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Volumn 29, Issue 3, 2004, Pages 561-567

Role of Oxidative Damage in Friedreich's Ataxia

Author keywords

Fibroblasts; Free radicals; Friedreich's ataxia; Malondialdehyde

Indexed keywords

ACONITATE HYDRATASE; FERROUS CHLORIDE; FRATAXIN; FREE RADICAL; GLUTATHIONE; HYDROGEN PEROXIDE; MALONALDEHYDE; OXYGEN RADICAL; PARAQUAT;

EID: 1542287925     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:NERE.0000014826.00881.c3     Document Type: Article
Times cited : (63)

References (31)
  • 5
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova, H., Campuzano, V., Foury, F., Dollé, P., Cazzalini, O., and Koenig, M. 1997. Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet. 16:345-351.
    • (1997) Nat. Genet. , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dollé, P.4    Cazzalini, O.5    Koenig, M.6
  • 8
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich's ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., and Koenig, M. 2001. Mouse models for Friedreich's ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 27: 181-186.
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossée, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 9
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini, P., O'Neill, H. A., Benada, O., and Isaya, G. 2002. Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum. Mol. Genet. 11:217-227.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 10
    • 0036799372 scopus 로고    scopus 로고
    • A non-essential function for yeast frataxin in iron-sulfur cluster assembly
    • Duby, G., Foury, F., Ramazzotti, A., Hermann, J., and Lutz, T. 2002. A non-essential function for yeast frataxin in iron-sulfur cluster assembly. Hum. Mol. Genet. 11:2635-2643.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2635-2643
    • Duby, G.1    Foury, F.2    Ramazzotti, A.3    Hermann, J.4    Lutz, T.5
  • 12
    • 0034642214 scopus 로고    scopus 로고
    • Increased levels of plasma malondialdehyde in Friedreich's ataxia
    • Emond, M., Lepage, G., Vanasse, M., and Pandolfo, M. 2000. Increased levels of plasma malondialdehyde in Friedreich's ataxia. Neurology 55:1752-1753.
    • (2000) Neurology , vol.55 , pp. 1752-1753
    • Emond, M.1    Lepage, G.2    Vanasse, M.3    Pandolfo, M.4
  • 13
    • 0027300736 scopus 로고
    • Lipid peroxidation: Its mechanism, measurement, and significance
    • Halliwell, B. and Chirico, S. 1993. Lipid peroxidation: Its mechanism, measurement, and significance. Am. J. Clin. Nutr. 57(Suppl): 715S-25S.
    • (1993) Am. J. Clin. Nutr. , vol.57 , Issue.SUPPL.
    • Halliwell, B.1    Chirico, S.2
  • 14
    • 0019782799 scopus 로고
    • Friedreich's ataxia: A clinical and genetic study of 90 families with an analysis of early diagnosis criteria and intrafamilial clustering of clinical features
    • Harding, A. E. 1981. Friedreich's ataxia: A clinical and genetic study of 90 families with an analysis of early diagnosis criteria and intrafamilial clustering of clinical features. Brain 104:589-620.
    • (1981) Brain , vol.104 , pp. 589-620
    • Harding, A.E.1
  • 16
    • 0002886691 scopus 로고
    • Kruse, P. F. Jr and Patterson, M. K. Jr. (eds.) Academic Press, New York
    • Martin, G. M. 1973. Pages 39-43, in Kruse, P. F. Jr and Patterson, M. K. Jr. (eds.), Tissue Culture Methods and Applications Academic Press, New York.
    • (1973) Tissue Culture Methods and Applications , pp. 39-43
    • Martin, G.M.1
  • 17
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and rat lungs
    • Gardner, P. R., Nguyen, D. D. H., and White, C. W. 1994. Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and rat lungs. Proc. Natl. Acad. Sci. USA 91:12248-12252.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.D.H.2    White, C.W.3
  • 18
  • 21
    • 0031437930 scopus 로고    scopus 로고
    • Oxidative stress does not appear to be involved in the aetiology of Friedreich's ataxia
    • MacEvilly, C. J. and Muller, D. P. R. 1997. Oxidative stress does not appear to be involved in the aetiology of Friedreich's ataxia. Res. Neurol. Neurosci. 11:131-137.
    • (1997) Res. Neurol. Neurosci. , vol.11 , pp. 131-137
    • MacEvilly, C.J.1    Muller, D.P.R.2
  • 22
    • 0024997609 scopus 로고
    • 1-Methyl-4-phenylpyridinium (MPP+) induces NADH-dependent superoxide formation and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles
    • Hasegawa, E., Takeshige, K., Oishi, T., Murai, Y., and Minakami, S. 1990. 1-Methyl-4-phenylpyridinium (MPP+) induces NADH-dependent superoxide formation and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles. Biochem. Biophys. Res. Commun. 170:1049-1055.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1049-1055
    • Hasegawa, E.1    Takeshige, K.2    Oishi, T.3    Murai, Y.4    Minakami, S.5
  • 23
    • 0035906334 scopus 로고    scopus 로고
    • Iron and its sensitive balance in the cell
    • De Freitas, J. M. and Meneghini, R. 2001. Iron and its sensitive balance in the cell. Mutation Res. 475:153-159.
    • (2001) Mutation Res. , vol.475 , pp. 153-159
    • De Freitas, J.M.1    Meneghini, R.2
  • 24
    • 0035976855 scopus 로고    scopus 로고
    • Manganese superoxide dismutase induction by iron is impaired in Friedreich's ataxia cells
    • Jiralerspong, S., Ge, B., Hudson, T. J., and Pandolfo, M. 2001. Manganese superoxide dismutase induction by iron is impaired in Friedreich's ataxia cells. FEBS Lett. 509:101-105.
    • (2001) FEBS Lett. , vol.509 , pp. 101-105
    • Jiralerspong, S.1    Ge, B.2    Hudson, T.J.3    Pandolfo, M.4
  • 26
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury, F. and Cazzalini, O. 1997. Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett. 411:373-377.
    • (1997) FEBS Lett. , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 27
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A., Yang, J., Cavadini, P., Gellera, C., Lonnerdal, B., Taroni, F., and Cortopassi, G. 1999. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8:425-430.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 28
    • 0032030445 scopus 로고    scopus 로고
    • Mitochondrial NADH-quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers
    • Shimada, H., Hirai, K., Simamura, E., and Pan, J. 1998. Mitochondrial NADH-quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers. Arch. Biochem. Biophys. 351:75-81.
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 75-81
    • Shimada, H.1    Hirai, K.2    Simamura, E.3    Pan, J.4
  • 29
    • 0026577788 scopus 로고
    • Paraquat damage of rat liver mitochondria by superoxide production depends on extramitochondrial NADH
    • Hirai, K., Ikeda, K., and Wang, G. Y. 1992. Paraquat damage of rat liver mitochondria by superoxide production depends on extramitochondrial NADH. Toxicology 72:1-16.
    • (1992) Toxicology , vol.72 , pp. 1-16
    • Hirai, K.1    Ikeda, K.2    Wang, G.Y.3
  • 30
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitase, but nitric oxide does not
    • Hausalden, A. and Fridovich, I. 1994. Superoxide and peroxynitrite inactivate aconitase, but nitric oxide does not. J. Biol. Chem. 269:29405-29408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausalden, A.1    Fridovich, I.2


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