Effects of transfection with the Cu, Zn-superoxide dismutase gene on Xanthine/xanthine oxidase-induced cytotoxicity in fibroblasts from rat skin

Pharmaceutical Research

Volumn 13, Issue 4, 1996, Pages 577-582

  Nishiguchi, Kohshi ^a   Ishida, Kazue ^b   Nakajima, Masanori ^a   Maeda, Tetsuo ^a   Komada, Fusao ^a   Iwakawa, Seigo ^b   Tanigawara, Yusuke ^a   Okumura, Katsuhiko ^a  

^a KOBE UNIVERSITY   (Japan)

^b KOBE PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Catalase; Gene therapy; Human Cu; Oxidative stress; Zn SOD

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; XANTHINE; XANTHINE OXIDASE;

ANIMAL CELL; ARTICLE; CYTOTOXICITY; GENE EXPRESSION; GENE THERAPY; GENETIC TRANSFECTION; IMMUNOBLOTTING; LIPID PEROXIDATION; MALE; NONHUMAN; OXIDATIVE STRESS; PLASMID; PRIORITY JOURNAL; RAT; SKIN FIBROBLAST;

ANALYSIS OF VARIANCE; ANIMALS; AVIAN SARCOMA VIRUSES; BASE SEQUENCE; DNA, COMPLEMENTARY; ELECTROPHORESIS, AGAR GEL; FIBROBLASTS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE THERAPY; HUMANS; MOLECULAR SEQUENCE DATA; OXIDATIVE STRESS; PLASMIDS; POLYMERASE CHAIN REACTION; PROMOTER REGIONS (GENETICS); RATS; SKIN; SUPEROXIDE DISMUTASE; THIOBARBITURIC ACID REACTIVE SUBSTANCES; TRANSFECTION; XANTHINE; XANTHINE OXIDASE; XANTHINES;

EID: 0029981871     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1016050205854     Document Type: Article

References (22)

1. C. E. Cross, B. Halliwell, E. T. Borish, W. A. Pryor, B. N. Ames, R. L. Saul, J. M. McCord, and D. Massaro. Oxygen radicals and human disease. Ann. Intern. Med. 107:526-545 (1987).
2. C. G. Cochrane, R. Spragg, and S. D. Revak. Pathogenesis of the adult respiratory distress syndrome. Evidence of oxidant activity in bronchoalveolar lavage fluid. J. Clin. Invest. 71:754-761 (1983).
3. I. Fridovich. Superoxide dismutase. J. Biol. Chem. 264:7761-7764 (1989).
4. H. Hiraishi, A. Terano, T. Sugimoto, T. Harada, M. Razandi, and K. J. Ivey. Protective role of intracellular superoxide dismutase against extracellular oxidants in cultured rat gastric cells. J. Clin. Invest. 93:331-338 (1994).
5. B. A. Markey, S. H. Phan, J. Varani, U. S. Ryan, and P. A. Ward. Inhibition of cytotoxicity by intracellular superoxide dismutase supplementation. Free Radicals Biol. Med. 9:307-314 (1990).
6. Y. Kiyohara, K. Nishiguchi, F. Komada, S. Iwakawa, M. Hirai, and K. Okumura. Cytoprotective effects of epidermal growth factor (EGF) ointment containing protease inhibitor, nafamostat, on tissue damage at burn sites in rats. Biol. Pharm. Bull. 16:1146-1149 (1993).
7. K. Nishiguchi, Y. Kiyohara, F. Komada, S. Iwakawa, and K. Okumura. Effect of epidermal growth factor on Cu, Zn-superoxide dismutase expression in cultured fibroblasts from rat skin. Pharm. Res. 11:1244-1249 (1994).
8. T. Ogino, M. Inoue, Y. Ando, A. Awai, H. Maeda, and Y. Morino. Chemical modification of superoxide dismutase: Extension of plasma half life of the enzyme through its reversible binding to the circulating albumin. Int. J. Pept. Protein Res. 32:153-159 (1988).
9. P. S. Pyatak, A. Abuchowski, and F. F. Davis. Preparation of a polyethylene glycol: superoxide dismutase adduct, and an examination of its blood circulation life and anti-inflammatory activity. Res. Commun. Chem. Pathol. Pharmacol. 29:113-127 (1980).
10. C. H. Evans, and P. D. Robbins. Gene therapy for Arthritis. In J. A. Wolff (eds.), Gene Therapeutics: Methods and Applications of Direct Gene Transfer, Birkhäuser, Boston, 1994, pp. 320-343.
11. P. L. Feigner, T. R. Gadek, M. Holm, R. Roman, H. W. Chan, M. Wenz, J. P. Northrop, G. M. Ringold, and M. Danielsen. Lipofection: A highly efficient, lipid-mediated DNA-transfection procedure. Proc. Natl. Acad. Sci. USA 84:7413-7417 (1987).
12. I. Fridovich. Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J. Biol. Chem. 245:4053-4057 (1970).
13. K. Yagi. A simple fluorometric assay for lipoperoxide in blood plasma. Biochem. Med. 15:212-216 (1976).
14. I. S. Ayene, C. Dodia, and A. B. Fisher. Role of oxygen in oxidation of lipid and protein during ischemia/reperfusion in isolated perfused rat lung. Arch. Biochem. Biophys. 296:183-189 (1992).
15. K. Okumura, Y. Kiyohara, F. Komada, S. Iwakawa, M. Hirai, and T. Fuwa. Improvement in wound healing by epidermal growth factor (EGF) ointment I. Effect of nafamostat, gabexate, or gelatin on stabilization and efficacy of EGF. Pharm. Res. 7:1289-1293 (1990).
16. Y. Kiyohara, F. Komada, S. Iwakawa, M. Hirai, T. Fuwa, and K. Okumura. Improvement in wound healing by epidermal growth factor (EGF) ointment II: Effect of protease inhibitor, nafamostat, on stabilization and efficacy of EGF in burn. J. Pharmacobio-Dyn. 14:47-52 (1991).
17. R. H. Simon, C. H. Scoggin, and D. Patterson. Hydrogen peroxide causes the fatal injury to human fibroblasts exposed to oxygen radicals. J. Biol. Chem. 256:7181-7186 (1981).
18. P. Amstad, A. Peskin, G. Shah, M. E. Mirault, R. Moret, I. Zbinden, and P. Cerutti. The balance between Cu, Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress. Biochemistry 30:9305-9313 (1991).
19. M. J. Goebel, N. Rudolph, and S. L. Wong. Developmental patterns of antioxidant defense mechanisms in human erythrocytes. Pediatr. Res. 26:366-369 (1989).
20. M. J. Speranza, A. C. Bagley, and R. E. Lynch. Cells enriched for catalase are sensitized to the toxicities of bleomycin, adriamycin, and paraquat. J. Biol. Chem. 268:19039-19043 (1993).
21. B. Halliwell, and J. M. C. Gutteridge. The importance of free radicals and catalytic metal ions in human diseases. Mol. Aspects Med. 8:89-193 (1985).
22. D. R. Rosen, T. Siddique, D. Patterson, D. A. Figlewicz, P. Sapp, A. Hentati, D. Donaldson, J. Goto, J. P. O'Regan, H.-X. Deng, Z. Rahmani, A. Krizus, D. Mck.-Yasek, A. Cayabyab, S. M. Gaston, R. Berger, R. E. Tanzi, J. J. Halperin, B. Herzfeldt, R. V. B. Bergh, W.-Y. Hung, T. Bird, G. Deng, D. W. Mulder, C. Smyth, N. G. Laing, E. Soriano, M. A. Pericak-Vance, J. Haines, G. A. Rouleau, J. S. Gusella, H. R. Horvitz and R. H. Brown, Jr. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59-62 (1993).