메뉴 건너뛰기




Volumn 12, Issue 6, 2011, Pages 430-438

Anti-superoxide dismutase antibodies are associated with survival in patients with sporadic amyotrophic later sclerosis

Author keywords

alzheimer's disease; immunotherapy; parkinson's disease; Sporadic amyotrophic lateral sclerosis; superoxide dismutase

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M;

EID: 80055044020     PISSN: 17482968     EISSN: 1471180X     Source Type: Journal    
DOI: 10.3109/17482968.2011.585163     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 78649277728 scopus 로고    scopus 로고
    • Genetic determinants minants of amyotrophic lateral sclerosis as therapeutic targets
    • Bosco DA, Landers JE. Genetic determinants minants of amyotrophic lateral sclerosis as therapeutic targets. CNS Neurol Disord Drug Targets. 2010;9:779-90.
    • (2010) CNS Neurol Disord Drug Targets. , vol.9 , pp. 779-790
    • Bosco, D.A.1    Landers, J.E.2
  • 3
    • 66749133370 scopus 로고    scopus 로고
    • Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS
    • Chattopadhyay M, Valentine JS. Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS. Antioxid Redox Signal. 2009;11:1603-14.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1603-1614
    • Chattopadhyay, M.1    Valentine, J.S.2
  • 4
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • DOI 10.1038/nn1603
    • Urushitani M, Sik A, Sakurai T, Nukina N, Takahashi R, Julien JP. Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat Neurosci. 2006;9:108-18. (Pubitemid 43011916)
    • (2006) Nature Neuroscience , vol.9 , Issue.1 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.-P.6
  • 5
    • 70449417623 scopus 로고    scopus 로고
    • Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
    • Magrane J, Hervias I, Henning MS, Damiano M, Kawamata H, Manfredi G. Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities. Hum Mol Genet. 2009;18:4552-64.
    • (2009) Hum Mol Genet , vol.18 , pp. 4552-4564
    • Magrane, J.1    Hervias, I.2    Henning, M.S.3    Damiano, M.4    Kawamata, H.5    Manfredi, G.6
  • 8
    • 34250177650 scopus 로고    scopus 로고
    • Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation
    • DOI 10.1111/j.1471-4159.2007.04531.x
    • Ezzi SA, Urushitani M, Julien JP. Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation. J Neurochem. 2007;102: 170-8. (Pubitemid 46906269)
    • (2007) Journal of Neurochemistry , vol.102 , Issue.1 , pp. 170-178
    • Ezzi, S.A.1    Urushitani, M.2    Julien, J.-P.3
  • 9
    • 77958519939 scopus 로고    scopus 로고
    • Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
    • Bosco DA, Morfi ni G, Karabacak NM, Song Y, Gros-Louis F, Pasinelli P, et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat Neurosci. 2010;13:1396-403.
    • (2010) Nat Neurosci. , vol.13 , pp. 1396-403
    • Bosco, D.A.1    Morfini, G.2    Karabacak, N.M.3    Song, Y.4    Gros-Louis, F.5    Pasinelli, P.6
  • 11
    • 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, Julien JP. 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. 2010;113: 1188-99.
    • (2010) J Neurochem. , vol.113 , pp. 1188-1199
    • Gros-Louis, F.1    Soucy, G.2    Lariviere, R.3    Julien, J.P.4
  • 12
    • 77957946030 scopus 로고    scopus 로고
    • Induction of protective immunity by vaccination with wild-type apo superoxide dismutase-1 in mutant SOD1 transgenic mice
    • Takeuchi S, Fujiwara N, Ido A, Oono M, Takeuchi Y, Tateno M, et al. Induction of protective immunity by vaccination with wild-type apo superoxide dismutase-1 in mutant SOD1 transgenic mice. J Neuropathol Exp Neurol. 2010;69:1044-56.
    • (2010) J Neuropathol Exp Neurol. , vol.69 , pp. 1044-1056
    • Takeuchi, S.1    Fujiwara, N.2    Ido, A.3    Oono, M.4    Takeuchi, Y.5    Tateno, M.6
  • 13
    • 2142761528 scopus 로고    scopus 로고
    • An Intersubunit Disulfide Bond Prevents in Vitro Aggregation of a Superoxide Dismutase-1 Mutant Linked to Familial Amytrophic Lateral Sclerosis
    • DOI 10.1021/bi030246r
    • Ray SS, Nowak RJ, Strokovich K, Brown RH Jr, Walz T, Lansbury PT Jr. An intersubunit disulfi de bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Biochemistry. 2004; 43:4899-905. (Pubitemid 38544443)
    • (2004) Biochemistry , vol.43 , Issue.17 , pp. 4899-4905
    • Ray, S.S.1    Nowak, R.J.2    Strokovich, K.3    Brown Jr., R.H.4    Walz, T.5    Lansbury Jr., P.T.6
  • 15
    • 0015367077 scopus 로고
    • Enzyme-linked immunosorbent assay, Elisa. 3. Quantitation of specifi c antibodies by enzymelabeled anti-immunoglobulin in antigen-coated tubes
    • Engvall E, Perlmann P. Enzyme-linked immunosorbent assay, Elisa. 3. Quantitation of specifi c antibodies by enzymelabeled anti-immunoglobulin in antigen-coated tubes. J Immunol. 1972;109:129-35.
    • (1972) J Immunol , vol.109 , pp. 129-135
    • Engvall, E.1    Perlmann, P.2
  • 16
    • 0034234565 scopus 로고    scopus 로고
    • Quantitation of the blocking effect of Tween 20 and bovine serum albumin in ELISA microwells
    • DOI 10.1006/abio.2000.4602
    • Steinitz M. Quantitation of the blocking effect of tween 20 and bovine serum albumin in ELISA microwells. Anal Biochem. 2000;282:232-8. (Pubitemid 30439496)
    • (2000) Analytical Biochemistry , vol.282 , Issue.2 , pp. 232-238
    • Steinitz, M.1
  • 17
    • 0032952645 scopus 로고    scopus 로고
    • Complement processing and immunoglobulin binding to Neisseria gonorrhoeae determined in vitro simulates in vivo effects
    • DOI 10.1086/314545
    • McQuillen DP, Gulati S, Ram S, Turner AK, Jani DB, Heeren TC, et al. Complement processing and immunoglobulin binding to Neisseria gonorrhoeae determined in vitro simulates in vivo effects. J Infect Dis. 1999;179: 124-35. (Pubitemid 29028347)
    • (1999) Journal of Infectious Diseases , vol.179 , Issue.1 , pp. 124-135
    • McQuillen, D.P.1    Gulati, S.2    Ram, S.3    Turner, A.K.4    Jani, D.B.5    Heeren, T.C.6    Rice, P.A.7
  • 18
    • 28644432746 scopus 로고    scopus 로고
    • Characterization of a peptide vaccine candidate mimicking an oligosaccharide epitope of Neisseria gonorrhoeae and resultant immune responses and function
    • DOI 10.1016/j.vaccine.2005.07.065, PII S0264410X05007413
    • Ngampasutadol J, Rice PA, Walsh MT, Gulati S. Characterization of a peptide vaccine candidate mimicking an oligosaccharide epitope of Neisseria gonorrhoeae and resultant immune responses and function. Vaccine. 2006;24: 157-70. (Pubitemid 41753003)
    • (2006) Vaccine , vol.24 , Issue.2 , pp. 157-170
    • Ngampasutadol, J.1    Rice, P.A.2    Walsh, M.T.3    Gulati, S.4
  • 19
    • 0021832360 scopus 로고
    • Characterization of antigens from nontypable Haemophilus influenzae recognized by human bactericidal antibodies
    • Gnehm HE, Pelton SI, Gulati S, Rice PA. Characterization of antigens from non-typeable Haemophilus infl uenzae recognized by human bactericidal antibodies. Role of Haemophilus outer membrane proteins. J Clin Invest. 1985;75: 1645-58. (Pubitemid 15039490)
    • (1985) Journal of Clinical Investigation , vol.75 , Issue.5 , pp. 1645-1658
    • Gnehm, H.E.1    Pelton, S.I.2    Gulati, S.3    Rice, P.A.4
  • 20
    • 0023018746 scopus 로고
    • Immunoglobulin G antibodies directed against protein III block killing of serum-resistant Neisseria gonorrhoeae by immune serum
    • DOI 10.1084/jem.164.5.1735
    • Rice PA, Vayo HE, Tam MR, Blake MS. Immunoglobulin G antibodies directed against protein III block killing of serumresistant Neisseria gonorrhoeae by immune serum. J Exp Med. 1986;164:1735-48. (Pubitemid 17184201)
    • (1986) Journal of Experimental Medicine , vol.164 , Issue.5 , pp. 1735-1748
    • Rice, P.A.1    Vayo, H.E.2    Tam, M.R.3    Blake, M.S.4
  • 21
    • 80055036741 scopus 로고    scopus 로고
    • Software CS, editor. Cambridge: MA
    • Mehta C, Patel N. StatXact8. In: Software CS, editor. Cambridge: MA; 2008.
    • (2008) StatXact8
    • Mehta, C.1    Patel, N.2
  • 22
    • 42649123314 scopus 로고    scopus 로고
    • Mechanism and regulation of class switch recombination
    • DOI 10.1146/annurev.immunol.26.021607.090248
    • Stavnezer J, Guikema JE, Schrader CE. Mechanism and regulation of class switch recombination. Annu Rev Immunol. 2008;26:261-92. (Pubitemid 351600377)
    • (2008) Annual Review of Immunology , vol.26 , pp. 261-292
    • Stavnezer, J.1    Guikema, J.E.J.2    Schrader, C.E.3
  • 23
    • 0004250845 scopus 로고    scopus 로고
    • Knipe DM, Howley PM editors 5th edn. Philidelphia: Lippincott Williams and Wilkins;
    • Knipe DM, Howley PM. In: Knipe DM, Howley PM, editors. Fields Virology. 5th edn. Philidelphia: Lippincott, Williams and Wilkins; 2007.
    • (2007) Fields Virology
    • Knipe, D.M.1    Howley, P.M.2
  • 24
    • 0021809173 scopus 로고
    • Amyotrophic lateral sclerosis: Part I. Clinical features, pathology, and ethical issues in management
    • DOI 10.1002/ana.410180302
    • Tandan R, Bradley WG. Amyotrophic lateral sclerosis: Part 1 Clinical features, pathology, and ethical issues in management. Ann Neurol. 1985;18:271-80. (Pubitemid 15023099)
    • (1985) Annals of Neurology , vol.18 , Issue.3 , pp. 271-280
    • Tandan, R.1    Bradley, W.G.2
  • 26
    • 71749117373 scopus 로고    scopus 로고
    • Metal-free superoxide dismutase-1 and three different ALS variants share a similar partially unfolded {beta}-barrel at physiological temperature
    • Durazo A, Shaw BF, Chattopadhyay M, Faull KF, Nersissian AM, Valentine JS, et al. Metal-free superoxide dismutase-1 and three different ALS variants share a similar partially unfolded {beta}-barrel at physiological temperature. J Biol Chem. 2009;284:34382-9.
    • (2009) J Biol Chem , vol.284 , pp. 34382-9
    • Durazo, A.1    Shaw, B.F.2    Chattopadhyay, M.3    Faull, K.F.4    Nersissian, A.M.5    Valentine, J.S.6
  • 27
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-defi cient superoxide dismutase
    • Estevez AG, Crow JP, Sampson JB, Reiter C, Zhuang Y, Richardson GJ, et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-defi cient superoxide dismutase. Science. 1999;286:2498-500.
    • (1999) Science , vol.286 , pp. 2498-500
    • Estevez, A.G.1    Crow, J.P.2    Sampson, J.B.3    Reiter, C.4    Zhuang, Y.5    Richardson, G.J.6
  • 29
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu,Zn-superoxide Dismutase Is a Common Misfolding Intermediate in the Oxidation Models of Sporadic and Familial Amyotrophic Lateral Sclerosis
    • DOI 10.1074/jbc.M313295200
    • Rakhit R, Crow JP, Lepock JR, Kondejewski LH, Cashman NR, Chakrabartty A. Monomeric Cu/Zn superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. J Biol Chem. 2004;279:15499-504. (Pubitemid 38618950)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6
  • 30
    • 0036373780 scopus 로고    scopus 로고
    • Cuzn-superoxide dismutase in human thymus: Immunocytochemical localisation and secretion in thymus-derived epithelial and fibroblast cell lines
    • Cimini V, Ruggiero G, Buonomo T, Seru R, Sciorio S, Zanzi C, et al. Cu/Zn superoxide dismutase in human thymus: immunocytochemical localization and secretion in thymusderived epithelial and fi broblast cell lines. Histochem Cell Biol. 2002;118:163-9. (Pubitemid 34983973)
    • (2002) Histochemistry and Cell Biology , vol.118 , Issue.2 , pp. 163-169
    • Cimini, V.1    Ruggiero, G.2    Buonomo, T.3    Seru, R.4    Sciorio, S.5    Zanzi, C.6    Santangelo, F.7    Mondola, P.8
  • 31
    • 0037474171 scopus 로고    scopus 로고
    • The Cu,Zn superoxide dismutase in neuroblastoma SK-N-BE cells is exported by a microvesicles dependent pathway
    • DOI 10.1016/S0169-328X(02)00583-1, PII S0169328X02005831
    • Mondola P, Ruggiero G, Seru R, Damiano S, Grimaldi S, Garbi C, et al. The Cu/Zn superoxide dismutase in neuroblastoma SK-N-BE cells is exported by a microvesicles dependent pathway. Brain Res Mol Brain Res. 2003;110: 45-51. (Pubitemid 36165041)
    • (2003) Molecular Brain Research , vol.110 , Issue.1 , pp. 45-51
    • Mondola, P.1    Ruggiero, G.2    Seru, R.3    Damiano, S.4    Grimaldi, S.5    Garbi, C.6    Monda, M.7    Greco, D.8    Santillo, M.9
  • 32
    • 49849094080 scopus 로고    scopus 로고
    • Evidence of compromised blood-spinal cord barrier in early and late symptomatic SOD1 mice modeling ALS
    • Garbuzova-Davis S, Saporta S, Haller E, Kolomey I, Bennett SP, Potter H, et al. Evidence of compromised blood-spinal cord barrier in early and late symptomatic SOD1 mice modeling ALS. PLoS One. 2007;2:1205.
    • (2007) PLoS One , vol.2 , pp. 1205
    • Garbuzova-Davis, S.1    Saporta, S.2    Haller, E.3    Kolomey, I.4    Bennett, S.P.5    Potter, H.6
  • 34
    • 0021287843 scopus 로고
    • 3 in the spinal cord and motor cortex of ALS patients
    • DOI 10.1016/0165-5728(84)90042-0
    • Donnenfeld H, Kascsak RJ, Bartfeld H. Deposits of IgG and C3 in the spinal cord and motor cortex of ALS patients. J Neuroimmunol. 1984;6:51-7. (Pubitemid 14132684)
    • (1984) Journal of Neuroimmunology , vol.6 , Issue.1 , pp. 51-57
    • Donnefeld, H.1    Kascsak, R.J.2    Bartfeld, H.3
  • 35
    • 0024994099 scopus 로고
    • IgG reactivity in the spinal cord and motor cortex in amyotrophic lateral sclerosis
    • Engelhardt JI, Appel SH. IgG reactivity in the spinal cord and motor cortex in amyotrophic lateral sclerosis. Arch Neurol. 1990;47:1210-6. (Pubitemid 20381002)
    • (1990) Archives of Neurology , vol.47 , Issue.11 , pp. 1210-1216
    • Engelhardt, J.I.1    Appel, S.H.2
  • 36
    • 21344437029 scopus 로고    scopus 로고
    • ALS-IgG-induced selective motor neurone apoptosis in rat mixed primary spinal cord cultures
    • DOI 10.1111/j.1471-4159.2005.03184.x
    • Demestre M, Pullen A, Orrell RW, Orth M. ALS-IgGinduced selective motor neuron apoptosis in rat mixed primary spinal cord cultures. J Neurochem. 2005;94:268-75. (Pubitemid 40911412)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.1 , pp. 268-275
    • Demestre, M.1    Pullen, A.2    Orrell, R.W.3    Orth, M.4
  • 38
    • 0034327381 scopus 로고    scopus 로고
    • Ultrastructural analysis of spinal motoneurons from mice treated with IgG from ALS patients, healthy individuals, or disease controls
    • Pullen AH, Humphreys P. Ultrastructural analysis of spinal motoneurons from mice treated with IgG from ALS patients, healthy individuals, or disease controls. J Neurol Sci. 2000; 180:35-45.
    • (2000) J Neurol Sci , vol.180 , pp. 35-45
    • Pullen, A.H.1    Humphreys, P.2
  • 39
    • 0030806863 scopus 로고    scopus 로고
    • -·), superoxide dismutases, and related matters
    • DOI 10.1074/jbc.272.30.18515
    • Fridovich I. Superoxide anion radical (O2?.), superoxide dismutases, and related matters. J Biol Chem. 1997;272:18515-7. (Pubitemid 27318184)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18515-18517
    • Fridovich, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.