메뉴 건너뛰기




Volumn 128, Issue 2, 2014, Pages 305-314

Distinctive features of the D101N and D101G variants of superoxide dismutase 1; Two mutations that produce rapidly progressing motor neuron disease

Author keywords

aggregation; ALS; oxidation; SOD1; stability

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 84891824614     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.12451     Document Type: Article
Times cited : (17)

References (32)
  • 1
    • 0346364657 scopus 로고    scopus 로고
    • Amino acid properties and consequences of substitutions
    • in (Barnes M. R. and Gray I. C. eds.), Wiley, Hoboken, NJ.
    • Betts M. J., and, Russell R. B,. (2003) Amino acid properties and consequences of substitutions,in Bioinformatics for geneticists (, Barnes M. R., and, Gray I. C., eds.), pp. 289-316. Wiley, Hoboken, NJ.
    • (2003) Bioinformatics for Geneticists , pp. 289-316
    • Betts, M.J.1    Russell, R.B.2
  • 2
    • 0027965073 scopus 로고
    • Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
    • Borchelt D. R., Lee M. K., Slunt H. S., et al,. (1994) Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl Acad. Sci. USA 91, 8292-8296.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8292-8296
    • Borchelt, D.R.1    Lee, M.K.2    Slunt, H.S.3
  • 3
    • 0028813380 scopus 로고
    • Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function
    • Borchelt D. R., Guarnieri M., Wong P. C., Lee M. K., Slunt H. S., Xu Z. S., Sisodia S. S., Price D. L., and, Cleveland D. W., (1995) Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J. Biol. Chem. 270, 3234-3238.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3234-3238
    • Borchelt, D.R.1    Guarnieri, M.2    Wong, P.C.3    Lee, M.K.4    Slunt, H.S.5    Xu, Z.S.6    Sisodia, S.S.7    Price, D.L.8    Cleveland, D.W.9
  • 4
    • 0032126386 scopus 로고    scopus 로고
    • Axonal transport of mutant superoxide dismutase 1 and focal axonal abnormalities in the proximal axons of transgenic mice
    • Borchelt D. R., Wong P. C., Becher M. W., et al,. (1998) Axonal transport of mutant superoxide dismutase 1 and focal axonal abnormalities in the proximal axons of transgenic mice. Neurobiol. Dis. 5, 27-35.
    • (1998) Neurobiol. Dis. , vol.5 , pp. 27-35
    • Borchelt, D.R.1    Wong, P.C.2    Becher, M.W.3
  • 6
    • 33846978054 scopus 로고    scopus 로고
    • Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants
    • Bruns C. K., and, Kopito R. R., (2007) Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants. EMBO J. 26, 855-866.
    • (2007) EMBO J. , vol.26 , pp. 855-866
    • Bruns, C.K.1    Kopito, R.R.2
  • 7
    • 77953532917 scopus 로고    scopus 로고
    • SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability
    • Bystrom R., Andersen P. M., Grobner G., and, Oliveberg M., (2010) SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability. J. Biol. Chem. 285, 19544-19552.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19544-19552
    • Bystrom, R.1    Andersen, P.M.2    Grobner, G.3    Oliveberg, M.4
  • 8
    • 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
  • 10
    • 0030810921 scopus 로고    scopus 로고
    • Intrathecal administration of recombinant human superoxide dismutase 1 in amyotrophic lateral sclerosis: A preliminary safety and pharmacokinetic study
    • Cudkowicz M. E., Warren L., Francis J. W., Lloyd K. J., Friedlander R. M., Borges L. F., Kassem N., Munsat T. L., and, Brown R. H., Jr, (1997) Intrathecal administration of recombinant human superoxide dismutase 1 in amyotrophic lateral sclerosis: a preliminary safety and pharmacokinetic study. Neurology 49, 213-222.
    • (1997) Neurology , vol.49 , pp. 213-222
    • Cudkowicz, M.E.1    Warren, L.2    Francis, J.W.3    Lloyd, K.J.4    Friedlander, R.M.5    Borges, L.F.6    Kassem, N.7    Munsat, T.L.8    Brown, Jr.R.H.9
  • 11
    • 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., 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
  • 12
    • 11144227941 scopus 로고    scopus 로고
    • Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability
    • Doucette P. A., Whitson L. J., Cao X., Schirf V., Demeler B., Valentine J. S., Hansen J. C., and, Hart P. J., (2004) Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability. J. Biol. Chem. 279, 54558-54566.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54558-54566
    • Doucette, P.A.1    Whitson, L.J.2    Cao, X.3    Schirf, V.4    Demeler, B.5    Valentine, J.S.6    Hansen, J.C.7    Hart, P.J.8
  • 13
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
    • Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T. V., and, Nukina N., (2008) Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. 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
  • 14
    • 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 E. D., Grashorn J. A., Hawkins R., van Duijn W., Verspaget H. W., London J., and, Holstege J. C., (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
    • 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
  • 17
    • 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
  • 18
    • 78951472170 scopus 로고    scopus 로고
    • Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice
    • Lelie H. L., Liba A., Bourassa M. W., et al,. (2011) Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice. J. Biol. Chem. 286, 2795-2806.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2795-2806
    • Lelie, H.L.1    Liba, A.2    Bourassa, M.W.3
  • 19
    • 34247505040 scopus 로고    scopus 로고
    • Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein
    • Potter S. Z., Zhu H., Shaw B. F., et al,. (2007) Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein. J. Am. Chem. Soc. 129, 4575-4583.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4575-4583
    • Potter, S.Z.1    Zhu, H.2    Shaw, B.F.3
  • 20
    • 81155151484 scopus 로고    scopus 로고
    • Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states
    • Prudencio M., and, Borchelt D. R., (2011) Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states. Mol. Neurodegener. 6, 77.
    • (2011) Mol. Neurodegener. , vol.6 , pp. 77
    • Prudencio, M.1    Borchelt, D.R.2
  • 21
    • 58549087977 scopus 로고    scopus 로고
    • Modulation of mutant superoxide dismutase 1 aggregation by co-expression of wild-type enzyme
    • Prudencio M., Durazo A., Whitelegge J. P., and, Borchelt D. R., (2009a) Modulation of mutant superoxide dismutase 1 aggregation by co-expression of wild-type enzyme. J. Neurochem. 108, 1009-1018.
    • (2009) J. Neurochem. , vol.108 , pp. 1009-1018
    • Prudencio, M.1    Durazo, A.2    Whitelegge, J.P.3    Borchelt, D.R.4
  • 22
    • 68749083546 scopus 로고    scopus 로고
    • Variation in aggregation propensities among ALS-associated variants of SOD1: Correlation to human disease
    • Prudencio M., Hart P. J., Borchelt D. R., and, Andersen P. M., (2009b) Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease. Hum. Mol. Genet. 18, 3217-3226.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3217-3226
    • Prudencio, M.1    Hart, P.J.2    Borchelt, D.R.3    Andersen, P.M.4
  • 23
    • 78649473387 scopus 로고    scopus 로고
    • An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1
    • Prudencio M., Durazo A., Whitelegge J. P., and, Borchelt D. R., (2010) An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Hum. Mol. Genet. 19, 4774-4789.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4774-4789
    • Prudencio, M.1    Durazo, A.2    Whitelegge, J.P.3    Borchelt, D.R.4
  • 24
    • 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
  • 25
    • 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 L. B., Strain J., Wong P., Cleveland D. W., Culotta V. C., and, Borchelt D. R., (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
  • 26
    • 0041367295 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in proteins: Unwanted alterations or surreptitious signals?
    • Reissner K. J., and, Aswad D. W., (2003) Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell. Mol. Life Sci. 60, 1281-1295.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1281-1295
    • Reissner, K.J.1    Aswad, D.W.2
  • 27
    • 23044431627 scopus 로고    scopus 로고
    • Destabilization of apoprotein is insufficient to explain Cu, Zn-superoxide dismutase-linked ALS pathogenesis
    • Rodriguez J. A., Shaw B. F., Durazo A., et al,. (2005) Destabilization of apoprotein is insufficient to explain Cu, Zn-superoxide dismutase-linked ALS pathogenesis. Proc. Natl Acad. Sci. USA 102, 10516-10521.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 10516-10521
    • Rodriguez, J.A.1    Shaw, B.F.2    Durazo, A.3
  • 28
    • 34547120448 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins
    • Sandelin E., Nordlund A., Andersen P. M., Marklund S. S., and, Oliveberg M., (2007) Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins. J. Biol. Chem. 282, 21230-21236.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21230-21236
    • Sandelin, E.1    Nordlund, A.2    Andersen, P.M.3    Marklund, S.S.4    Oliveberg, M.5
  • 30
    • 26244451092 scopus 로고    scopus 로고
    • Coincident thresholds of mutant protein for paralytic disease and protein aggregation caused by restrictively expressed superoxide dismutase cDNA
    • Wang J., Xu G., Slunt H. H., Gonzales V., Coonfield M., Fromholt D., Copeland N. G., Jenkins N. A., and, Borchelt D. R., (2005) Coincident thresholds of mutant protein for paralytic disease and protein aggregation caused by restrictively expressed superoxide dismutase cDNA. Neurobiol. Dis. 20, 943-952.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 943-952
    • Wang, J.1    Xu, G.2    Slunt, H.H.3    Gonzales, V.4    Coonfield, M.5    Fromholt, D.6    Copeland, N.G.7    Jenkins, N.A.8    Borchelt, D.R.9
  • 31
    • 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., and, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.