메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

Lack of effect of methylene blue in the SOD1 G93A mouse model of amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; COPPER ZINC SUPEROXIDE DISMUTASE; GLYCINE; METHYLENE BLUE; SUPEROXIDE DISMUTASE;

EID: 80053585258     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023141     Document Type: Article
Times cited : (13)

References (41)
  • 1
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D, Siddique T, Patteron D, Figlewicz D, Sapp P, 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.1    Siddique, T.2    Patteron, D.3    Figlewicz, D.4    Sapp, P.5
  • 2
    • 0034785509 scopus 로고    scopus 로고
    • The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis
    • Yang Y, Hentati A, Deng H, Dabbagh O, Sasaki T, et al. (2001) The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis. Nat Genet 29: 160-165.
    • (2001) Nat Genet , vol.29 , pp. 160-165
    • Yang, Y.1    Hentati, A.2    Deng, H.3    Dabbagh, O.4    Sasaki, T.5
  • 3
    • 4143084861 scopus 로고    scopus 로고
    • Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS
    • Munch C, Sedlmeier R, Meyer T, Homberg V, Sperfeld A, et al. (2004) Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS. Neurology 63: 724-726.
    • (2004) Neurology , vol.63 , pp. 724-726
    • Munch, C.1    Sedlmeier, R.2    Meyer, T.3    Homberg, V.4    Sperfeld, A.5
  • 4
    • 6344257200 scopus 로고    scopus 로고
    • A mutation in the vesicle trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis
    • Nishimura A, Mitne-Neto M, Silva H, Richieri-Costa A, Middleton S, et al. (2004) A mutation in the vesicle trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am J Hum Genet 75: 822-831.
    • (2004) Am J Hum Genet , vol.75 , pp. 822-831
    • Nishimura, A.1    Mitne-Neto, M.2    Silva, H.3    Richieri-Costa, A.4    Middleton, S.5
  • 5
    • 33645422711 scopus 로고    scopus 로고
    • ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis
    • Greenway M, Andersen P, Russ C, Ennis S, Cashman S, et al. (2006) ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis. Nat Genet 38: 411-413.
    • (2006) Nat Genet , vol.38 , pp. 411-413
    • Greenway, M.1    Andersen, P.2    Russ, C.3    Ennis, S.4    Cashman, S.5
  • 6
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu D, Kwong L, Truax A, Micsenyi M, et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314: 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.2    Kwong, L.3    Truax, A.4    Micsenyi, M.5
  • 7
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Bioph Res Co 351: 602-611.
    • (2006) Biochem Bioph Res Co , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5
  • 8
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
    • Vance C, Rogelj B, Hortobagyi T, De Vos K, Nishimura A, et al. (2009) Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6. Science 323: 1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    de Vos, K.4    Nishimura, A.5
  • 9
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T, Bosco D, Leclerc A, Tamrazian E, Vanderburg C, et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 23: 1205-1208.
    • (2009) Science , vol.23 , pp. 1205-1208
    • Kwiatkowski, T.1    Bosco, D.2    Leclerc, A.3    Tamrazian, E.4    Vanderburg, C.5
  • 10
    • 22044432063 scopus 로고    scopus 로고
    • Early-onset ALS with long-term survival associated with spastin gene mutation
    • Meyer T, Schwan A, Dullinger J, Brocke J, Hoffman K, (2005) Early-onset ALS with long-term survival associated with spastin gene mutation. Neurology 65: 141-143.
    • (2005) Neurology , vol.65 , pp. 141-143
    • Meyer, T.1    Schwan, A.2    Dullinger, J.3    Brocke, J.4    Hoffman, K.5
  • 11
    • 0035949791 scopus 로고    scopus 로고
    • An ALS-like syndrome with new HIV infection and complete response to antiretroviral therapy
    • McGowan D, Scelsa S, Waldron M, (2001) An ALS-like syndrome with new HIV infection and complete response to antiretroviral therapy. Neurology 57 (6): 1094-1097.
    • (2001) Neurology , vol.57 , Issue.6 , pp. 1094-1097
    • McGowan, D.1    Scelsa, S.2    Waldron, M.3
  • 13
    • 37049024934 scopus 로고    scopus 로고
    • Neuro- and cardioprotective effects of blockade of nitric oxide action by administration of methylene blue
    • Wiklund L, Basu S, Micescu A, Wiklund P, Ronquist G, et al. (2007) Neuro- and cardioprotective effects of blockade of nitric oxide action by administration of methylene blue. Ann NY Acad Sci 1122: 231-244.
    • (2007) Ann NY Acad Sci , vol.1122 , pp. 231-244
    • Wiklund, L.1    Basu, S.2    Micescu, A.3    Wiklund, P.4    Ronquist, G.5
  • 14
    • 0032539791 scopus 로고    scopus 로고
    • Impairment of mitochondrial function in skeletal muscles of patients with amyotrophic lateral sclerosis
    • Wiedemann F, Winkler K, Kuznetsov A, Bartels C, Vielhaber S, et al. (1998) Impairment of mitochondrial function in skeletal muscles of patients with amyotrophic lateral sclerosis. J Neurol Sci 156: 65-72.
    • (1998) J Neurol Sci , vol.156 , pp. 65-72
    • Wiedemann, F.1    Winkler, K.2    Kuznetsov, A.3    Bartels, C.4    Vielhaber, S.5
  • 15
    • 0027533361 scopus 로고
    • Inhibition of nitric oxide synthesis by methylene blue
    • Mayer B, Brunner F, Schmidt K, (1993) Inhibition of nitric oxide synthesis by methylene blue. Biochem Pharmacol 45: 367-374.
    • (1993) Biochem Pharmacol , vol.45 , pp. 367-374
    • Mayer, B.1    Brunner, F.2    Schmidt, K.3
  • 16
    • 0033018506 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase up-regulation in a transgenic mouse model of familial Amyotrophic Lateral Sclerosis
    • Almer G, Vukosavic S, Romero N, Przedborski S, (1999) Inducible nitric oxide synthase up-regulation in a transgenic mouse model of familial Amyotrophic Lateral Sclerosis. J Neurochem 72: 2415-2425.
    • (1999) J Neurochem , vol.72 , pp. 2415-2425
    • Almer, G.1    Vukosavic, S.2    Romero, N.3    Przedborski, S.4
  • 17
    • 0030851761 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
    • Beal M, Ferrante R, Browne S, Matthews R, Kowall N, et al. (1997) Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol 42: 644-654.
    • (1997) Ann Neurol , vol.42 , pp. 644-654
    • Beal, M.1    Ferrante, R.2    Browne, S.3    Matthews, R.4    Kowall, N.5
  • 18
    • 0030767498 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation
    • Ferrante R, Shinobu L, Schulz J, Matthews R, Thomas C, et al. (1997) Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation. Ann Neurol 42: 326-334.
    • (1997) Ann Neurol , vol.42 , pp. 326-334
    • Ferrante, R.1    Shinobu, L.2    Schulz, J.3    Matthews, R.4    Thomas, C.5
  • 19
    • 40449086359 scopus 로고    scopus 로고
    • Methylene blue delays cellular senescence and enhances key mitochondrial biochemical pathways
    • Atamna H, Nguyen A, Schultz C, Boyle K, Newberry J, et al. (2008) Methylene blue delays cellular senescence and enhances key mitochondrial biochemical pathways. FASEB 22: 703-712.
    • (2008) FASEB , vol.22 , pp. 703-712
    • Atamna, H.1    Nguyen, A.2    Schultz, C.3    Boyle, K.4    Newberry, J.5
  • 20
    • 33847038020 scopus 로고    scopus 로고
    • Overexpression of Selenoprotein H Reduces HT22 Neuronal Cell Death after UVB Irradiation by Preventing Superoxide Formation
    • Jilani K, Panee J, He Q, Berry M, Li P, (2007) Overexpression of Selenoprotein H Reduces HT22 Neuronal Cell Death after UVB Irradiation by Preventing Superoxide Formation. Int J Biol Sci 3 (4): 198-204.
    • (2007) Int J Biol Sci , vol.3 , Issue.4 , pp. 198-204
    • Jilani, K.1    Panee, J.2    He, Q.3    Berry, M.4    Li, P.5
  • 21
    • 77649248565 scopus 로고    scopus 로고
    • Selenium and selenoproteins in health and Disease
    • Papp L, Holmgren A, Khanna K, (2010) Selenium and selenoproteins in health and Disease. Antioxid Redox Sign 12 (7): 793-795.
    • (2010) Antioxid Redox Sign , vol.12 , Issue.7 , pp. 793-795
    • Papp, L.1    Holmgren, A.2    Khanna, K.3
  • 22
    • 0031784348 scopus 로고    scopus 로고
    • Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Andrus P, Fleck T, Gurney M, Hall E, (1998) Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J Neurochem 71: 2041-2048.
    • (1998) J Neurochem , vol.71 , pp. 2041-2048
    • Andrus, P.1    Fleck, T.2    Gurney, M.3    Hall, E.4
  • 23
    • 33751003518 scopus 로고    scopus 로고
    • Oxidative stress in ALS: a mechanism of neurodegeneration and a therapeutic target
    • Barber S, Mead R, Shaw P, (2006) Oxidative stress in ALS: a mechanism of neurodegeneration and a therapeutic target. Biochim Biophys Acta 1762: 1051-1067.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 1051-1067
    • Barber, S.1    Mead, R.2    Shaw, P.3
  • 24
    • 67349187297 scopus 로고    scopus 로고
    • Methylethioninium chloride (MTC) acts as a tau aggregation inhibitor (TAI) in a cellular model and reverses tau pathology in transgenic mouse models of Alzheimer's disease
    • Harrington C, Rickard J, Horsley D, Harrington K, Hindley K, et al. (2008) Methylethioninium chloride (MTC) acts as a tau aggregation inhibitor (TAI) in a cellular model and reverses tau pathology in transgenic mouse models of Alzheimer's disease. Alzheimer's Dement 4: T120-T121.
    • (2008) Alzheimer's Dement , vol.4
    • Harrington, C.1    Rickard, J.2    Horsley, D.3    Harrington, K.4    Hindley, K.5
  • 25
    • 51349134160 scopus 로고    scopus 로고
    • Hope in Alzheimer's fight emerges from unexpected place
    • Gura T, (2008) Hope in Alzheimer's fight emerges from unexpected place. Nat Med 14: 894.
    • (2008) Nat Med , vol.14 , pp. 894
    • Gura, T.1
  • 26
    • 0346734159 scopus 로고    scopus 로고
    • Microtubule associated tau protein positive neuronal and glial inclusions in amyotrophic lateral sclerosis
    • Yang W, Sopper M, Leystra-Lutz C, Strong M, (2003) Microtubule associated tau protein positive neuronal and glial inclusions in amyotrophic lateral sclerosis. Neurology 61: 1766-1773.
    • (2003) Neurology , vol.61 , pp. 1766-1773
    • Yang, W.1    Sopper, M.2    Leystra-Lutz, C.3    Strong, M.4
  • 27
    • 33745654119 scopus 로고    scopus 로고
    • Tau protein hyperphosphorylation in sporadic ALS with cognitive impairment
    • Strong M, Yang W, Strong W, Leystra-Lantz C, Jaffe H, et al. (2006) Tau protein hyperphosphorylation in sporadic ALS with cognitive impairment. Neurology 66: 1770-1771.
    • (2006) Neurology , vol.66 , pp. 1770-1771
    • Strong, M.1    Yang, W.2    Strong, W.3    Leystra-Lantz, C.4    Jaffe, H.5
  • 28
    • 0029812897 scopus 로고    scopus 로고
    • Impairment in fast axonal transport in the proximal axons of anterior horn neurons in amyotrophic lateral sclerosis
    • Sasaki S, Iwata M, (1996) Impairment in fast axonal transport in the proximal axons of anterior horn neurons in amyotrophic lateral sclerosis. Neurology 47: 535-540.
    • (1996) Neurology , vol.47 , pp. 535-540
    • Sasaki, S.1    Iwata, M.2
  • 29
    • 0345742771 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis is a distal axonopathy: evidence in mice and man
    • Fischer L, Culver D, Tennant P, Davis A, Wang M, et al. (2004) Amyotrophic lateral sclerosis is a distal axonopathy: evidence in mice and man. Exp Neurol 185: 232-240.
    • (2004) Exp Neurol , vol.185 , pp. 232-240
    • Fischer, L.1    Culver, D.2    Tennant, P.3    Davis, A.4    Wang, M.5
  • 30
    • 85003346469 scopus 로고    scopus 로고
    • NTP toxicology and carcinogenesis studies of methylene blue trihydrate (CAS No. 7220-79-3) in F344/N rats and B6C3F1 mice (Gavage Studies)
    • National Toxicology Program
    • National Toxicology Program (2008) NTP toxicology and carcinogenesis studies of methylene blue trihydrate (CAS No. 7220-79-3) in F344/N rats and B6C3F1 mice (Gavage Studies). Natl Toxicol Prog Tech Rep Ser 540: 1-244.
    • (2008) Natl Toxicol Prog Tech Rep Ser , vol.540 , pp. 1-244
  • 31
    • 0015939376 scopus 로고
    • Motoneuron disease and ageing
    • McComas A, Upton A, Sica R, (1973) Motoneuron disease and ageing. Lancet 29: 1477-1480.
    • (1973) Lancet , vol.29 , pp. 1477-1480
    • McComas, A.1    Upton, A.2    Sica, R.3
  • 32
    • 39349107014 scopus 로고    scopus 로고
    • Design, power, and interpretation of studies in the standard murine model of ALS
    • Scott S, Kranz J, Cole J, Lincecum J, Thompson K, et al. (2008) Design, power, and interpretation of studies in the standard murine model of ALS. Amyotroph Lateral Sc. 9: 4-15.
    • (2008) Amyotroph Lateral Sc , vol.9 , pp. 4-15
    • Scott, S.1    Kranz, J.2    Cole, J.3    Lincecum, J.4    Thompson, K.5
  • 33
    • 21444451106 scopus 로고    scopus 로고
    • Gait analysis detects early changes in transgenic SOD1(G93A) mice
    • Wooley C, Sher R, Kale A, Frankel W, Cox G, et al. (2005) Gait analysis detects early changes in transgenic SOD1(G93A) mice. Muscle Nerve 32: 43-50.
    • (2005) Muscle Nerve , vol.32 , pp. 43-50
    • Wooley, C.1    Sher, R.2    Kale, A.3    Frankel, W.4    Cox, G.5
  • 34
    • 70350543562 scopus 로고    scopus 로고
    • Pre-symptomatic detection of chronic motor deficits and genotype prediction in congenic B6.SOD1G93A ALS mouse model
    • Hayworth C, Gonzalez-Lima F, (2009) Pre-symptomatic detection of chronic motor deficits and genotype prediction in congenic B6.SOD1G93A ALS mouse model. Neuroscience 164: 975-985.
    • (2009) Neuroscience , vol.164 , pp. 975-985
    • Hayworth, C.1    Gonzalez-Lima, F.2
  • 35
    • 73949149584 scopus 로고    scopus 로고
    • RNA processing defects associated with diseases of the motor neuron
    • Kolb S, Sutton S, Schoenberg D, (2010) RNA processing defects associated with diseases of the motor neuron. Muscle Nerve 41 (1): 5-17.
    • (2010) Muscle Nerve , vol.41 , Issue.1 , pp. 5-17
    • Kolb, S.1    Sutton, S.2    Schoenberg, D.3
  • 36
    • 78650018920 scopus 로고    scopus 로고
    • Cellular and molecular actions of methylene blue in the nervous system
    • Oz M, Lorke DE, Hasan M, Petroianu GA, (2010) Cellular and molecular actions of methylene blue in the nervous system. Med Res Rev 31: 93-117.
    • (2010) Med Res Rev , vol.31 , pp. 93-117
    • Oz, M.1    Lorke, D.E.2    Hasan, M.3    Petroianu, G.A.4
  • 37
    • 77958566761 scopus 로고    scopus 로고
    • Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
    • O'Leary J, Qingyou L, Marinec P, Blair L, Congdon E, et al. (2010) Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden. Mol Neurodegener 5: 45-55.
    • (2010) Mol Neurodegener , vol.5 , pp. 45-55
    • O'Leary, J.1    Qingyou, L.2    Marinec, P.3    Blair, L.4    Congdon, E.5
  • 39
    • 0033948654 scopus 로고    scopus 로고
    • Pharmacokinetics and organ distribution of intravenous and oral methylene blue
    • Peter C, Hongwan D, Kupfer A, Lauterburg B, (2000) Pharmacokinetics and organ distribution of intravenous and oral methylene blue. Eur J Clin Pharmacol 56: 247-250.
    • (2000) Eur J Clin Pharmacol , vol.56 , pp. 247-250
    • Peter, C.1    Hongwan, D.2    Kupfer, A.3    Lauterburg, B.4
  • 40
    • 0030690490 scopus 로고    scopus 로고
    • The use of transgenic mouse models of amyotrophic lateral sclerosis in preclinical drug studies
    • Gurney M, (1997) The use of transgenic mouse models of amyotrophic lateral sclerosis in preclinical drug studies. J Neurol Sci 152: S67-S73.
    • (1997) J Neurol Sci , vol.152
    • Gurney, M.1
  • 41
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation
    • Gurney M, Pu H, Chiu A, Dal Canto M, Polchow C, et al. (1994) Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264: 1772-1775.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.1    Pu, H.2    Chiu, A.3    Dal Canto, M.4    Polchow, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.