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Volumn 114, Issue 2, 2010, Pages 408-418

Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice

Author keywords

amyotrophic lateral sclerosis; endoplasmic reticulum; inclusion; proteomics; superoxide dismutase 1; transgenic mice

Indexed keywords

CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOSKELETON PROTEIN; OLIGOMER;

EID: 77953832329     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06753.x     Document Type: Article
Times cited : (36)

References (52)
  • 2
    • 0038446777 scopus 로고    scopus 로고
    • Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: A decade of discoveries, defects and disputes
    • Andersen P. M., Sims K. B., Xin W. W. et al. (2003) Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes. Amyotroph. Lateral Scler. Other Motor Neuron Disord. 4, 1 12.
    • (2003) Amyotroph. Lateral Scler. Other Motor Neuron Disord. , vol.4 , pp. 1-12
    • Andersen, P.M.1    Sims, K.B.2    Xin, W.W.3
  • 3
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin J. D., Farg M. A., Turner B. J. et al. (2006) Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem. 281, 30152 30165.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3
  • 4
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin J. D., Farg M. A., Walker A. K., McLean C., Tomas D. Horne M. K. (2008) Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol. Dis. 30, 400 407.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5    Horne, M.K.6
  • 7
    • 77949505299 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis
    • Basso M., Samengo G., Nardo G. et al. (2009) Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis. PLoS ONE 4, e8130.
    • (2009) PLoS ONE , vol.4 , pp. 8130
    • Basso, M.1    Samengo, G.2    Nardo, G.3
  • 8
    • 33646452761 scopus 로고    scopus 로고
    • Overloading of stable and exclusion of unstable human superoxide dismutase-1 variants in mitochondria of murine amyotrophic lateral sclerosis models
    • Bergemalm D., Jonsson P. A., Graffmo K. S., Andersen P. M., Brannstrom T., Rehnmark A. Marklund S. L. (2006) Overloading of stable and exclusion of unstable human superoxide dismutase-1 variants in mitochondria of murine amyotrophic lateral sclerosis models. J. Neurosci. 26, 4147 4154.
    • (2006) J. Neurosci. , vol.26 , pp. 4147-4154
    • Bergemalm, D.1    Jonsson, P.A.2    Graffmo, K.S.3    Andersen, P.M.4    Brannstrom, T.5    Rehnmark, A.6    Marklund, S.L.7
  • 11
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn L. I., Becher M. W., Lee M. K. et al. (1997) ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18, 327 338.
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1    Becher, M.W.2    Lee, M.K.3
  • 13
    • 4344703472 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with mutant Cu/Zn-superoxide dismutase proteins linked to familial amyotrophic lateral sclerosis and promotes their degradation by proteasomes
    • Choi J. S., Cho S., Park S. G., Park B. C. Lee D. H. (2004) Co-chaperone CHIP associates with mutant Cu/Zn-superoxide dismutase proteins linked to familial amyotrophic lateral sclerosis and promotes their degradation by proteasomes. Biochem. Biophys. Res. Commun. 321, 574 583.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 574-583
    • Choi, J.S.1    Cho, S.2    Park, S.G.3    Park, B.C.4    Lee, D.H.5
  • 14
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in familial form of ALS
    • Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T. V. Nukina N. (2008) Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in familial form of ALS. J. Biol. Chem. 283, 24167 24176.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24167-24176
    • Furukawa, Y.1    Kaneko, K.2    Yamanaka, K.3    O'Halloran, T.V.4    Nukina, N.5
  • 16
    • 0029037348 scopus 로고
    • Natural history of amyotrophic lateral sclerosis in a database population. Validation of a scoring system and a model for survival prediction
    • Haverkamp L. J., Appel V. Appel S. H. (1995) Natural history of amyotrophic lateral sclerosis in a database population. Validation of a scoring system and a model for survival prediction. Brain 118, 707 719.
    • (1995) Brain , vol.118 , pp. 707-719
    • Haverkamp, L.J.1    Appel, V.2    Appel, S.H.3
  • 18
    • 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 J. A., Dalton M. J., Gurney M. E. Kopito R. R. (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
  • 22
    • 44849090909 scopus 로고    scopus 로고
    • Inclusions of amyotrophic lateral sclerosis-linked superoxide dismutase in ventral horns, liver, and kidney
    • Jonsson P. A., Bergemalm D., Andersen P. M., Gredal O., Brannstrom T. Marklund S. L. (2008) Inclusions of amyotrophic lateral sclerosis-linked superoxide dismutase in ventral horns, liver, and kidney. Ann. Neurol. 63, 671 675.
    • (2008) Ann. Neurol. , vol.63 , pp. 671-675
    • Jonsson, P.A.1    Bergemalm, D.2    Andersen, P.M.3    Gredal, O.4    Brannstrom, T.5    Marklund, S.L.6
  • 23
    • 46649096661 scopus 로고    scopus 로고
    • A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis
    • Karch C. M. Borchelt D. R. (2008) A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. J. Biol. Chem. 283, 13528 13537.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13528-13537
    • Karch, C.M.1    Borchelt, D.R.2
  • 24
    • 66049156169 scopus 로고    scopus 로고
    • Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
    • Karch C. M., Prudencio M., Winkler D. D., Hart P. J. Borchelt D. R. (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc. Natl Acad. Sci. USA 106, 7774 7779.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7774-7779
    • Karch, C.M.1    Prudencio, M.2    Winkler, D.D.3    Hart, P.J.4    Borchelt, D.R.5
  • 25
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D., Kalmar B., Dick J. R., Riddoch-Contreras J., Burnstock G. Greensmith L. (2004) Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10, 402 405.
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 27
    • 3242701496 scopus 로고    scopus 로고
    • Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria
    • Liu J., Lillo C., Jonsson P. A. et al. (2004) Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria. Neuron 43, 5 17.
    • (2004) Neuron , vol.43 , pp. 5-17
    • Liu, J.1    Lillo, C.2    Jonsson, P.A.3
  • 29
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
    • Niwa J. I., Yamada S. I., Ishigaki S., Sone J., Takahashi M., Katsuno M., Tanaka F., Doyu M. Sobue G. (2007) Disulfide bond mediates aggregation, toxicity and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J. Biol. Chem. 282, 28087 28095.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28087-28095
    • Niwa, J.I.1    Yamada, S.I.2    Ishigaki, S.3    Sone, J.4    Takahashi, M.5    Katsuno, M.6    Tanaka, F.7    Doyu, M.8    Sobue, G.9
  • 30
    • 63449092530 scopus 로고    scopus 로고
    • Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase
    • Oztug Durer Z. A., Cohlberg J. A., Dinh P. et al. (2009) Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. PLoS ONE 4, e5004.
    • (2009) PLoS ONE , vol.4 , pp. 5004
    • Oztug Durer, Z.A.1    Cohlberg, J.A.2    Dinh, P.3
  • 31
    • 27744542191 scopus 로고    scopus 로고
    • No widespread induction of cell death genes occurs in pure motoneurons in an amyotrophic lateral sclerosis mouse model
    • Perrin F. E., Boisset G., Docquier M., Schaad O., Descombes P. Kato A. C. (2005) No widespread induction of cell death genes occurs in pure motoneurons in an amyotrophic lateral sclerosis mouse model. Hum. Mol. Genet. 14, 3309 3320.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3309-3320
    • Perrin, F.E.1    Boisset, G.2    Docquier, M.3    Schaad, O.4    Descombes, P.5    Kato, A.C.6
  • 32
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan R. S., Illing M. E., Bence N. F. Kopito R. R. (2001) Specificity in intracellular protein aggregation and inclusion body formation. Proc. Natl Acad. Sci. USA 98, 13060 13065.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.R.4
  • 33
    • 58149102066 scopus 로고    scopus 로고
    • The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1
    • Reddehase S., Grumbt B., Neupert W. Hell K. (2009) The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1. J. Mol. Biol. 385, 331 338.
    • (2009) J. Mol. Biol. , vol.385 , pp. 331-338
    • Reddehase, S.1    Grumbt, B.2    Neupert, W.3    Hell, K.4
  • 34
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide-dismutase gene are associated with familial amyotrophic-lateral-sclerosis
    • Rosen D. R., Siddique T., Patterson D. et al. (1993) Mutations in Cu/Zn superoxide-dismutase gene are associated with familial amyotrophic-lateral- sclerosis. Nature 362, 59 62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 35
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena S., Cabuy E. Caroni P. (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci. 12, 627 636.
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 37
    • 43749109844 scopus 로고    scopus 로고
    • Detergent insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1
    • Shaw B. F., Lelie H. L., Durazo A. et al. (2008) Detergent insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. J. Biol. Chem. 283, 8340 8350.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8340-8350
    • Shaw, B.F.1    Lelie, H.L.2    Durazo, A.3
  • 38
    • 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 H. D. (2001) 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, 12791 12796.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4
  • 39
    • 65249112094 scopus 로고    scopus 로고
    • Alternative splicing studies of the reactive oxygen species gene network in Populus reveal two isoforms of high-isoelectric-point superoxide dismutase
    • Srivastava V., Srivastava M. K., Chibani K., Nilsson R., Rouhier N., Melzer M. Wingsle G. (2009) Alternative splicing studies of the reactive oxygen species gene network in Populus reveal two isoforms of high-isoelectric-point superoxide dismutase. Plant Physiol. 149, 1848 1859.
    • (2009) Plant Physiol. , vol.149 , pp. 1848-1859
    • Srivastava, V.1    Srivastava, M.K.2    Chibani, K.3    Nilsson, R.4    Rouhier, N.5    Melzer, M.6    Wingsle, G.7
  • 41
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • Turner B. J., Atkin J. D., Farg M. A., Zang d. W., Rembach A., Lopes E. C., Patch J. D., Hill A. F. Cheema S. S. (2005) Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J. Neurosci. 25, 108 117.
    • (2005) J. Neurosci. , vol.25 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3    Zang, D.W.4    Rembach, A.5    Lopes, E.C.6    Patch, J.D.7    Hill, A.F.8    Cheema, S.S.9
  • 42
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani M., Sik A., Sakurai T., Nukina N., Takahashi R. Julien J. P. (2006) Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci. 9, 108 118.
    • (2006) Nat. Neurosci. , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.P.6
  • 43
    • 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. 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
  • 44
    • 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. 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
  • 45
    • 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 D. R. (2002a) 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
  • 46
    • 0036076642 scopus 로고    scopus 로고
    • Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site
    • Wang J., Xu G., Gonzales V., Coonfield M., Fromholt D., Copeland N. G., Jenkins N. A. Borchelt D. R. (2002b) Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site. Neurobiol. Dis. 10, 128 138.
    • (2002) Neurobiol. Dis. , vol.10 , pp. 128-138
    • Wang, J.1    Xu, G.2    Gonzales, V.3    Coonfield, M.4    Fromholt, D.5    Copeland, N.G.6    Jenkins, N.A.7    Borchelt, D.R.8
  • 48
    • 26444542945 scopus 로고    scopus 로고
    • Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: AlphaB-crystallin modulates aggregation
    • Wang J., Xu G., Li H., Gonzales V., Fromholt D., Karch C., Copeland N. G., Jenkins N. A. Borchelt D. R. (2005) Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: alphaB-crystallin modulates aggregation. Hum. Mol. Genet. 14, 2335 2347.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2335-2347
    • Wang, J.1    Xu, G.2    Li, H.3    Gonzales, V.4    Fromholt, D.5    Karch, C.6    Copeland, N.G.7    Jenkins, N.A.8    Borchelt, D.R.9
  • 49
    • 60849126687 scopus 로고    scopus 로고
    • Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS
    • Wang J., Farr G. W., Zeiss C. J. et al. (2009) Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS. Proc. Natl Acad. Sci. USA 106, 1392 1397.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1392-1397
    • Wang, J.1    Farr, G.W.2    Zeiss, C.J.3
  • 50
    • 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 V. C., Price D. L., Wong P. C. Rothstein J. D. (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
  • 51
    • 28844507918 scopus 로고    scopus 로고
    • Expression of an endoplasmic reticulum-resident chaperone, glucose-regulated stress protein 78, in the spinal cord of a mouse model of amyotrophic lateral sclerosis
    • Wate R., Ito H., Zhang J. H., Ohnishi S., Nakano S. Kusaka H. (2005) Expression of an endoplasmic reticulum-resident chaperone, glucose-regulated stress protein 78, in the spinal cord of a mouse model of amyotrophic lateral sclerosis. Acta Neuropathol. 110, 557 562.
    • (2005) Acta Neuropathol. , vol.110 , pp. 557-562
    • Wate, R.1    Ito, H.2    Zhang, J.H.3    Ohnishi, S.4    Nakano, S.5    Kusaka, H.6


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