Induction of phenotypes resembling CuZn-superoxide dismutase deletion in wild-type yeast cells: An in vivo assay for the role of superoxide in the toxicity of redox-cycling compounds

Chemical Research in Toxicology

Volumn 18, Issue 8, 2005, Pages 1279-1286

  Wallace, Matthew Alan ^a   Bailey, Sasaneh ^a   Fukuto, Jon M ^a   Valentine, Joan Selverstone ^a   Gralla, Edith Butler ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; ACONITATE HYDRATASE; BIPYRIDINE DERIVATIVE; COPPER ZINC SUPEROXIDE DISMUTASE; DIQUAT; HERBICIDE; MENADIONE; PARAQUAT; PLUMBAGIN; SUPEROXIDE; VIOLOGEN;

ANIMAL CELL; ARTICLE; CONCENTRATION RESPONSE; ENZYME ACTIVITY; GENE INDUCTION; GROWTH INHIBITION; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PARKINSONISM; PHENOTYPE; SACCHAROMYCES CEREVISIAE; STRAIN DIFFERENCE; TOXICITY TESTING; YEAST CELL;

1-METHYL-4-PHENYLPYRIDINIUM; 2,2'-DIPYRIDYL; ACONITATE HYDRATASE; ENZYME INHIBITORS; GENE DELETION; MUTAGENS; OXIDATION-REDUCTION; OXYGEN; PHENOTYPE; QUINONES; SACCHAROMYCES CEREVISIAE; SUPEROXIDE DISMUTASE; SUPEROXIDES; VITAMIN K 3;

SACCHAROMYCES CEREVISIAE;

EID: 23844457628     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx050050n     Document Type: Article

References (54)

1. Lyons, T. J., Gralla, E. B., and Valentine, J. S. (1999) Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis. In Metal Ions in Biological Systems (Sigel, A., and Sigel, H., Eds.) pp 125-177, Marcel Dekker, New York.
2. Wallace, M. A., Liou, L. L., Martins, J., Clement, M. H., Bailey, S., Longo, V. D., Valentine, J. S., and Gralla, E. B. (2004) Superoxide inhibits 4Fe-4S cluster enzymes involved in amino acid biosynthesis. Cross-compartment protection by CuZn-superoxide dismutase. J. Biol. Chem. 279, 32055-32062.
3. Srinivasan, C., Liba, A., Imlay, J. A., Valentine, J. S., and Gralla, E. B. (2000) Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance. J. Biol. Chem. 275, 29187-29192.
4. Gralla, E. B., and Valentine, J. S. (1991) Null mutants of Saccharomyces cerevisiae Cu, Zn superoxide dismutase: characterization and spontaneous mutation rates. J. Bacteriol. 173, 5918-5920.
5. Gralla, E. B., and Kosman, D. J. (1992) Molecular genetics of superoxide dismutases in yeasts and related fungi. Adv. Genet. 30, 251-319.
6. Gralla, E. B. (1997) Superoxide dismutase: Studies in the yeast Saccharomyces cerevisiae. In Cold Spring Harbor Monograph Series, 34. Oxidative Stress and the Molecular Biology of Antioxidant Defenses (Scandalios, J. G., Ed.) pp 495-525, Cold Spring Harbor Laboratory Press, Plainview, NY.
7. Wei, J. P., Srinivasan, C., Han, H., Valentine, J. S., and Gralla, E. B. (2001) Evidence for a novel role of copper-zinc superoxide dismutase in zinc metabolism. J. Biol. Chem. 276, 44798-44803.
8. Slekar, K. H., Kosman, D. J., and Culotta, V. C. (1996) The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J. Biol. Chem. 271, 28831-28836.
9. Halliwell, B., and Gutteridge, J. M. C. (1999) Free Radicals in Biology and Medicine, 3rd ed., Oxford University Press, Oxford.
10. Bolton, J. L., Trush, M. A., Penning, T. M., Dryhurst, G., and Monks, T. J. (2000) Role of quinones in toxicology. Chem. Res. Toxicol. 13, 135-160.
11. Hassan, H. M., and Fridovich, I. (1979) Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J. Biol. Chem. 254, 10846-10852.
12. Velazquez, I., and Pardo, J. P. (2001) Kinetic characterization of the rotenone-insensitive internal NADH: Ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Arch. Biochem. Biophys. 389, 7-14.
13. Fang, J., and Beattie, D. S. (2003) External alternative NADH dehydrogenase of Saccharomyces cerevisiae: A potential source of superoxide. Free Radical Biol. Med. 34, 478-488.
14. Hassan, H. M., and Fridovich, I. (1977) Regulation of the synthesis of superoxide dismutase in Escherichia coli. Induction by methyl viologen. J. Biol. Chem. 252, 7667-7672.
15. Hassan, H. M., and Fridovich, I. (1978) Superoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli. J. Biol. Chem. 253, 8143-8148.
16. Hassan, H. M., and Fridovich, I. (1979) Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds. Arch. Biochem. Biophys. 196, 385-395.
17. Kohen, R., and Chevion, M. (1985) Involvement of iron and copper in biological damage that is induced by oxygen free radicals. J. Free Radical Biol. Med. 1, 339-340.
18. Korbashi, P., Kohen, R., Katzhendler, J., and Chevion, M. (1986) Iron mediates paraquat toxicity in Escherichia coli. J. Biol. Chem. 261, 12472-12476.
19. Liochev, S. I., and Fridovich, I. (1993) Effects of paraquat on Escherichia coli: Sensitivity to small changes in pH of the medium-A cautionary note. Arch. Biochem. Biophys. 306, 518-520.
20. Minakami, H., Kitzler, J. W., and Fridovich, I. (1990) Effects of pH, glucose, and chelating agents on lethality of paraquat to Escherichia coli. J. Bacteriol. 172, 691-695.
21. Kitzler, J., and Fridovich, I. (1986) Effects of salts on the lethality of paraquat. J. Bacteriol. 167, 346-349.
22. Vicente, J. A., Peixoto, F., Lopes, M. L., and Madeira, V. M. (2001) Differential sensitivities of plant and animal mitochondria to the herbicide paraquat. J. Biochem. Mol. Toxicol. 15, 322-330.
23. Palmeira, C. M., Moreno, A. J., and Madeira, V. M. (1995) Mitochondrial bioenergetics is affected by the herbicide paraquat. Biochim. Biophys. Acta 1229, 187-192.
24. Blaszczynski, M., Litwinska, J., Zaborowska, D., and Bilinski, T. (1985) The role of respiratory chain in paraquat toxicity in yeast. Acta Microbiol. Pol. 34, 243-254.
25. Rodriguez, C. E., Shinyashiki, M., Froines, J., Yu, R. C., Fukuto, J. M., and Cho, A. K. (2004) An examination of quinone toxicity using the yeast Saccharomyces cerevisiae model system. Toxicology 201, 185-196.
26. Cadenas, E., Hochstein, P., and Ernster, L. (1992) Pro- and antioxidant functions of quinones and quinone reductases in mammalian cells. Adv. Enzymol. Relat. Areas Mol. Biol. 65, 97-146.
27. O'Brien, P. J. (1991) Molecular mechanisms of quinone cytotoxicity. Chem.-Biol. Interact. 80, 1-41.
28. Jamieson, D. J., Rivers, S. L., and Stephen, D. W. (1994) Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress. Microbiology 140 (Part 12), 3277-3283.
29. Chaput, M., Brygier, J., Lion, Y., and Sels, A. (1983) Potentiation of oxygen toxicity by menadione in Saccharomyces cerevisiae. Biochimie 65, 501-512.
30. Cyrne, L., Martins, L., Fernandes, L., and Marinho, H. S. (2003) Regulation of antioxidant enzymes gene expression in the yeast Saccharomyces cerevisiae during stationary phase. Free Radical Biol. Med. 34, 385-393.
31. Zadzinski, R., Fortuniak, A., Bilinski, T., Grey, M., and Bartosz, G. (1998) Menadione toxicity in Saccharomyces cerevisiae cells: Activation by conjugation with glutathione. Biochem. Mol. Biol. Int. 44, 747-759.
32. Mauzeroll, J., and Bard, A. J. (2004) Scanning electrochemical microscopy of menadione-glutathione conjugate export from yeast cells. Proc. Natl. Acad. Sci. U.S.A. 101, 7862-7867.
33. McAmis, W. C., Schaeffer, R. C., Jr., Baynes, J. W., and Wolf, M. B. (2003) Menadione causes endothelial barrier failure by a direct effect on intracellular thiols, independent of reactive oxidant production. Biochim. Biophys. Acta 1641, 43-53.
34. Rodriguez-Manzaneque, M. T., Tamarit, J., Belli, G., Ros, J., and Herrero, E. (2002) Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 13, 1109-1121.
35. Przedborski, S., and Jackson-Lewis, V. (1998) Mechanisms of MPTP toxicity. Mov. Disord. 13 (Suppl. 1), 35-38.
36. Mitsumoto, A., Nagano, T., and Hirobe, M. (1992) Toxicity of 1-methyl-4-phenylpyridinium derivatives in Escherichia coli. Arch. Biochem. Biophys. 296, 482-488.
37. Frank, D. M., Arora, P. K., Blumer, J. L., and Sayre, L. M. (1987) Model study on the bioreduction of paraquat, MPP+, and analogues. Evidence against a "redox cycling" mechanism in MPTP neurotoxicity. Biochem. Biophys. Res. Commun. 147, 1095-1104.
38. Przedborski, S., Kostic, V., Jackson-Lewis, V., Naini, A. B., Simonetti, S., Fahn, S., Carlson, E., Epstein, C. J., and Cadet, J. L. (1992) Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity. J. Neurosci. 12, 1658-1667.
39. Foster, S. B., Wrona, M. Z., Han, J., and Dryhurst, G. (2003) The parkinsonian neurotoxin 1-methyl-4-phenylpyridinium (MPP(+)) mediates release of 1-3,4-dihydroxyphenylalanine (1-DOPA) and inhibition of 1-DOPA decarboxylase in the rat striatum: a microdialysis study. Chem. Res. Toxicol. 16, 1372-1384.
40. Cassarino, D. S., Fall, C. P., Swerdlow, R. H., Smith, T. S., Halvorsen, E. M., Miller, S. W., Parks, J. P., Parker, W. D., Jr., and Bennett, J. P., Jr. (1997) Elevated reactive oxygen species and antioxidant enzyme activities in animal and cellular models of Parkinson's disease. Biochim. Biophys. Acta 1362, 77-86.
41. Shang, T., Kotamraju, S., Kalivendi, S. V., Hillard, C. J., and Kalyanaraman, B. (2004) 1-Methyl-4-phenylpyridinium-induced apoptosis in cerebellar granule neurons is mediated by transferrin receptor iron-dependent depletion of tetrahydrobiopterin and neuronal nitric-oxide synthase-derived superoxide. J. Biol. Chem. 279, 19099-19112.
42. Lambert, C. E., and Bondy, S. C. (1989) Effects of MPTP, MPP+ and paraquat on mitochondrial potential and oxidative stress. Life Sci. 44, 1277-1284.
43. Nakai, M., Mori, A., Watanabe, A., and Mitsumoto, Y. (2003) 1-methyl-4-phenylpyridinium (MPP+) decreases mitochondrial oxidation-reduction (REDOX) activity and membrane potential (Deltapsi(m)) in rat striatum. Exp. Neurol. 179, 103-110.
44. Nakamura, K., Bindokas, V. P., Marks, J. D., Wright, D. A., Frim, D. M., Miller, R. J., and Kang, U. J. (2000) The selective toxicity of 1-methyl-4-phenylpyridinium to dopaminergic neurons: The role of mitochondrial complex I and reactive oxygen species revisited. Mol. Pharmacol. 58, 271-278.
45. Fonck, C., and Baudry, M. (2001) Toxic effects of MPP(+) and MPTP in PC12 cells independent of reactive oxygen species formation. Brain Res. 905, 199-206.
46. Kaiser, C., Michaelis, S., and Mitchell, A., Eds. (1994) Methods in Yeast Genetics, Vol., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
47. McManus, D. C., and Josephy, P. D. (1993) A new approach to measurement of redox-cycling activity in Escherichia coli. Arch. Biochem. Biophys. 304, 367-370.
48. Gardner, P. R., Raineri, I., Epstein, L. B., and White, C. W. (1995) Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270, 13399-13405.
49. Jamieson, D. J. (1998) Oxidative stress responses of the yeast Saccharomyces cerevisiae. Yeast 14, 1511-1527.
50. Costa, V., and Moradas-Ferreira, P. (2001) Oxidative stress and signal transduction in Saccharomyces cerevisiae: Insights into aging, apoptosis and diseases. Mol. Aspects Med. 22, 217-246.
51. -.), superoxide dismutases, and related matters. J. Biol. Chem. 272, 18515-18517.
52. Beinert, H., Holm, R. H., and Munck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 277, 653-659.
53. Gonzalez-Polo, R. A., Soler, G., Rodriguezmartin, A., Moran, J. M., and Fuentes, J. M. (2004) Protection against MPP+ neurotoxicity in cerebellar granule cells by antioxidants. Cell Biol. Int. 28, 373-380.
54. Seyfried, J., Soldner, F., Kunz, W. S., Schulz, J. B., Klockgether, T., Kovar, K. A., and Wullner, U. (2000) Effect of 1-methyl-4-phenylpyridinium on glutathione in rat pheochromocytoma PC 12 cells. Neurochem. Int. 36, 489-497.