메뉴 건너뛰기




Volumn 44, Issue 5, 1998, Pages 763-770

Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; FREE RADICAL; OXYGEN RADICAL;

EID: 0031768025     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.410440510     Document Type: Article
Times cited : (134)

References (33)
  • 1
    • 0026099960 scopus 로고
    • Motor neuron disease (amyotrophic lateral sclerosis)
    • Williams DB, Windebank AJ. Motor neuron disease (amyotrophic lateral sclerosis). Mayo Clin Proc 1991;66:54-82
    • (1991) Mayo Clin Proc , vol.66 , pp. 54-82
    • Williams, D.B.1    Windebank, A.J.2
  • 2
    • 0027401203 scopus 로고
    • Mutations in CuZn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR, Siddique T, Patterson D, et al. Mutations in CuZn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993;362:59-62
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 3
    • 0027426169 scopus 로고
    • Amyotrophic lateral sclerosis and structural defects in CuZn superoxide dismutase
    • Deng H-X, Hentati A, Tainer JA, et al. Amyotrophic lateral sclerosis and structural defects in CuZn superoxide dismutase. Science 1993;362:1047-1051
    • (1993) Science , vol.362 , pp. 1047-1051
    • Deng, H.-X.1    Hentati, A.2    Tainer, J.A.3
  • 4
    • 0027965073 scopus 로고
    • Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
    • Borchelt DR, Lee MK, Slunt HS, et al. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc Natl Acad Sci USA 1994;91: 8292-8296
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8292-8296
    • Borchelt, D.R.1    Lee, M.K.2    Slunt, H.S.3
  • 6
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human CuZn superoxide dismutase mutation
    • Gurney ME, Pu H, Chiu AY, et al. Motor neuron degeneration in mice that express a human CuZn superoxide dismutase mutation. Science 1994;264:1772-1775
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1    Pu, H.2    Chiu, A.Y.3
  • 7
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration og mitochondria
    • Wong PC, Pardo CA, Borchelt DR, et al. An adverse property of a familial ALS linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration og mitochondria. Neuron 1995;14:1105-1116
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3
  • 8
    • 0030916609 scopus 로고    scopus 로고
    • A low expressor line of transgenic mice carrying a mutant human CuZn superoxide dismutase (SOD1) gene develops pathological changes which most closely resemble those in human ALS
    • Dal Canto MC, Gurney ME. A low expressor line of transgenic mice carrying a mutant human CuZn superoxide dismutase (SOD1) gene develops pathological changes which most closely resemble those in human ALS. Acta Neuropathol 1997;93:537-550
    • (1997) Acta Neuropathol , vol.93 , pp. 537-550
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 9
    • 0030927253 scopus 로고    scopus 로고
    • Transgenic animal models of familial amyotrophic lateral sclerosis
    • Gurney ME. Transgenic animal models of familial amyotrophic lateral sclerosis. J Neurol 1997;244(Suppl 2):S15-S20
    • (1997) J Neurol , vol.244 , Issue.2 SUPPL.
    • Gurney, M.E.1
  • 10
    • 0029671220 scopus 로고    scopus 로고
    • Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis
    • Wiedau Pazos M, Goto JJ, Rabizadeh S, et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 1996;271:515-518
    • (1996) Science , vol.271 , pp. 515-518
    • Wiedau Pazos, M.1    Goto, J.J.2    Rabizadeh, S.3
  • 12
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Hodgson EK, Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 1975;14:5294-5299
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 13
    • 0025285382 scopus 로고
    • Copper zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • Yim MB, Chock PB, Stadtman ER. Copper zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc Natl Acad Sci USA 1990;87:5006-5010
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5006-5010
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 14
    • 0027456505 scopus 로고
    • Enzyme function of copper zinc superoxide dismutase as a free radical generator
    • Yim MB, Chock PB, Stadtman ER. Enzyme function of copper zinc superoxide dismutase as a free radical generator. J Biol Chem 1993;268:4099-4105
    • (1993) J Biol Chem , vol.268 , pp. 4099-4105
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 15
    • 16044366720 scopus 로고    scopus 로고
    • Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein
    • Lyons TJ, Liu H, Goto JJ, et al. Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein. Proc Natl Acad Sci USA 1996;93:12240-12244
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12240-12244
    • Lyons, T.J.1    Liu, H.2    Goto, J.J.3
  • 16
    • 0030020575 scopus 로고    scopus 로고
    • Highly sensitive colorimetric detection and facile isolation of diamagnetic free radical adducts of novel chromotropic nitrone spin trapping agents readily derived from guaiazulene
    • Becker DA. Highly sensitive colorimetric detection and facile isolation of diamagnetic free radical adducts of novel chromotropic nitrone spin trapping agents readily derived from guaiazulene. J Am Chem Soc 1996;118:905-906
    • (1996) J Am Chem Soc , vol.118 , pp. 905-906
    • Becker, D.A.1
  • 17
    • 0032521118 scopus 로고    scopus 로고
    • Azulenyl nitrones: Colorimetric detection of oxyradical end products and neuroprotection in the gerbil forebrain ischemia/reperfusion model
    • Althaus JS, Fleck TJ, Becker DA, et al. Azulenyl nitrones: colorimetric detection of oxyradical end products and neuroprotection in the gerbil forebrain ischemia/reperfusion model. Free Radic Biol Med 1998;24:738-744
    • (1998) Free Radic Biol Med , vol.24 , pp. 738-744
    • Althaus, J.S.1    Fleck, T.J.2    Becker, D.A.3
  • 18
    • 0029096114 scopus 로고
    • Age dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Chiu AY, Zhai P, Dal Canto MC, et al. Age dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis. Mol Cell Neurosci 1995;6:349-362
    • (1995) Mol Cell Neurosci , vol.6 , pp. 349-362
    • Chiu, A.Y.1    Zhai, P.2    Dal Canto, M.C.3
  • 19
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 1971;44:276-287
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 20
    • 0002827274 scopus 로고
    • Improvements in the salicylate trapping method for measurement of hydroxyl radical levels in the brain
    • Ohnishi ST, Ohnishi T, ed. Boca Raton, FL: CRC Press
    • Althaus JS, Andrus PK, Hall ED, et al. Improvements in the salicylate trapping method for measurement of hydroxyl radical levels in the brain. In: Ohnishi ST, Ohnishi T, ed. Central nervous system trauma: research techniques. Boca Raton, FL: CRC Press, 1995:437-444
    • (1995) Central Nervous System Trauma: Research Techniques , pp. 437-444
    • Althaus, J.S.1    Andrus, P.K.2    Hall, E.D.3
  • 21
    • 0027997236 scopus 로고
    • Analysis of the functional effects of a mutation in SOD1 associated with familial amyotrophic lateral sclerosis
    • Tsuda T, Munthasser S, Fraser PE, et al. Analysis of the functional effects of a mutation in SOD1 associated with familial amyotrophic lateral sclerosis. Neuron 1994;13:727-736
    • (1994) Neuron , vol.13 , pp. 727-736
    • Tsuda, T.1    Munthasser, S.2    Fraser, P.E.3
  • 22
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Brujin LI, Becher MW, Lee MK, et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997;18:327-338
    • (1997) Neuron , vol.18 , pp. 327-338
    • Brujin, L.I.1    Becher, M.W.2    Lee, M.K.3
  • 23
    • 0017087427 scopus 로고
    • Superoxide dismutase in the rat and mouse as a function of age and longevity
    • Kellogg EW, Fridovich I. Superoxide dismutase in the rat and mouse as a function of age and longevity. J Gerontol 1976;31: 405-408
    • (1976) J Gerontol , vol.31 , pp. 405-408
    • Kellogg, E.W.1    Fridovich, I.2
  • 24
    • 0026514680 scopus 로고
    • Cu/Zn superoxide dismutase mRNA and enzyme activity, and susceptibility to lipid peroxidation, increases with aging in murine brains
    • De Haan JB, Newman JD, Kola I. Cu/Zn superoxide dismutase mRNA and enzyme activity, and susceptibility to lipid peroxidation, increases with aging in murine brains. Mol Brain Res 1992;13:179-187
    • (1992) Mol Brain Res , vol.13 , pp. 179-187
    • De Haan, J.B.1    Newman, J.D.2    Kola, I.3
  • 25
    • 0027946294 scopus 로고
    • The development of CNS pathology in a murine transgenic model of human ALS
    • Dal Canto MC, Gurney ME. The development of CNS pathology in a murine transgenic model of human ALS. Am J Pathol 1994;145:1271-1279
    • (1994) Am J Pathol , vol.145 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 26
    • 0028933344 scopus 로고
    • Neuropathological changes in two lines of mice carrying a transgene for mutant human CuZn SOD and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)
    • Dal Canto MC, Gurney ME. Neuropathological changes in two lines of mice carrying a transgene for mutant human CuZn SOD and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS). Brain Res 1995;676:25-40
    • (1995) Brain Res , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 27
    • 0030887622 scopus 로고    scopus 로고
    • Midbrain dopaminergic neuronal degeneration in a transgenic model of familial amyotrophic lateral sclerosis
    • Kostic V, Gurney ME, Deng H-X, et al. Midbrain dopaminergic neuronal degeneration in a transgenic model of familial amyotrophic lateral sclerosis. Ann Neurol 1997;41:497-504
    • (1997) Ann Neurol , vol.41 , pp. 497-504
    • Kostic, V.1    Gurney, M.E.2    Deng, H.-X.3
  • 28
    • 0030862630 scopus 로고    scopus 로고
    • The copper chelator d-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Hottinger AF, Fine EG, Gurney ME, et al. The copper chelator d-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis. Eur J Neurosci 1997;9:1548-1551
    • (1997) Eur J Neurosci , vol.9 , pp. 1548-1551
    • Hottinger, A.F.1    Fine, E.G.2    Gurney, M.E.3
  • 29
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin e riluzole and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • Gurney ME, Cutting FB, Zhai P, et al. Benefit of vitamin E riluzole and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann Neurol 1996;39:147-157
    • (1996) Ann Neurol , vol.39 , pp. 147-157
    • Gurney, M.E.1    Cutting, F.B.2    Zhai, P.3
  • 30
    • 0001897915 scopus 로고    scopus 로고
    • Carboxyfullerenes as neuroprotective reagents
    • Dugan LL, Turetsky DM, Du C, et al. Carboxyfullerenes as neuroprotective reagents. Proc Natl Acad Sci USA 1997;94: 9434-9439
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9434-9439
    • Dugan, L.L.1    Turetsky, D.M.2    Du, C.3
  • 31
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic model of familial amyotrophic lateral sclerosis
    • Kostic V, Jackson-Lewis V, de Bilbao F, et al. Bcl-2: prolonging life in a transgenic model of familial amyotrophic lateral sclerosis. Science 1997;277:559-562
    • (1997) Science , vol.277 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3
  • 32
    • 0027717968 scopus 로고
    • Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species
    • Kane DJ, Sarafian TA, Anton R, et al. Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species. Science 1993;262:1274-1277
    • (1993) Science , vol.262 , pp. 1274-1277
    • Kane, D.J.1    Sarafian, T.A.2    Anton, R.3
  • 33
    • 0027485461 scopus 로고
    • Bcl-2 functions in an antioxidant pathway to prevent apoptosis
    • Hockenbery DM, Oltvai ZN, Yin XM, et al. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell 1993;75: 241-251
    • (1993) Cell , vol.75 , pp. 241-251
    • Hockenbery, D.M.1    Oltvai, Z.N.2    Yin, X.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.