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Volumn 73, Issue 3, 1999, Pages 1175-1180

Aberrant copper chemistry as a major mediator of oxidative stress in a human cellular model of amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis; Copper; D Penicillamine; Oxidative stress; Paraquat; Superoxide dismutase

Indexed keywords

COPPER ION; COPPER ZINC SUPEROXIDE DISMUTASE; PARAQUAT; PENICILLAMINE;

EID: 0032840228     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0731175.x     Document Type: Article
Times cited : (58)

References (31)
  • 2
    • 0030851761 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
    • Beal M. F., Ferrante R. J., Browne S. E., Matthews R., Kowall N. W., and Brown R. H. (1997) Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann. Neurol. 42, 646-654.
    • (1997) Ann. Neurol. , vol.42 , pp. 646-654
    • Beal, M.F.1    Ferrante, R.J.2    Browne, S.E.3    Matthews, R.4    Kowall, N.W.5    Brown, R.H.6
  • 3
    • 0031868461 scopus 로고    scopus 로고
    • Elevated "hydroxyl radical" generation in vivo in an animal model of amyotrophic lateral sclerosis
    • Bogdanov M. B., Ramos L. E., Xu Z., and Beal M. F. (1998) Elevated "hydroxyl radical" generation in vivo in an animal model of amyotrophic lateral sclerosis. J. Neurochem. 71, 1321-1324.
    • (1998) J. Neurochem. , vol.71 , pp. 1321-1324
    • Bogdanov, M.B.1    Ramos, L.E.2    Xu, Z.3    Beal, M.F.4
  • 4
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but not 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., Shulz J. B., Wong P. C., Price D. L., and Cleveland D. W. (1997) Elevated free nitrotyrosine levels, but not 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    Shulz, J.B.4    Wong, P.C.5    Price, D.L.6    Cleveland, D.W.7
  • 6
    • 0028172052 scopus 로고
    • Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis
    • Carrì 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 Lett. 356, 314-316.
    • (1994) FEBS Lett. , vol.356 , pp. 314-316
    • Carrì, M.T.1    Battistoni, A.2    Polizio, F.3    Desideri, A.4    Rotilio, G.5
  • 8
    • 0032568546 scopus 로고    scopus 로고
    • Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants
    • Corson L. B., Strain J. J., Culotta V. C., and Cleveland D. W. (1998) Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants. Proc. Natl. Acad. Sci. USA 95, 6361-6366.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6361-6366
    • Corson, L.B.1    Strain, J.J.2    Culotta, V.C.3    Cleveland, D.W.4
  • 9
    • 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
    • Crow J. P., Sampson J. B., Zhuang Y., Thompson J. A., and Beckman J. S. (1997) Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69, 1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 12
    • 0030831352 scopus 로고    scopus 로고
    • Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: Molecular mechanisms of neuronal death and protection
    • Ghadge G. D., Lee J. P., Bindokas V. P., Jordan J., Ma L., Miller R. J., and Roos R. P. (1997) Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: molecular mechanisms of neuronal death and protection. J. Neurosci. 17, 8756-8766.
    • (1997) J. Neurosci. , vol.17 , pp. 8756-8766
    • Ghadge, G.D.1    Lee, J.P.2    Bindokas, V.P.3    Jordan, J.4    Ma, L.5    Miller, R.J.6    Roos, R.P.7
  • 13
    • 0016816805 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Chemiluminescence and peroxidation
    • Hodgson E. K. and Fridovich I. (1975) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry 14, 5299-5303.
    • (1975) Biochemistry , vol.14 , pp. 5299-5303
    • Hodgson, E.K.1    Fridovich, I.2
  • 14
    • 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 A. F., Fine E. G., Gurney M. E., Zurn A. D., and Aebischer P. (1997) 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. 9, 1548-1551.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1548-1551
    • Hottinger, A.F.1    Fine, E.G.2    Gurney, M.E.3    Zurn, A.D.4    Aebischer, P.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1972) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-689.
    • (1972) Nature , vol.227 , pp. 680-689
    • Laemmli, U.K.1
  • 17
    • 0002191974 scopus 로고
    • Catalase
    • Bergmayer H. U., ed. Academic Press, New York
    • Luck H. (1963) Catalase, in Methods in Enzymatic Analysis, 2nd edit. (Bergmayer H. U., ed), pp. 885-888. Academic Press, New York.
    • (1963) Methods in Enzymatic Analysis, 2nd Edit. , pp. 885-888
    • Luck, H.1
  • 18
    • 0016272750 scopus 로고
    • Involvement of superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S. and Marklund G. (1974) Involvement of superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 47, 469-474.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 19
    • 0024515890 scopus 로고
    • Effects of chelators on copper metabolism and copper pools in mouse hepatocytes
    • McArdle H. J., Gross S. M., Creaser I., Sargeson A. M., and Danks D. M. (1989) Effects of chelators on copper metabolism and copper pools in mouse hepatocytes. Am. J. Physiol. 256, G667-G672.
    • (1989) Am. J. Physiol. , vol.256
    • McArdle, H.J.1    Gross, S.M.2    Creaser, I.3    Sargeson, A.M.4    Danks, D.M.5
  • 20
    • 0014691242 scopus 로고
    • Superoxide dismutase, enzymic function for erythrocuprein (hemocuprein)
    • McCord J. and Fridovich I. (1969) Superoxide dismutase, enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.1    Fridovich, I.2
  • 21
    • 10344222645 scopus 로고    scopus 로고
    • Identification of an apo-superoxide dismutase pool in human lymphoblasts
    • Petrovic N., Comi A., and 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
  • 22
    • 0029050058 scopus 로고
    • Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: Neuropathology and a model of dimer dysequilibrium
    • Phillips J. P., Tainer J. A., Getzoff E. D., Boulianne G. L., Kirby K., and Hilliker A. J. (1995) Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: neuropathology and a model of dimer dysequilibrium. Proc. Natl. Acad. Sci. USA 92, 8574-8578.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8574-8578
    • Phillips, J.P.1    Tainer, J.A.2    Getzoff, E.D.3    Boulianne, G.L.4    Kirby, K.5    Hilliker, A.J.6
  • 25
    • 0026350895 scopus 로고
    • Increase of Cu,Zn-superoxide dismutase activity during differentiation of human K562 cells involves activation by copper of a constantly expressed copper-deficient protein
    • Steinkhuler C., Sapora O., Carrì M. T., Nagel W., Marcocci L., Ciriolo M. R., Weser U., and Rotilio G. (1991) Increase of Cu,Zn-superoxide dismutase activity during differentiation of human K562 cells involves activation by copper of a constantly expressed copper-deficient protein. J. Biol. Chem. 266, 24580-24587.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24580-24587
    • Steinkhuler, C.1    Sapora, O.2    Carrì, M.T.3    Nagel, W.4    Marcocci, L.5    Ciriolo, M.R.6    Weser, U.7    Rotilio, G.8
  • 28
    • 0029053881 scopus 로고
    • An adverse property of a 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. J., Jenkins N. A., Sisodia S. S., Cleveland D. W., and Price D. L. (1995) An adverse property of a 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.J.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 29
    • 0025285382 scopus 로고
    • Copper,zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • Yim M. B., Chock P. B., and 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
  • 30
    • 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
  • 31
    • 0030900245 scopus 로고    scopus 로고
    • A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide
    • Yim H.-S., Kang J.-H., Chock P. B., Stadtman E. R., and Yim M. B. (1997) A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. J. Biol. Chem. 272, 8861-8863.
    • (1997) J. Biol. Chem. , 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


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