Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase

Nature Genetics

Volumn 11, Issue 4, 1995, Pages 376-381

  Li, Yibing ^a   Huang, Ting Ting ^a   Carlson, Elaine J ^a   Melov, Simon ^b   Ursell, Philip C ^a   Olson, Jean L ^a   Noble, Linda J ^a   Yoshimura, Midori P ^a   Berger, Christoph ^a,c   Chan, Pak H ^a   Wallace, Douglas C ^b   Epstein, Charles J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c CHILDREN'S MEDICAL RESEARCH INSTITUTE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

MANGANESE; SUPEROXIDE DISMUTASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONGESTIVE CARDIOMYOPATHY; CONTROLLED STUDY; CYTOCHEMISTRY; ENZYME ACTIVITY; ENZYME INACTIVATION; GENETIC RECOMBINATION; LETHALITY; METABOLIC ACIDOSIS; MOUSE; NEWBORN MORTALITY; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL; SKELETAL MUSCLE; TISSUE INJURY;

ACIDOSIS; ANIMAL; ANIMALS, NEWBORN; BASE SEQUENCE; CARDIOMYOPATHY, CONGESTIVE; CYTOCHROME-C OXIDASE; GENE TARGETING; GENES, LETHAL; HOMOZYGOTE; LIPID PEROXIDATION; LIPIDS; LIVER; MICE; MICE, MUTANT STRAINS; MITOCHONDRIA, HEART; MITOCHONDRIA, MUSCLE; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; SEQUENCE DELETION; SUCCINATE DEHYDROGENASE; SUPEROXIDE DISMUTASE; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0028827252     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1295-376     Document Type: Article

References (31)

1. Chan, RH. Oxygen radicals in focaJ cerebral ischemia. Brain Pathol. 4, 59-65(1994).
2. Kinouchi, H. et al. Attenuation of focal cerebral ischemic injury in transgenic mice overexpressing CuZn superoxide dismutase. Proc. natn. Acad. Sci. U. S. A. 88, 11158-11162 (1991).
3. Euler, D. E. Role of oxygen-derived free radicals in canine reperfusion arrhythmia. Am. J. Physiol. 268, H295-H300(1995).
4. Samaja, M., Motterlini, R., Santoro, F., Dell' Antonio, G. & Corno, A. Oxidative injury in reoxygenated and reperfused hearts. Free Rad. Biol. Med. 16, 255-262 (1994).
5. Jenner, R Oxidative damage in neurodegenerative disease. Lancet 344, 796-798(1994).
6. Fahn, S. & Cohen, G. The oxidant stress hypothesis in Parkinson's disease: evidence supporting it. Am. Neurol. 32, 804-812 (1992).
7. Laforv-Cazal, M., Pietri, S., Culcasi, M. & Bockaert, J. NMDA-dependent superoxide production and neurotoxicity. Nature 364, 535-537 (1993).
8. Davis, J. M., Rosenfeld, W. N., Sanders, R. J. & Gonenne, A. Prophylactic effects of recombinant human superoxide dismutase in neonatal lung injury. J. appl. Physiol. 74, 2234-2241 (1993).
9. Halliwell, B. Tìie role of oxygen radicals in human disease, with particular reference to the vascular system. Homeostasis Suppl 1, 118-126 (1993).
10. Orr, W. C. & Sohal, R. S. Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263, 1128-1130 (1994).
11. Ku, H. H., Brunk, U. T. & Sohal, R. S. Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species. Free Rad. Biol. Med. 15, 621-627 (1993).
12. Harris, C A et al. Manganese superoxide dismutase is induced by IFN-'y in multiple cell types. Synergistic induction by IFN-γ and tumor necrosis factor or IL-1. J. Immunol. 147, 149-154 (1991).
13. Sato, M., Sasaki, M. & Hojo, H. Antioxidative roles of metaílothíonein and manganese superoxide dismutase induced by tumor necrosis factor-alpha and interleukin-6. Arch. Bioch. Biophy. 316, 738-744(1995).
14. Akashi, M. et al. Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts. Possible mechanisms for its accumulation. J. bioi. Chem. 270, 15864-15869 (1995).
15. Church, S. L. et al. Increased manganese superoxide dismutase expression suppresses the malignant phenotype of human melanoma cells. Proc. natn. Acad. Sci. U. S. A 90, 3113-3117 (1993).
16. St. Clair, O. K., Oberiey, T. D., Muse, K. E. & St. Clair, W. H. Expression of manganese superoxide dismutase promotes cellular differentiation. Free Rad. Biol. Med. 16, 275-282 (1994).
17. Bourgeron, T. et al. Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nature Genet. 11, 144-149(1995).
18. Müller-Höcker, J. et al. Fatal infantile mitochondrial cardiomyopathy and myopathy with heterogeneous tissue expression of combined respiratory chain deficiencies. Virchows Archiv. A Pathol. Anat. Histopathol. 419, 355-362(1991).
19. Zheng, X. et al. Evidence in a lethal infantile mitochondrial disease for a nuclear mutation affecting respiratory complexes I and IV. Neurology 39, 1203-1209(1989).
20. Reichmann, H. & Angeini, C. Single muscle fibre analyses in 2 brothers with succinate dehydrogenase deficiency. Eur. Neurol. 34, 95-98 (1994).
21. Underholm, H., Essen-Gustavsson, B. & Thornell, L. E. Low succinate dehydrogenase (SDH) activity in a patient with a hereditary myopathy with paroxysmal myoglobinuria. J. int. Med. 228, 43-52 (1990).
22. Hall, R. E., Henriksson, K. G., Lewis, S. F., Haller, R. G. & Kennaway, N. G. Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins. J. din. Invest. 92, 2660-2666(1993).
23. Zhang, Y, Marcillat, O., Giulivi, C., Ernster, L & Davies, K. J. The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J. bioi Chem. 265, 16330-16336 (1990).
24. Gardner, P. R., Nguyen, D. D. & White, C. W. Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc. natn. Acad. Sd. U. S. A 91, 12248-12252 (1994).
25. Gardner, P. R., Raineri, I., Epstein, LB. & White, C. W. Superoxide radical and iron modulate aconitase activity in mammalian cells. J. bioi. Chem. 270, 13399-13405(1995).
26. Chen, Y., Saari, J. T. & Kang, Y. J. Weak antioxidant defenses make the heart a target for damage in copper-deficient rats. Free Rad. Biol. Med. 17, 529-536 (1994).
27. Chen, S & Evans, G. A. Use of polymerase chain reaction for screening transgenic mice, in PCR Protocols Current Methods and Applications, Methods in Molecular Biology Vol. 15 (ed White, B. A.) 75-80 (Humana Press, Totowa, New Jersey 1993).
28. de Rosa, G., Duncan, D. S., Keen, C. L. & Hurley, L. S. Evaluation of negative staining technique for determination of CN-Insensitive superoxide dismutase activity. Bioch. biophy. Acte 566, 32-39 (1979).
29. Fridovich, I. Measuring the activity of superoxide dismutase: an embarrassment of riches. In Superoxide Dismutase 1 (ed. Oberiey, C. W.) 69-77 (CRC Press, Boca Raton 1982).
30. Rifai, Z., Welle, S., Kamp, C. & Thornton, C. A. Ragged red fibers in normal aging and inflammatory myopathy. Ann. Neurol. 37, 24-29 (1995).
31. Borgstahl, G. E et al. The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 71, 107-118 (1992).