메뉴 건너뛰기




Volumn 33, Issue 1, 2000, Pages 65-73

Gain in functions of mutant Cu,Zn-superoxide dismutases as a causative factor in familial amyotrophic lateral sclerosis: Less reactive oxidant formation but high spontaneous aggregation and precipitation

Author keywords

Baculovirus; Copper toxicity; Gain of function; Hydroxyl radicals; Protein aggregation

Indexed keywords

COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; HYALIN; HYDROGEN PEROXIDE; HYDROXYL RADICAL; REACTIVE OXYGEN METABOLITE;

EID: 0034039381     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715760000300621     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • I. Fridovich (1995) Superoxide radical and superoxide dismutases. Annual Review of Biochemistry 64, 97-112.
    • (1995) Annual Review of Biochemistry , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 3
    • 0032908774 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: A putative mechanism of degeneration
    • B.M. Morrison and J.H. Morrison (1999) Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: a putative mechanism of degeneration. Brain Research Review 29, 121-135.
    • (1999) Brain Research Review , vol.29 , pp. 121-135
    • Morrison, B.M.1    Morrison, J.H.2
  • 5
    • 0028955472 scopus 로고
    • Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells
    • J. Fujii, T. Myint, H.G. Seo, Y. Kayanoki, Y. Ikeda and N. Taniguchi (1995) Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells. Journal of Neurochemistry 64, 1456-1461.
    • (1995) Journal of Neurochemistry , vol.64 , pp. 1456-1461
    • Fujii, J.1    Myint, T.2    Seo, H.G.3    Kayanoki, Y.4    Ikeda, Y.5    Taniguchi, N.6
  • 10
    • 0029939471 scopus 로고    scopus 로고
    • A gain-of function of an amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide
    • M.B. Yim, J.H. Kang, H.S. Yim, H.S. Kwak, P.B. Chock and E.R. Stadtman (1996) A gain-of function of an amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. Proceedings of the National Academy of Science of the USA 93, 5709-5714.
    • (1996) Proceedings of the National Academy of Science of the USA , vol.93 , pp. 5709-5714
    • Yim, M.B.1    Kang, J.H.2    Yim, H.S.3    Kwak, H.S.4    Chock, P.B.5    Stadtman, E.R.6
  • 11
    • 0030900245 scopus 로고    scopus 로고
    • A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value
    • H.S. Yim, J.H. Kang, P.B. Chock, E.R. Stadtman and M.B. Yim (1997) A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value. Journal of Biological Chemistry 272, 8861-8863.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 8861-8863
    • Yim, H.S.1    Kang, J.H.2    Chock, P.B.3    Stadtman, E.R.4    Yim, M.B.5
  • 12
    • 0032426850 scopus 로고    scopus 로고
    • The free radical-generating function of a familial amyotrophic lateral sclerosis-associated D90A Cu,Zn-superoxide dismutase mutant
    • S.M. Kim, W.S. Eum, O.B. Kwon and J.H. Kang (1998) The free radical-generating function of a familial amyotrophic lateral sclerosis-associated D90A Cu,Zn-superoxide dismutase mutant. Biochemical Molecular Biology International 46, 1191-1200.
    • (1998) Biochemical Molecular Biology International , vol.46 , pp. 1191-1200
    • Kim, S.M.1    Eum, W.S.2    Kwon, O.B.3    Kang, J.H.4
  • 13
    • 0032942541 scopus 로고    scopus 로고
    • Increased hydroxyl radical production and apoptosis in PC12 neuron cells expressing the gain-of-function mutant G93A SOD1 gene
    • R. Liu, R.K. Narla, I. Kurinov, B. Li and F.M. Uckun (1999) Increased hydroxyl radical production and apoptosis in PC12 neuron cells expressing the gain-of-function mutant G93A SOD1 gene. Radiation Research 151, 133-141.
    • (1999) Radiation Research , vol.151 , pp. 133-141
    • Liu, R.1    Narla, R.K.2    Kurinov, I.3    Li, B.4    Uckun, F.M.5
  • 14
    • 0031768025 scopus 로고    scopus 로고
    • Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • R. Liu, J.S. Althaus, B.R. Ellerbrock, D.A. Becker and M.E. Gurney (1998) Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis. Annual Neurology 44, 763-770.
    • (1998) Annual Neurology , vol.44 , pp. 763-770
    • Liu, R.1    Althaus, J.S.2    Ellerbrock, B.R.3    Becker, D.A.4    Gurney, M.E.5
  • 15
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • J.P. Crow, J.B. Sampson, Y. Zhuang, J.A. Thompson and J.S. Beckman (1997) Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. Journal of Neurochemistry 69, 1936-1944.
    • (1997) Journal of Neurochemistry , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 17
    • 0033611619 scopus 로고    scopus 로고
    • Release of copper ions from the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants
    • W.S. Eum and J.H. Kang (1999) Release of copper ions from the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants. Molecular Cells 9, 110-114.
    • (1999) Molecular Cells , vol.9 , pp. 110-114
    • Eum, W.S.1    Kang, J.H.2
  • 21
    • 0032553346 scopus 로고    scopus 로고
    • Formation of granular cytoplasmic aggregates in COS7 cells expressing mutant Cu/Zn superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • T. Koide, S. Igarashi, K. Kikugawa, R. Nakano, T. Inuzuka, M. Yamada, H. Takahashi and S. Tsuji (1998) Formation of granular cytoplasmic aggregates in COS7 cells expressing mutant Cu/Zn superoxide dismutase associated with familial amyotrophic lateral sclerosis. Neuroscience Letter 257, 29-32.
    • (1998) Neuroscience Letter , vol.257 , pp. 29-32
    • Koide, T.1    Igarashi, S.2    Kikugawa, K.3    Nakano, R.4    Inuzuka, T.5    Yamada, M.6    Takahashi, H.7    Tsuji, S.8
  • 23
    • 0027456505 scopus 로고
    • Enzyme function of copper, zinc superoxide dismutase as a free radical generator
    • M.B. Yim, P.B. Chock and E.R. Stadtman (1993) Enzyme function of copper, zinc superoxide dismutase as a free radical generator. Journal of Biological Chemistry 268, 4099-4105.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 4099-4105
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 25
  • 26
    • 0027467423 scopus 로고
    • Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis
    • Y. Ikeda, J. Fujii and N. Taniguchi (1993) Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. Journal of Biological Chemistry 268, 3980-3985.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 3980-3985
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3
  • 28
    • 0002542580 scopus 로고
    • Ausubel, P.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (Eds.), Greene/Wiley Interscience, New York
    • H. Piwnica-Worms (1987) In: Current Protocols in Molecular Biology. Ausubel, P.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (Eds.), Greene/Wiley Interscience, New York, pp. 16.8.1-16.11.7.
    • (1987) Current Protocols in Molecular Biology , pp. 1681-16117
    • Piwnica-Worms, H.1
  • 29
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acryl-amide gels
    • C. Beauchamp and I. Fridovich (1971) Superoxide dismutase: improved assays and an assay applicable to acryl-amide gels. Analytical Biochemistry 44, 276-287.
    • (1971) Analytical Biochemistry , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 30
    • 0026469348 scopus 로고
    • 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme
    • 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme. Journal of Biological Chemistry 267, 25 371-25 377.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 25371-25377
    • Sato, K.1    Akaike, T.2    Kohno, M.3    Ando, M.4    Maeda, H.5
  • 31
    • 0032514907 scopus 로고    scopus 로고
    • Reactions of hydrogen peroxide with familial amyotrophic lateral sclerosis mutant human copper-zinc superoxide dismutases studied by pulse radiolysis
    • J.J. Goto, E.B. Gralla, J.S. Valentine and D.E. Cabelli (1998) Reactions of hydrogen peroxide with familial amyotrophic lateral sclerosis mutant human copper-zinc superoxide dismutases studied by pulse radiolysis. Journal of Biological Chemistry 273, 30 104-30 109.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 30104-30109
    • Goto, J.J.1    Gralla, E.B.2    Valentine, J.S.3    Cabelli, D.E.4
  • 35
    • 0031933163 scopus 로고    scopus 로고
    • Presence of Cu/Zn superoxide dismutase (SOD) immunoreactivity in neuronal hyaline inclusions in spinal cords from mice carrying a transgene for Gly93Ala mutant human Cu/Zn SOD
    • N. Shibata, A. Hirano, M. Kobayashi, M.C. Dal Canto, M.E. Gurney, T. Komori, T. Umahara and K. Asayama (1998) Presence of Cu/Zn superoxide dismutase (SOD) immunoreactivity in neuronal hyaline inclusions in spinal cords from mice carrying a transgene for Gly93Ala mutant human Cu/Zn SOD. Acta Neuropathology 95, 136-142.
    • (1998) Acta Neuropathology , vol.95 , pp. 136-142
    • Shibata, N.1    Hirano, A.2    Kobayashi, M.3    Dal Canto, M.C.4    Gurney, M.E.5    Komori, T.6    Umahara, T.7    Asayama, K.8
  • 37
    • 0033405524 scopus 로고    scopus 로고
    • On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase
    • S.I. Liochev and I. Fridovich (1999) On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase. Free Radical Biology & Medicine 27, 1444-1447.
    • (1999) Free Radical Biology & Medicine , vol.27 , pp. 1444-1447
    • Liochev, S.I.1    Fridovich, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.