메뉴 건너뛰기




Volumn 18, Issue 23, 2009, Pages 4552-4564

Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 70449417623     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddp421     Document Type: Article
Times cited : (132)

References (46)
  • 1
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in Als
    • Bruijn, L.I., Miller, T.M. and Cleveland, D.W. (2004) Unraveling the mechanisms involved in motor neuron degeneration in Als. Annu. Rev. Neurosci., 27, 723-749.
    • (2004) Annu. Rev. Neurosci , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 2
    • 33646241740 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and amyotrophic lateral sclerosis
    • Hervias, I., Beal, M.F. and Manfredi, G. (2006) Mitochondrial dysfunction and amyotrophic lateral sclerosis. Muscle Nerve, 33 598-608.
    • (2006) Muscle Nerve , vol.33 , pp. 598-608
    • Hervias, I.1    Beal, M.F.2    Manfredi, G.3
  • 3
    • 66749104344 scopus 로고    scopus 로고
    • Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis
    • Magrane, J. and Manfredi, G. (2009) Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis. Antioxid. Redox Signal., 11, 1615-1626.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 1615-1626
    • Magrane, J.1    Manfredi, G.2
  • 4
    • 0037086851 scopus 로고    scopus 로고
    • A quantitative histochemical assay for activities of mitochondrial electron transport chain complexes in mouse spinal cord sections
    • Jung, C., Higgins, C.M. and Xu, Z. (2002) A quantitative histochemical assay for activities of mitochondrial electron transport chain complexes in mouse spinal cord sections. J. Neurosci. Methods, 114, 165-172.
    • (2002) J. Neurosci. Methods , vol.114 , pp. 165-172
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 5
    • 0037119407 scopus 로고    scopus 로고
    • Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice
    • Mattiazzi, M., D'Aurelio, M., Gajewski, C.D., Martushova, K., Kiaei, M., Beal, M.F. and Manfredi, G. (2002) Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J. Biol. Chem., 277, 29626-29633.
    • (2002) J. Biol. Chem , vol.277 , pp. 29626-29633
    • Mattiazzi, M.1    D'Aurelio, M.2    Gajewski, C.D.3    Martushova, K.4    Kiaei, M.5    Beal, M.F.6    Manfredi, G.7
  • 9
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1
    • Kong, J. and Xu, Z. (1998) Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Neurosci., 18, 3241-3250.
    • (1998) J. Neurosci , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 10
  • 11
    • 0029812897 scopus 로고    scopus 로고
    • Impairment of fast axonal transport in the proximal axons of anterior horn neurons in amyotrophic lateral sclerosis
    • Sasaki, S. and Iwata, M. (1996) Impairment of fast axonal transport in the proximal axons of anterior horn neurons in amyotrophic lateral sclerosis. Neurology, 47, 535-540.
    • (1996) Neurology , vol.47 , pp. 535-540
    • Sasaki, S.1    Iwata, M.2
  • 13
    • 0015848173 scopus 로고
    • Superoxide dismutase. Organelle specificity
    • Weisiger, R.A. and Fridovich, I. (1973) Superoxide dismutase. Organelle specificity. J. Biol. Chem., 248, 3582-3592.
    • (1973) J. Biol. Chem , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 14
    • 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. and Culotta, V.C. (2001) 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, 38084-38089.
    • (2001) J. Biol. Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 15
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto, A. and Fridovich, I. (2001) Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem., 276, 38388-38393.
    • (2001) J. Biol. Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 16
    • 0034821922 scopus 로고    scopus 로고
    • CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations
    • Jaarsma, D., Rognoni, F., van Duijn, W., Verspaget, H.W., Haasdijk, E.D. and Holstege, J.C. (2001) CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations. Acta Neuropathol. (Berl), 102, 293-305.
    • (2001) Acta Neuropathol. (Berl) , vol.102 , pp. 293-305
    • Jaarsma, D.1    Rognoni, F.2    van Duijn, W.3    Verspaget, H.W.4    Haasdijk, E.D.5    Holstege, J.C.6
  • 17
    • 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. and Xu, Z. (2002) Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci., 22, RC215.
    • (2002) J. Neurosci , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 18
    • 0344240348 scopus 로고    scopus 로고
    • ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes
    • Higgins, C.M., Jung, C. and Xu, Z. (2003) ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes. BMC Neurosci. 4, 16.
    • (2003) BMC Neurosci , vol.4 , pp. 16
    • Higgins, C.M.1    Jung, C.2    Xu, Z.3
  • 19
    • 14944385595 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice
    • Vijayvergiya, C., Beal, M.F., Buck, J. and Manfredi, G. (2005) Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J. Neurosci., 25 2463-2470.
    • (2005) J. Neurosci , vol.25 , pp. 2463-2470
    • Vijayvergiya, C.1    Beal, M.F.2    Buck, J.3    Manfredi, G.4
  • 20
    • 54449092952 scopus 로고    scopus 로고
    • Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria
    • Kawamata, H. and Manfredi, G. (2008) Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria. Hum. Mol. Genet., 17, 3303-3317.
    • (2008) Hum. Mol. Genet , vol.17 , pp. 3303-3317
    • Kawamata, H.1    Manfredi, G.2
  • 21
    • 41649086378 scopus 로고    scopus 로고
    • Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria
    • Vande Velde, C., Miller, T.M., Cashman, N.R. and Cleveland, D.W. (2008) Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria. Proc. Natl. Acad. Sci. USA, 105, 4022-4027.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4022-4027
    • Vande Velde, C.1    Miller, T.M.2    Cashman, N.R.3    Cleveland, D.W.4
  • 23
    • 34347237645 scopus 로고    scopus 로고
    • Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology
    • Son, M., Puttaparthi, K., Kawamata, H., Rajendran, B., Boyer, P.J., Manfredi, G. and Elliott, J.L. (2007) Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology. Proc. Natl. Acad. Sci. USA, 104, 6072-6077.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6072-6077
    • Son, M.1    Puttaparthi, K.2    Kawamata, H.3    Rajendran, B.4    Boyer, P.J.5    Manfredi, G.6    Elliott, J.L.7
  • 24
    • 0028982927 scopus 로고
    • Sorting of cytochrome b2 to the intermembrane space of mitochondria. Kinetic analysis of intermediates demonstrates passage through the matrix
    • Ono, H., Gruhler, A., Stuart, R.A., Guiard, B., Schwarz, E. and Neupert, W. (1995) Sorting of cytochrome b2 to the intermembrane space of mitochondria. Kinetic analysis of intermediates demonstrates passage through the matrix. J. Biol. Chem., 270, 16932-16938.
    • (1995) J. Biol. Chem , vol.270 , pp. 16932-16938
    • Ono, H.1    Gruhler, A.2    Stuart, R.A.3    Guiard, B.4    Schwarz, E.5    Neupert, W.6
  • 28
    • 0032430185 scopus 로고    scopus 로고
    • Pasinelli, P., Borchelt, D.R., Houseweart, M.K., Cleveland, D.W. and Brown, R.H. Jr (1998) Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase [published erratum appears in Proc Natl Acad Sci USA 1999 Mar 16;96(6):3330]. Proc. Natl. Acad. Sci. USA, 95, 15763-15768.
    • Pasinelli, P., Borchelt, D.R., Houseweart, M.K., Cleveland, D.W. and Brown, R.H. Jr (1998) Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase [published erratum appears in Proc Natl Acad Sci USA 1999 Mar 16;96(6):3330]. Proc. Natl. Acad. Sci. USA, 95, 15763-15768.
  • 29
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos, A. and Moraes, C.T. (1999) Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem., 274, 16188-16197.
    • (1999) J. Biol. Chem , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 30
    • 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.G., 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.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 33
    • 10244236554 scopus 로고    scopus 로고
    • Mitochondrial degeneration in amyotrophic lateral sclerosis
    • Xu, Z., Jung, C., Higgins, C., Levine, J. and Kong, J. (2004) Mitochondrial degeneration in amyotrophic lateral sclerosis. J. Bioenerg. Biomembr., 36, 395-399.
    • (2004) J. Bioenerg. Biomembr , vol.36 , pp. 395-399
    • Xu, Z.1    Jung, C.2    Higgins, C.3    Levine, J.4    Kong, J.5
  • 34
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli, P. and Brown, R.H. (2006) Molecular biology of amyotrophic lateral sclerosis: Insights from genetics. Nat. Rev. Neurosci., 7, 710-723.
    • (2006) Nat. Rev. Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 35
    • 17844364182 scopus 로고    scopus 로고
    • Low levels of ALS-linked Cu/Zn superoxide dismutase increase the production of reactive oxygen species and cause mitochondrial damage and death in motor neuron-like cells
    • Rizzardini, M., Mangolini, A., Lupi, M., Ubezio, P., Bendotti, C. and Cantoni, L. (2005) Low levels of ALS-linked Cu/Zn superoxide dismutase increase the production of reactive oxygen species and cause mitochondrial damage and death in motor neuron-like cells. J. Neurol. Sci., 232, 95-103.
    • (2005) J. Neurol. Sci , vol.232 , pp. 95-103
    • Rizzardini, M.1    Mangolini, A.2    Lupi, M.3    Ubezio, P.4    Bendotti, C.5    Cantoni, L.6
  • 37
    • 66749163087 scopus 로고    scopus 로고
    • Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity
    • Cozzolino, M., Pesaresi, M.G., Amori, I., Crosio, C., Ferri, A., Nencini, M. and Carri, M.T. (2009) Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity. Antioxid. Redox Signal., 11, 1547-1558.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 1547-1558
    • Cozzolino, M.1    Pesaresi, M.G.2    Amori, I.3    Crosio, C.4    Ferri, A.5    Nencini, M.6    Carri, M.T.7
  • 39
    • 33845361630 scopus 로고    scopus 로고
    • Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: Mechanisms of mitochondriopathy and cell death
    • Martin, L.J., Liu, Z., Chen, K., Price, A.C., Pan, Y., Swaby, J.A. and Golden, W.C. (2007) Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: Mechanisms of mitochondriopathy and cell death. J. Comp. Neurol., 500, 20-46.
    • (2007) J. Comp. Neurol , vol.500 , pp. 20-46
    • Martin, L.J.1    Liu, Z.2    Chen, K.3    Price, A.C.4    Pan, Y.5    Swaby, J.A.6    Golden, W.C.7
  • 40
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • Deng, H.X., Shi, Y., Furukawa, Y., Zhai, H., Fu, R., Liu, E., Gorrie, G.H., Khan, M.S., Hung, W.Y., Bigio, E.H. et al. (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc. Natl. Acad. Sci. USA, 103, 7142-7147.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7142-7147
    • Deng, H.X.1    Shi, Y.2    Furukawa, Y.3    Zhai, H.4    Fu, R.5    Liu, E.6    Gorrie, G.H.7    Khan, M.S.8    Hung, W.Y.9    Bigio, E.H.10
  • 41
    • 57649138442 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase is a target for mutant SOD1 toxicity in mitochondria
    • Kawamata, H., Magrane, J., Kunst, C., King, M.P. and Manfredi, G. (2008) Lysyl-tRNA synthetase is a target for mutant SOD1 toxicity in mitochondria. J. Biol. Chem., 283, 28321-28328.
    • (2008) J. Biol. Chem , vol.283 , pp. 28321-28328
    • Kawamata, H.1    Magrane, J.2    Kunst, C.3    King, M.P.4    Manfredi, G.5
  • 42
    • 3242703300 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria
    • Pasinelli, P., Belford, M.E., Lennon, N., Bacskai, B.J., Hyman, B.T., Trotti, D. and Brown, R.H. Jr (2004) Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron, 43, 19-30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3    Bacskai, B.J.4    Hyman, B.T.5    Trotti, D.6    Brown Jr, R.H.7
  • 43
    • 34447550238 scopus 로고    scopus 로고
    • Interaction between familial ALS-linked SOD1 mutants and the dynein complex: Implications of retrograde axonal transport in ALS
    • Zhang, F., Strom, A.L., Fukada, K., Lee, S., Hayward, L.J. and Zhu, H. (2007) Interaction between familial ALS-linked SOD1 mutants and the dynein complex: Implications of retrograde axonal transport in ALS. J. Biol. Chem., 282, 16691-16699.
    • (2007) J. Biol. Chem , vol.282 , pp. 16691-16699
    • Zhang, F.1    Strom, A.L.2    Fukada, K.3    Lee, S.4    Hayward, L.J.5    Zhu, H.6
  • 45
    • 0035310832 scopus 로고    scopus 로고
    • Recombinant aequorin and green fluorescent protein as valuable tools in the study of cell signalling
    • Chiesa, A., Rapizzi, E., Tosello, V., Pinton, P., de Virgilio, M., Fogarty, K.E. and Rizzuto, R. (2001) Recombinant aequorin and green fluorescent protein as valuable tools in the study of cell signalling. Biochem. J., 355, 1-12.
    • (2001) Biochem. J , vol.355 , pp. 1-12
    • Chiesa, A.1    Rapizzi, E.2    Tosello, V.3    Pinton, P.4    de Virgilio, M.5    Fogarty, K.E.6    Rizzuto, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.