schulz H. Candidate genes controlling pulmonary function in mice: transcript profiling and predicted protein structure. Physiol. Genomics 31 (2007) 410-421
40. Ganguly K., and Schulz H. Association studies of lung function in mice. Dtsch. Tierarztl. Wochenschr. 115 (2008) 276-284