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Volumn 25, Issue 10, 2005, Pages 2463-2470

Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice

Author keywords

Aggregation; ALS; Amyotrophic lateral sclerosis; Brain; Matrix; Mitochondria; SOD1

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 14944385595     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4385-04.2005     Document Type: Article
Times cited : (209)

References (38)
  • 1
  • 2
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44:276-287.
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 7
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham HD, Roy J, Dong L, Figlewicz DA (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J Neuropathol Exp Neurol 56:523-530.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 8
    • 0025616225 scopus 로고
    • Hepatocyte differentiation and liver progenitor cells
    • Fausto N (1990) Hepatocyte differentiation and liver progenitor cells. Curr Opin Cell Biol 2:1036-1042.
    • (1990) Curr Opin Cell Biol , vol.2 , pp. 1036-1042
    • Fausto, N.1
  • 9
    • 0041344579 scopus 로고    scopus 로고
    • Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria
    • Field LS, Furukawa Y, O'Halloran TV, Culotta VC (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J Biol Chem 278:28052-28059.
    • (2003) J Biol Chem , vol.278 , pp. 28052-28059
    • Field, L.S.1    Furukawa, Y.2    O'Halloran, T.V.3    Culotta, V.C.4
  • 10
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y, Hubbard AL, Fowler S, Lazarow PB (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J Cell Biol 93:97-102.
    • (1982) J Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 12
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Hayward LJ, Rodriguez JA, Kim JW, Tiwari A, Goto JJ, Cabelli DE, Valentine JS, Brown Jr RH (2002) Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. J Biol Chem 277:15923-15931.
    • (2002) J Biol Chem , vol.277 , 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 Jr., R.H.8
  • 13
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • 1-6
    • Higgins CM, Jung C, Ding H, Xu Z (2002) Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J Neurosci 22:RC215(1-6).
    • (2002) J Neurosci , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 14
    • 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 CM, Jung C, 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
  • 15
    • 0034520591 scopus 로고    scopus 로고
    • Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1
    • Jaarsma D, Haasdijk ED, Grashorn JA, Hawkins R, van Duijn W, Verspaget HW, London J, Holstege JC (2000) Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1. Neurobiol Dis 7:623-643.
    • (2000) Neurobiol Dis , vol.7 , pp. 623-643
    • Jaarsma, D.1    Haasdijk, E.D.2    Grashorn, J.A.3    Hawkins, R.4    Van Duijn, W.5    Verspaget, H.W.6    London, J.7    Holstege, J.C.8
  • 16
    • 0034821922 scopus 로고    scopus 로고
    • CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations
    • Berl
    • Jaarsma D, Rognoni F, van Duijn W, Verspaget HW, Haasdijk ED, Holstege JC (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 , 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
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston JA, Dalton MJ, Gurney ME, Kopito RR (2000) Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 97:12571-12576.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 18
    • 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 CM, 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
  • 19
    • 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
    • Koide T, Igarashi S, Kikugawa K, Nakano R, Inuzuka T, Yamada M, Takahashi H, Tsuji S (1998) Formation of granular cytoplasmic aggregates in COS7 cells expressing mutant Cu/Zn superoxide dismutase associated with familial amyotrophic lateral sclerosis. Neurosci Lett 257:29-32.
    • (1998) Neurosci Lett , 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
  • 22
    • 0028234557 scopus 로고
    • Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion
    • Millar DG, Shore GC (1994) Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion. J Biol Chem 269:12229-12232.
    • (1994) J Biol Chem , vol.269 , pp. 12229-12232
    • Millar, D.G.1    Shore, G.C.2
  • 23
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A, 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
  • 24
    • 0037173038 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: A proposed mechanism
    • Okado-Matsumoto A, Fridovich I (2002) Amyotrophic lateral sclerosis: a proposed mechanism. Proc Natl Acad Sci USA 99:9010-9014.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9010-9014
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 25
    • 0035227198 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from animal cells and tissue culture lines
    • Pallotti F, Lenaz G (2001) Isolation and subfractionation of mitochondria from animal cells and tissue culture lines. Methods Cell Biol 65:1-35.
    • (2001) Methods Cell Biol , vol.65 , pp. 1-35
    • Pallotti, F.1    Lenaz, G.2
  • 26
    • 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 ME, Lennon N, Bacskai BJ, Hyman BT, Trotti D, Brown Jr RH (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
  • 27
    • 0023645869 scopus 로고
    • The carboxyl-terminal two-thirds of the ADP/ATP carrier polypeptide contains sufficient information to direct translocation into mitochondria
    • Pfanner N, Hoeben P, Tropschug M, Neupert W (1987) The carboxyl-terminal two-thirds of the ADP/ATP carrier polypeptide contains sufficient information to direct translocation into mitochondria. J Biol Chem 262:14851-14854.
    • (1987) J Biol Chem , vol.262 , pp. 14851-14854
    • Pfanner, N.1    Hoeben, P.2    Tropschug, M.3    Neupert, W.4
  • 28
    • 0032815965 scopus 로고    scopus 로고
    • Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds
    • Ratovitski T, Corson LB, Strain J, Wong P, Cleveland DW, Culotta VC, Borchelt DR (1999) Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds. Hum Mol Genet 8:1451-1460.
    • (1999) Hum Mol Genet , vol.8 , pp. 1451-1460
    • Ratovitski, T.1    Corson, L.B.2    Strain, J.3    Wong, P.4    Cleveland, D.W.5    Culotta, V.C.6    Borchelt, D.R.7
  • 31
    • 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 LA, Diekert K, Jensen LT, Lill R, Culotta VC (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
  • 33
    • 0037458564 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction
    • Tiwari A, Hayward LJ (2003) Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction. J Biol Chem 278:5984-5992.
    • (2003) J Biol Chem , vol.278 , pp. 5984-5992
    • Tiwari, A.1    Hayward, L.J.2
  • 34
    • 0036199623 scopus 로고    scopus 로고
    • High molecular weight complexes of mutant superoxide dismutase 1: Age-dependent and tissue-specific accumulation
    • Wang J, Xu G, Borchelt DR (2002) High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. Neurobiol Dis 9:139-148.
    • (2002) Neurobiol Dis , vol.9 , pp. 139-148
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 35
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD (2001) Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis 8:933-941.
    • (2001) Neurobiol Dis , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 36
    • 0015848173 scopus 로고
    • Superoxide dismutase. Organelle specificity
    • Weisiger RA, 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
  • 37
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, Price DL (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
  • 38
    • 0030298544 scopus 로고    scopus 로고
    • Isolation, mapping, and genomic structure of an X-linked gene for a subunit of human mitochondrial complex I
    • Zhuchenko O, Wehnert M, Bailey J, Sun ZS, Lee CC (1996) Isolation, mapping, and genomic structure of an X-linked gene for a subunit of human mitochondrial complex I. Genomics 37:281-288.
    • (1996) Genomics , vol.37 , pp. 281-288
    • Zhuchenko, O.1    Wehnert, M.2    Bailey, J.3    Sun, Z.S.4    Lee, C.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.