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Volumn 448, Issue , 1999, Pages 205-213

A study of the dual role of copper in superoxide dismutase as antioxidant and pro-oxidant in cellular models of amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; COPPER ION; SUPEROXIDE DISMUTASE; ZINC ION;

EID: 0033278283     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-4859-1_18     Document Type: Conference Paper
Times cited : (3)

References (38)
  • 1
    • 0027946813 scopus 로고
    • The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis
    • Alexianu, M.E., Ho, B.-K., Mohamed, H., LaBelia, V., Smith, R.G. and Appel, S.H. (1994) The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis. Ann.Neurol. 36, 846-858.
    • (1994) Ann.Neurol. , vol.36 , pp. 846-858
    • Alexianu, M.E.1    Ho, B.-K.2    Mohamed, H.3    LaBelia, V.4    Smith, R.G.5    Appel, S.H.6
  • 4
    • 0002437327 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide in mitochondria
    • (Oberley L.W. ed.), CRC Press, Boca Raton, Florida
    • Boveris, A. and Cadenas, E. (1982). Production of superoxide radicals and hydrogen peroxide in mitochondria, in Superoxide dismutase. Vol.11 (Oberley L.W. ed.), pp.15-30. CRC Press, Boca Raton, Florida.
    • (1982) Superoxide Dismutase , vol.11 , pp. 15-30
    • Boveris, A.1    Cadenas, E.2
  • 5
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage and mithocondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling, A.C., Schulz, J.B., Brown, R.H., Jr. and Beal, M.F. (1993). Superoxide dismutase activity, oxidative damage and mithocondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61, 2322-2325.
    • (1993) J. Neurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown R.H., Jr.3    Beal, M.F.4
  • 6
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling, A.C. and Beal, M.F. (1995). Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171.
    • (1995) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 8
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but no protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
    • Bruijn, L.I., Beal, M.F., Becher, M.W., Schulz, J.B., Wong, P.C., Price, D.L. and Cleveland, D.W. (1997). Elevated free nitrotyrosine levels, but no protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl. Acad. Sci USA 94, 7606-7611.
    • (1997) Proc. Natl. Acad. Sci USA , vol.94 , pp. 7606-7611
    • Bruijn, L.I.1    Beal, M.F.2    Becher, M.W.3    Schulz, J.B.4    Wong, P.C.5    Price, D.L.6    Cleveland, D.W.7
  • 9
    • 0028172052 scopus 로고
    • Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis
    • Carri', M.T., Battistoni, A., Polizio, F., Desideri, A. and Rotilio G. (1994). Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis. FEBS letters 356, 314-316.
    • (1994) FEBS Letters , vol.356 , pp. 314-316
    • Carri', M.T.1    Battistoni, A.2    Polizio, F.3    Desideri, A.4    Rotilio, G.5
  • 11
    • 0038153078 scopus 로고
    • A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering
    • Culotta, V.C., Joh, H.-D., Lin, S.-J., Slekar, K.H. and Strain, J. (1995). A physiological role for Saccharomyces cerevisiae Copper/zinc superoxide dismutase in copper buffering. J.Biol.Chem., 270, 29991-29997.
    • (1995) J.Biol.Chem. , vol.270 , pp. 29991-29997
    • Culotta, V.C.1    Joh, H.-D.2    Lin, S.-J.3    Slekar, K.H.4    Strain, J.5
  • 13
    • 0027933701 scopus 로고
    • +: Implications for neurodegeneration
    • +: Implications for neurodegeneration. J.of Neurochem. 63, 584-591.
    • (1994) J.of Neurochem. , vol.63 , pp. 584-591
    • Dykens, J.A.1
  • 14
    • 0022684839 scopus 로고
    • Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: Extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation
    • Elroy-Stein, O., Bernstein, Y. and Groner, Y (1986). Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. Embo J. 5, 615-622.
    • (1986) Embo J. , vol.5 , pp. 615-622
    • Elroy-Stein, O.1    Bernstein, Y.2    Groner, Y.3
  • 15
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutase
    • Fridovich, I. (1995). Superoxide radical and superoxide dismutase. Ann. Rev. Biochem. 64, 97-112.
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 18
    • 0029933694 scopus 로고    scopus 로고
    • Regulation of Bcl-2 protein expression in human neuroblastoma SH-Sy5Y cells : Positive and negative effects of protein kinase C and A, respectively
    • Itano, Y., Ito, A., Uehara, T. and Nomura, Y. (1996) Regulation of Bcl-2 Protein expression in human neuroblastoma SH-SY5Y Cells : Positive and negative effects of protein kinase C and A, respectively. J.Neurochem. 67, 131-137.
    • (1996) J.Neurochem. , vol.67 , pp. 131-137
    • Itano, Y.1    Ito, A.2    Uehara, T.3    Nomura, Y.4
  • 21
    • 0029883795 scopus 로고    scopus 로고
    • Copper biochemistry and molecular biology
    • Linder, M.C. and Hazegh-Azan, M. (1996). Copper biochemistry and molecular biology. Am.J.Clin. Nutr. 63, 797-811.
    • (1996) Am.J.Clin. Nutr. , vol.63 , pp. 797-811
    • Linder, M.C.1    Hazegh-Azan, M.2
  • 23
    • 0002093506 scopus 로고
    • Bioengineering of superoxide dismutase and related enzymes. Basic and clinical aspects. In bioengineered molecules : Basic and clinical aspects
    • Verna, R., Blumenthal, R. e Frati, L. eds. Raven Press
    • Marcocci L., Carri, M.T., Battistoni, A. e Rotilio, G. (1989). Bioengineering of superoxide dismutase and related enzymes. Basic and clinical aspects. In Bioengineered molecules : basic and clinical aspects, Verna, R., Blumenthal, R. e Frati, L. eds. Serono Symposia Series Adv. Exp. Med. 1 pp. 11-27 Raven Press.
    • (1989) Serono Symposia Series Adv. Exp. Med. , vol.1 , pp. 11-27
    • Marcocci, L.1    Carri, M.T.2    Battistoni, A.3    Rotilio, G.4
  • 24
    • 0020362126 scopus 로고
    • Superoxide dismutase, glutathione peroxidase and catalase in oxidative hemolysis. A study of fanconi's anemia erythrocytes
    • Mavelli, I., Ciriolo, M.R., Rotilio, G., DeSole, P., Castorino, M. and Stabile, A. (1982) Superoxide dismutase, glutathione peroxidase and catalase in oxidative hemolysis. A study of Fanconi's anemia erythrocytes. Biochem.Biophys.Res.Commun., 106, 286-290.
    • (1982) Biochem.Biophys.Res.Commun. , vol.106 , pp. 286-290
    • Mavelli, I.1    Ciriolo, M.R.2    Rotilio, G.3    DeSole, P.4    Castorino, M.5    Stabile, A.6
  • 25
    • 0030819491 scopus 로고    scopus 로고
    • Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage
    • Nishikawa, T., Lee, S.M., Shiraishi, N., Ishikawa, T., Ohta, Y. and Nishikimi, M. (1997). Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage. J. Biol. Chem. 272, 23037-23041.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23037-23041
    • Nishikawa, T.1    Lee, S.M.2    Shiraishi, N.3    Ishikawa, T.4    Ohta, Y.5    Nishikimi, M.6
  • 26
    • 0027452090 scopus 로고
    • Mild ALS in Japan associated with novel SOD mutation
    • Ogasawara, M., Matsubara, Y. and Narisawa, K. (1993). Mild ALS in Japan associated with novel SOD mutation. Nature Genetics 5, 323-324.
    • (1993) Nature Genetics , vol.5 , pp. 323-324
    • Ogasawara, M.1    Matsubara, Y.2    Narisawa, K.3
  • 27
    • 10344222645 scopus 로고    scopus 로고
    • Identification of an apo-superoxide dismutase pool in human lymphoblasts
    • Petrovic, N., Comi, A., Ettinger, M.J. (1996). Identification of an apo-superoxide dismutase pool in human lymphoblasts. J. Biol. Chem. 271, 28331-28334.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28331-28334
    • Petrovic, N.1    Comi, A.2    Ettinger, M.J.3
  • 29
    • 0029808008 scopus 로고    scopus 로고
    • Molecular genetic basis of familial ALS
    • Siddique, T., Nijhawan, D. and Hantati, A. (1996) Molecular genetic basis of familial ALS. Neurol. 47 (Suppl.2) S27.
    • (1996) Neurol. , vol.47 , Issue.SUPPL. 2
    • Siddique, T.1    Nijhawan, D.2    Hantati, A.3
  • 30
    • 0026795635 scopus 로고
    • Protein oxidation
    • Stadman, E.R. (1992) Protein oxidation. Science 257, 1220-1224
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadman, E.R.1
  • 31
    • 0026350895 scopus 로고
    • Increase of Cu/Zn superoxide dismutase activity during differentiation of K562 cells involves activation by copper of a constantly expressed copper-free protein
    • 1991
    • Steinkhuler, C., Sapora, O., Carri, M.T., Nagel, W., Marcocci, L., Ciriolo, M.R., Weser, U. e Rotilio, G. (1991). Increase of Cu/Zn superoxide dismutase activity during differentiation of K562 cells involves activation by copper of a constantly expressed copper-free protein. J. Biol. Chem. 266, 24580-24587 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 24580-24587
    • Steinkhuler, C.1    Sapora, O.2    Carri, M.T.3    Nagel, W.4    Marcocci, L.5    Ciriolo, M.R.6    Weser, U.7    Rotilio, G.8
  • 32
    • 0028031495 scopus 로고
    • Copper-dependent metabolism of Cu,Zn-superoxide dismutase in human K562 cells
    • Steinkhuler, C., Carri, M.T., Micheli, G., Knoepfel, L., Weser, U. and Rotilio, G. (1994). Copper-dependent metabolism of Cu,Zn-superoxide dismutase in human K562 cells. Biochem.J. 302, 687-694.
    • (1994) Biochem.J. , vol.302 , pp. 687-694
    • Steinkhuler, C.1    Carri, M.T.2    Micheli, G.3    Knoepfel, L.4    Weser, U.5    Rotilio, G.6
  • 34
    • 0029053881 scopus 로고
    • An adverse property of familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong, P.C., Pardo, C.A., Borchelt, D.R., Lee, M.K., Copeland, N.G., Jenkins, N.A., Sisodia, S.S., Cleveland, D.W. and Price, D.L. (1995) An adverse property of familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 35
    • 0025285382 scopus 로고
    • Copper,zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • Yim, M.B., Chock, P.B., Stadtman, E.R. (1990). Copper,zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc.Natl.Acad.Sci. USA 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
  • 36
    • 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
    • Yim, M.B., Kang, J.-H., Yim, H.-S., Kwak, H.-S., Chock, P.B. and Stadtman, E.R. (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. Proc.Natl.Acad.Sci.USA 93, 5709-5714.
    • (1996) Proc.Natl.Acad.Sci.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
  • 38
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang, Y., Marcillat, O., Giulivi, C., Ernster, L. and Davies, K.J.A. (1990) The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J.Biol.Chem. 265, 16330-16336.
    • (1990) J.Biol.Chem. , vol.265 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulivi, C.3    Ernster, L.4    Davies, K.J.A.5


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