메뉴 건너뛰기




Volumn 24, Issue 12, 2015, Pages 3427-3439

A cysteine residue affects the conformational state and neuronal toxicity of mutant SOD1 in mice: Relevance to the pathogenesis of ALS

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; THIOREDOXIN; COPPER ZINC SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE;

EID: 84930466683     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv093     Document Type: Article
Times cited : (21)

References (49)
  • 4
    • 0029927679 scopus 로고    scopus 로고
    • Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement
    • Shibata, N., Hirano, A., Kobayashi, M., Siddique, T., Deng, H.X., Hung, W.Y., Kato, T. and Asayama, K. (1996) Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. J. Neuropathol. Exp. Neurol., 55, 481-490.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 481-490
    • Shibata, N.1    Hirano, A.2    Kobayashi, M.3    Siddique, T.4    Deng, H.X.5    Hung, W.Y.6    Kato, T.7    Asayama, K.8
  • 6
    • 66749133370 scopus 로고    scopus 로고
    • Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS
    • Chattopadhyay, M. and Valentine, J.S. (2009) Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS. Antioxid. Redox Signal, 11, 1603-1614.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 1603-1614
    • Chattopadhyay, M.1    Valentine, J.S.2
  • 7
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine, J.S., Doucette, P.A. and Zittin Potter, S. (2005) Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem., 74, 563-593.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 8
    • 84883674898 scopus 로고    scopus 로고
    • The redox biochemistry of protein sulfenylation and sulfinylation
    • Lo Conte, M. and Carroll, K.S. (2013) The redox biochemistry of protein sulfenylation and sulfinylation. J. Biol. Chem., 288, 26480-26488.
    • (2013) J. Biol. Chem. , vol.288 , pp. 26480-26488
    • Lo Conte, M.1    Carroll, K.S.2
  • 9
    • 20444504724 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo-and reduced form of SOD1, leading to unfolding and oxidative aggregation
    • Furukawa, Y. and O'Halloran, T.V. (2005) Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo-and reduced form of SOD1, leading to unfolding and oxidative aggregation. J. Biol. Chem., 280, 17266-17274.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17266-17274
    • Furukawa, Y.1    O'Halloran, T.V.2
  • 10
    • 8644290067 scopus 로고    scopus 로고
    • Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers
    • Lindberg, M.J., Normark, J., Holmgren, A. and Oliveberg, M. (2004) Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers. Proc. Natl Acad. Sci. USA, 101, 15893-15898.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15893-15898
    • Lindberg, M.J.1    Normark, J.2    Holmgren, A.3    Oliveberg, M.4
  • 12
  • 13
    • 67649407767 scopus 로고    scopus 로고
    • Modifications of superoxide dismutase (SOD1) in human erythrocytes:a possible role in amyotrophic lateral sclerosis
    • Wilcox, K.C., Zhou, L., Jordon, J.K., Huang, Y., Yu, Y., Redler, R. L., Chen, X., Caplow, M. and Dokholyan, N.V. (2009) Modifications of superoxide dismutase (SOD1) in human erythrocytes:a possible role in amyotrophic lateral sclerosis. J. Biol. Chem., 284, 13940-13947.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13940-13947
    • Wilcox, K.C.1    Zhou, L.2    Jordon, J.K.3    Huang, Y.4    Yu, Y.5    Redler, R.L.6    Chen, X.7    Caplow, M.8    Dokholyan, N.V.9
  • 14
    • 77249126861 scopus 로고    scopus 로고
    • Monomerized Cu, Zn-superoxide dismutase induces oxidative stress through aberrant Cu binding
    • Kishigami, H., Nagano, S., Bush, A.I. and Sakoda, S. (2010) Monomerized Cu, Zn-superoxide dismutase induces oxidative stress through aberrant Cu binding. Free Radic. Biol. Med., 48, 945-952.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 945-952
    • Kishigami, H.1    Nagano, S.2    Bush, A.I.3    Sakoda, S.4
  • 15
    • 80051503291 scopus 로고    scopus 로고
    • Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers
    • Redler, R.L.,Wilcox, K.C., Proctor, E.A., Fee, L., Caplow, M. and Dokholyan, N.V. (2011) Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers. Biochemistry, 50, 7057-7066.
    • (2011) Biochemistry , vol.50 , pp. 7057-7066
    • Redler, R.L.1    Wilcox, K.C.2    Proctor, E.A.3    Fee, L.4    Caplow, M.5    Dokholyan, N.V.6
  • 16
    • 84888218077 scopus 로고    scopus 로고
    • Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis
    • McAlary, L., Yerbury, J.J. and Aquilina, J.A. (2013) Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis. Sci. Rep., 3, 3275.
    • (2013) Sci. Rep. , vol.3 , pp. 3275
    • McAlary, L.1    Yerbury, J.J.2    Aquilina, J.A.3
  • 17
    • 0037458564 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction
    • Tiwari, A. and Hayward, L.J. (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
  • 18
    • 23844471242 scopus 로고    scopus 로고
    • Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis
    • Tiwari, A., Xu, Z. and Hayward, L.J. (2005) Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis. J. Biol. Chem., 280, 29771-29779.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29771-29779
    • Tiwari, A.1    Xu, Z.2    Hayward, L.J.3
  • 20
    • 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
  • 21
    • 33646486372 scopus 로고    scopus 로고
    • Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice
    • Furukawa, Y., Fu, R., Deng, H.X., Siddique, T. and O'Halloran, T.V. (2006) Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. Proc. Natl Acad. Sci. USA, 103, 7148-7153.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 7148-7153
    • Furukawa, Y.1    Fu, R.2    Deng, H.X.3    Siddique, T.4    O'Halloran, T.V.5
  • 22
    • 84874086845 scopus 로고    scopus 로고
    • Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis
    • Toichi, K., Yamanaka, K. and Furukawa, Y. (2013) Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. J. Biol. Chem., 288, 4970-4980.
    • (2013) J. Biol. Chem. , vol.288 , pp. 4970-4980
    • Toichi, K.1    Yamanaka, K.2    Furukawa, Y.3
  • 23
    • 84885443699 scopus 로고    scopus 로고
    • Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation
    • Leinartaite, L. and Johansson, A.S. (2013) Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation. PLoS ONE, 8, e78060.
    • (2013) PLoS ONE , vol.8 , pp. e78060
    • Leinartaite, L.1    Johansson, A.S.2
  • 24
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
    • Niwa, J., Yamada, S., Ishigaki, S., Sone, J., Takahashi, M., Katsuno, M., Tanaka, F., Doyu, M. and 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.1    Yamada, S.2    Ishigaki, S.3    Sone, J.4    Takahashi, M.5    Katsuno, M.6    Tanaka, F.7    Doyu, M.8    Sobue, G.9
  • 25
    • 38149115471 scopus 로고    scopus 로고
    • Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • Cozzolino, M., Amori, I., Pesaresi, M.G., Ferri, A., Nencini, M. and Carri, M.T. (2008) Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis. J. Biol. Chem., 283, 866-874.
    • (2008) J. Biol. Chem. , vol.283 , pp. 866-874
    • Cozzolino, M.1    Amori, I.2    Pesaresi, M.G.3    Ferri, A.4    Nencini, M.5    Carri, M.T.6
  • 26
    • 34247125547 scopus 로고    scopus 로고
    • Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis
    • Watanabe, S., Nagano, S., Duce, J., Kiaei, M., Li, Q.X., Tucker, S. M., Tiwari, A., Brown, R.H. Jr., Beal, M.F., Hayward, L.J. et al. (2007) Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis. Free Radic. Biol. Med., 42, 1534-1542.
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 1534-1542
    • Watanabe, S.1    Nagano, S.2    Duce, J.3    Kiaei, M.4    Li, Q.X.5    Tucker, S.M.6    Tiwari, A.7    Brown, R.H.8    Beal, M.F.9    Hayward, L.J.10
  • 28
    • 0025197660 scopus 로고
    • Background pathology in BDF1 mice allowed to live out their lifespan
    • Yamate, J., Tajima, M., Kudow, S. and Sannai, S. (1990) Background pathology in BDF1 mice allowed to live out their lifespan. Lab. Anim., 24, 332-340.
    • (1990) Lab. Anim. , vol.24 , pp. 332-340
    • Yamate, J.1    Tajima, M.2    Kudow, S.3    Sannai, S.4
  • 29
    • 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. and Brown, R.H. Jr. (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, R.H.8
  • 32
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • Urushitani, M., Ezzi, S.A. and Julien, J.P. (2007) Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc. Natl Acad. Sci. USA, 104, 2495-2500.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2495-2500
    • Urushitani, M.1    Ezzi, S.A.2    Julien, J.P.3
  • 33
    • 77951924183 scopus 로고    scopus 로고
    • Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS
    • Gros-Louis, F., Soucy, G., Lariviere, R. and Julien, J.P. (2010) Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS. J. Neurochem., 113, 1188-1199.
    • (2010) J. Neurochem. , vol.113 , pp. 1188-1199
    • Gros-Louis, F.1    Soucy, G.2    Lariviere, R.3    Julien, J.P.4
  • 34
    • 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. and 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
  • 35
    • 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. and 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
  • 42
    • 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. and 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
  • 43
    • 84862862329 scopus 로고    scopus 로고
    • Oxidative modification of cysteine 111 promotes disulfide bond-independent aggregation of SOD1
    • Chen, X., Shang, H., Qiu, X., Fujiwara, N., Cui, L., Li, X.M., Gao, T.M. and Kong, J. (2012) Oxidative modification of cysteine 111 promotes disulfide bond-independent aggregation of SOD1. Neurochem. Res., 37, 835-845.
    • (2012) Neurochem. Res. , vol.37 , pp. 835-845
    • Chen, X.1    Shang, H.2    Qiu, X.3    Fujiwara, N.4    Cui, L.5    Li, X.M.6    Gao, T.M.7    Kong, J.8
  • 45
    • 84859573746 scopus 로고    scopus 로고
    • A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo
    • Prudencio, M., Lelie, H., Brown, H.H., Whitelegge, J.P., Valentine, J.S. and Borchelt, D.R. (2012) A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo. J. Neurochem., 121, 475-485.
    • (2012) J. Neurochem. , vol.121 , pp. 475-485
    • Prudencio, M.1    Lelie, H.2    Brown, H.H.3    Whitelegge, J.P.4    Valentine, J.S.5    Borchelt, D.R.6
  • 46
    • 0026711256 scopus 로고
    • Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase
    • Parge, H.E., Hallewell, R.A. and Tainer, J.A. (1992) Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl Acad. Sci. USA, 89, 6109-6113.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6109-6113
    • Parge, H.E.1    Hallewell, R.A.2    Tainer, J.A.3
  • 49
    • 0015153416 scopus 로고
    • Superoxide dismutase:improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C. and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.