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Volumn 13, Issue 3, 2003, Pages 213-221

Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with amyotrophic lateral sclerosis is reversed by N-acetylcysteine

Author keywords

Amyotrophic lateral sclerosis; Mitochondrial function; N Acetylcysteine; Oxidative stress; SOD1

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM; ACETYLCYSTEINE; ADENOSINE TRIPHOSPHATE; COPPER ZINC SUPEROXIDE DISMUTASE; REACTIVE OXYGEN METABOLITE; TETRAZOLIUM; UNCLASSIFIED DRUG;

EID: 0042093555     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-9961(03)00043-3     Document Type: Article
Times cited : (72)

References (47)
  • 1
    • 0034601439 scopus 로고    scopus 로고
    • N-acetyl-L-cysteine improves survival and preserves motor performance in an animal model of familial amyotrophic lateral sclerosis
    • Andreassen O.A., Dedeoglu A., Klivenyi P., Beal M.F., Bush A.I. N-acetyl-L-cysteine improves survival and preserves motor performance in an animal model of familial amyotrophic lateral sclerosis. NeuroReport. 11:(11):2000;2491-2493.
    • (2000) NeuroReport , vol.11 , Issue.11 , pp. 2491-2493
    • Andreassen, O.A.1    Dedeoglu, A.2    Klivenyi, P.3    Beal, M.F.4    Bush, A.I.5
  • 2
    • 0035163332 scopus 로고    scopus 로고
    • Palliative care in amyotrophic lateral sclerosis
    • Borasio G.D., Voltz R., Miller R.G. Palliative care in amyotrophic lateral sclerosis. Neurol. Clin. 19:(4):2001;829-847.
    • (2001) Neurol. Clin. , vol.19 , Issue.4 , pp. 829-847
    • Borasio, G.D.1    Voltz, R.2    Miller, R.G.3
  • 3
    • 0032745071 scopus 로고    scopus 로고
    • Mitochondrial enzyme activity in amyotrophic lateral sclerosis: Implication for the role of mitochondria in neuronal cell death
    • Borthwick G.M., Johnson M.A., Ince P.G., Shaw P.J., Turnbull D.M. Mitochondrial enzyme activity in amyotrophic lateral sclerosis implication for the role of mitochondria in neuronal cell death . Ann. Neurol. 46:1999;787-790.
    • (1999) Ann. Neurol. , vol.46 , pp. 787-790
    • Borthwick, G.M.1    Johnson, M.A.2    Ince, P.G.3    Shaw, P.J.4    Turnbull, D.M.5
  • 4
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling A.C., Shulz J.B., Brown R.H. Jr., Beal M.F. Superoxide dismutase activity, oxidative damage and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61:(6):1993;2322-2325.
    • (1993) J. Neurochem. , vol.61 , Issue.6 , pp. 2322-2325
    • Bowling, A.C.1    Shulz, J.B.2    Brown R.H., Jr.3    Beal, M.F.4
  • 5
    • 0031728550 scopus 로고    scopus 로고
    • SOD1 aggregates in ALS: Cause, correlate or consequence?
    • Brown R.H. SOD1 aggregates in ALS cause, correlate or consequence? Nat. Medi. 4:1998;1362-1364.
    • (1998) Nat. Medi. , vol.4 , pp. 1362-1364
    • Brown, R.H.1
  • 7
    • 33845333122 scopus 로고    scopus 로고
    • Is ALS caused by an altered oxidative activity of mutant superoxide dismutase?
    • discussion 919-920
    • Bush A.I. Is ALS caused by an altered oxidative activity of mutant superoxide dismutase? Nat. Neurosci. 5:(10):2002;919. discussion 919-920.
    • (2002) Nat. Neurosci. , vol.5 , Issue.10 , pp. 919
    • Bush, A.I.1
  • 8
    • 0031559896 scopus 로고    scopus 로고
    • Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells
    • Carri M.T., Ferri A., Battistoni A., Famhy L., Gabbianelli R., Poccia F., Rotilio G. Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett. 414:1997;365-368.
    • (1997) FEBS Lett. , vol.414 , pp. 365-368
    • Carri, M.T.1    Ferri, A.2    Battistoni, A.3    Famhy, L.4    Gabbianelli, R.5    Poccia, F.6    Rotilio, G.7
  • 9
    • 0036892743 scopus 로고    scopus 로고
    • Oxidative modulation of NF-κB in human cells expressing mutant FALS-typical superoxide dismutases
    • Casciati A., Ferri A., Cozzolino M., Celsi F., Nencini M., Rotilio G., Carri M.T. Oxidative modulation of NF-κB in human cells expressing mutant FALS-typical superoxide dismutases. J. Neurochem. 83:2002;1019-1029.
    • (2002) J. Neurochem. , vol.83 , pp. 1019-1029
    • Casciati, A.1    Ferri, A.2    Cozzolino, M.3    Celsi, F.4    Nencini, M.5    Rotilio, G.6    Carri, M.T.7
  • 10
    • 0034678528 scopus 로고    scopus 로고
    • Intracellular glutathione levels determine cerebellar granule neuron sensitivity to excitotoxic injury by kainic acid
    • Ceccon M., Giusti P., Facci L., Borin G., Imbevi M., Floreali M., Skaper S.D. Intracellular glutathione levels determine cerebellar granule neuron sensitivity to excitotoxic injury by kainic acid. Brain Res. 862:2000;83-89.
    • (2000) Brain Res. , vol.862 , pp. 83-89
    • Ceccon, M.1    Giusti, P.2    Facci, L.3    Borin, G.4    Imbevi, M.5    Floreali, M.6    Skaper, S.D.7
  • 11
    • 0034681320 scopus 로고    scopus 로고
    • Cu,Zn-superoxide dismutase-dependent apoptosis induced by nitric oxide in neuronal cells
    • Ciriolo M.R., De Martino A., Lafavia E., Rossi L., Carri M.T., Rotilio G. Cu,Zn-superoxide dismutase-dependent apoptosis induced by nitric oxide in neuronal cells. J. Biol. Chem. 275:2000;5065-5072.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5065-5072
    • Ciriolo, M.R.1    De Martino, A.2    Lafavia, E.3    Rossi, L.4    Carri, M.T.5    Rotilio, G.6
  • 12
    • 0034974866 scopus 로고    scopus 로고
    • Differential role of superoxide and glutathione in S-nitrosoglutathione-mediated apoptosis: A rationale for mild forms of familial amyotrophic lateral sclerosis associated with less active Cu,Zn superoxide dismutase mutants
    • Ciriolo M.R., Aquilano K., De Martino A., Carri M.T., Rotilio G. Differential role of superoxide and glutathione in S-nitrosoglutathione-mediated apoptosis a rationale for mild forms of familial amyotrophic lateral sclerosis associated with less active Cu,Zn superoxide dismutase mutants . J. Neurochem. 77:(6):2001;1433-1443.
    • (2001) J. Neurochem. , vol.77 , Issue.6 , pp. 1433-1443
    • Ciriolo, M.R.1    Aquilano, K.2    De Martino, A.3    Carri, M.T.4    Rotilio, G.5
  • 13
    • 0029809528 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Oxidative energy metabolism and calcium homeostasis in peripheral blood lymphocytes
    • Curti D., Malspina A., Facchetti G., Camana C., Mazzini L., Tosca P., Zerbi F., Ceroni M. Amyotrophic lateral sclerosis oxidative energy metabolism and calcium homeostasis in peripheral blood lymphocytes . Neurol. 47:1996;1060-1064.
    • (1996) Neurol. , vol.47 , pp. 1060-1064
    • Curti, D.1    Malspina, A.2    Facchetti, G.3    Camana, C.4    Mazzini, L.5    Tosca, P.6    Zerbi, F.7    Ceroni, M.8
  • 14
    • 0028823914 scopus 로고
    • Familial amyotrophic lateral sclerosis/motor neurone disease (FASL): A review of current developments
    • De Belleroche J., Orrell R., King A. Familial amyotrophic lateral sclerosis/motor neurone disease (FASL) a review of current developments . J. Med. Genet. 32:1995;841-847.
    • (1995) J. Med. Genet. , vol.32 , pp. 841-847
    • De Belleroche, J.1    Orrell, R.2    King, A.3
  • 16
    • 0033914937 scopus 로고    scopus 로고
    • Calcineurin activity is regulated both by redox compounds and by mutant familial amyotrophic lateral sclerosis-superoxide dismutase
    • Ferri A., Gabbianelli R., Casciati A., Paolucci E., Rotilio G., Carri M.T. Calcineurin activity is regulated both by redox compounds and by mutant familial amyotrophic lateral sclerosis-superoxide dismutase. J. Neurochem. 75:(2):2000;606-613.
    • (2000) J. Neurochem. , vol.75 , Issue.2 , pp. 606-613
    • Ferri, A.1    Gabbianelli, R.2    Casciati, A.3    Paolucci, E.4    Rotilio, G.5    Carri, M.T.6
  • 17
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:1995;97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 18
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Hayward L.J., Rodriguez J.A., Kim J.W., Tiwari A., Goto J.J., Cabelli D.E., Valentine J.S., Brown R.H. Jr. Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 277:(18):2002;15923-15931.
    • (2002) J. Biol. Chem. , vol.277 , Issue.18 , pp. 15923-15931
    • Hayward, L.J.1    Rodriguez, J.A.2    Kim, J.W.3    Tiwari, A.4    Goto, J.J.5    Cabelli, D.E.6    Valentine, J.S.7    Brown R.H., Jr.8
  • 20
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu,Zn Superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins C.M., Jung C., Ding H., Xu Z. Mutant Cu,Zn Superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci. 22:(6):2002;RC215.
    • (2002) J. Neurosci. , vol.22 , Issue.6 , pp. 215
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 21
    • 0035936804 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Unfolding the toxicity of the misfolded
    • Julien J.P. Amyotrophic lateral sclerosis unfolding the toxicity of the misfolded . Cell. 104:(4):2001;581-591.
    • (2001) Cell , vol.104 , Issue.4 , pp. 581-591
    • Julien, J.P.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:(259):1970;680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0036724314 scopus 로고    scopus 로고
    • No correlation between aggregates of Cu/Zn superoxide dismutase and cell death in familial amyotrophic lateral sclerosis
    • Lee J.P., Gerin C., Bindokas V.P., Miller R., Ghadge G., Roos R.P. No correlation between aggregates of Cu/Zn superoxide dismutase and cell death in familial amyotrophic lateral sclerosis. J. Neurochem. 82:(5):2002;1229-1238.
    • (2002) J. Neurochem. , vol.82 , Issue.5 , pp. 1229-1238
    • Lee, J.P.1    Gerin, C.2    Bindokas, V.P.3    Miller, R.4    Ghadge, G.5    Roos, R.P.6
  • 24
    • 0035958729 scopus 로고    scopus 로고
    • Intracellular generation of free radicals and modifications of detoxifying enzymes in cultured neurons from the developing rat forebrain in response to transient hypoxia
    • Lievre V., Becuwe P., Bianchi A., Bossenmeyer-Pourie C., Koziel V., Franck P., Nicolas M.B., Dauca M., Vert P., Daval J.L. Intracellular generation of free radicals and modifications of detoxifying enzymes in cultured neurons from the developing rat forebrain in response to transient hypoxia. Neuroscience. 105:(2):2001;287-297.
    • (2001) Neuroscience , vol.105 , Issue.2 , pp. 287-297
    • Lievre, V.1    Becuwe, P.2    Bianchi, A.3    Bossenmeyer-Pourie, C.4    Koziel, V.5    Franck, P.6    Nicolas, M.B.7    Dauca, M.8    Vert, P.9    Daval, J.L.10
  • 25
    • 0037144562 scopus 로고    scopus 로고
    • Copper, zinc superoxide dismutase and H2O2: Effects of bicarbonate on inactivation and oxidations of NADPH and urate, and on consumption of H2O2
    • Liochev S.I., Fridovich I. Copper, zinc superoxide dismutase and H2O2 effects of bicarbonate on inactivation and oxidations of NADPH and urate, and on consumption of H2O2 . J. Biol. Chem. 277:(38):2002;34674-34678.
    • (2002) J. Biol. Chem. , vol.277 , Issue.38 , pp. 34674-34678
    • Liochev, S.I.1    Fridovich, I.2
  • 26
    • 0030852948 scopus 로고    scopus 로고
    • Mechanisms of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolinium bromide (MTT) reduction
    • Liu Y., Peterson D.A., Kimura H., Schubert D. Mechanisms of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolinium bromide (MTT) reduction. J. Neurochem. 69:(2):1997;581-593.
    • (1997) J. Neurochem. , vol.69 , Issue.2 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 29
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A., Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver Cu,Zn-SOD in mitochondria . J. Biol. Chem. 276:(42):2001;38388-38393.
    • (2001) J. Biol. Chem. , vol.276 , Issue.42 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 30
    • 0036209161 scopus 로고    scopus 로고
    • A proposed mechanism of ALS fails the test in vivo
    • Orr H.T. A proposed mechanism of ALS fails the test in vivo. Nat. Neurosci. 5:(4):2002;287-288.
    • (2002) Nat. Neurosci. , vol.5 , Issue.4 , pp. 287-288
    • Orr, H.T.1
  • 31
    • 0037013224 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase
    • Rodriguez J.A., Valentine J.S., Eggers D.K., Roe J.A., Tiwari A., Brown R.H. Jr., Hayward L.J. Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase. J. Biol. Chem. 277:(18):2002;15932-15937.
    • (2002) J. Biol. Chem. , vol.277 , Issue.18 , pp. 15932-15937
    • Rodriguez, J.A.1    Valentine, J.S.2    Eggers, D.K.3    Roe, J.A.4    Tiwari, A.5    Brown R.H., Jr.6    Hayward, L.J.7
  • 33
    • 0028899301 scopus 로고
    • Amyotrophic lateral sclerosis: Human challenge for neuroscience
    • Rowland L.P. Amyotrophic lateral sclerosis human challenge for neuroscience . Proc. Natl. Acad. Sci. USA. 92:1995;1251-1253.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1251-1253
    • Rowland, L.P.1
  • 34
    • 0032100603 scopus 로고    scopus 로고
    • Redox signaling and the emerging therapeutic potential of thiol antioxidants
    • Sen C.K. Redox signaling and the emerging therapeutic potential of thiol antioxidants. Biochem. Pharmacol. 55:1998;1747-1758.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1747-1758
    • Sen, C.K.1
  • 35
    • 0035918258 scopus 로고    scopus 로고
    • Mutant Cu,Zn-Superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder G.A., Lacourse M.C., Minotti S., Durham D. Mutant Cu,Zn-Superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem. 276:2001;12791-12796.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, D.4
  • 37
    • 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
    • Steinkuhler C., Sapora O., Carri M.T., Nagel W., Marcocci L., Ciriolo M.R., Weser U., Rotilio G. 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. 266:1991;24580-24587.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24580-24587
    • Steinkuhler, 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
  • 38
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria: A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz L.A., Diekert K., Jensen L.T., Lill R., Culotta C.V. A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria a physiological role for SOD1 in guarding against mitochondrial oxidative damage . J. Biol. Chem. 276:(41):2001;38084-38089.
    • (2001) J. Biol. Chem. , vol.276 , Issue.41 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, C.V.5
  • 42
    • 0035906260 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in spinal motoneurons of transgenic ALS mice
    • Warita H., Hayashi T., Murakami T., Manabe Y., Abe K. Oxidative damage to mitochondrial DNA in spinal motoneurons of transgenic ALS mice. Mol. Brain Res. 89:2001;147-152.
    • (2001) Mol. Brain Res. , vol.89 , pp. 147-152
    • Warita, H.1    Hayashi, T.2    Murakami, T.3    Manabe, Y.4    Abe, K.5
  • 44
    • 0036321382 scopus 로고    scopus 로고
    • Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients
    • Wiedemann F.R., Manfredi G., Mawrin C., Beal M.F., Schon E.A. Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients. J. Neurochem. 80:(4):2002;616-625.
    • (2002) J. Neurochem. , vol.80 , Issue.4 , pp. 616-625
    • Wiedemann, F.R.1    Manfredi, G.2    Mawrin, C.3    Beal, M.F.4    Schon, E.A.5
  • 45
    • 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 P.C., Borchelt D.R., Lee M.K., Copeland N.G., Jenkins N.A., Sisodia S.S., Cleveland D.W., Price D.L. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron. 14:1995;1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, P.C.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
  • 46
    • 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., Stadtman E.R. 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:(12):1996;5709-5714.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.12 , 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
  • 47
    • 0032569619 scopus 로고    scopus 로고
    • Voltage-activated sodium currents in a cell line expressing a Cu,Zn superoxide dismutase typical of familial ALS
    • Zona C., Ferri A., Gabbianelli R., Mercuri N.B., Bernardi G., Rotilio G., Carri M.T. Voltage-activated sodium currents in a cell line expressing a Cu,Zn superoxide dismutase typical of familial ALS. NeuroReport. 9:1998;3515-3518.
    • (1998) NeuroReport , vol.9 , pp. 3515-3518
    • Zona, C.1    Ferri, A.2    Gabbianelli, R.3    Mercuri, N.B.4    Bernardi, G.5    Rotilio, G.6    Carri, M.T.7


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