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Volumn 94, Issue 1, 2013, Pages 56-64

Premature death of TDP-43 (A315T) transgenic mice due to gastrointestinal complications prior to development of full neurological symptoms of amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis; Gastrointestinal track; Mouse model of ALS; TDP 43

Indexed keywords

BIOLOGICAL MARKER; TAR DNA BINDING PROTEIN;

EID: 84872465426     PISSN: 09599673     EISSN: 13652613     Source Type: Journal    
DOI: 10.1111/iep.12006     Document Type: Article
Times cited : (66)

References (35)
  • 1
  • 2
    • 0035132167 scopus 로고    scopus 로고
    • Increased expression of the pro-inflammatory enzyme cyclooxygenase-2 in amyotrophic lateral sclerosis
    • Almer G., Guegan C., Teismann P. et al. (2001) Increased expression of the pro-inflammatory enzyme cyclooxygenase-2 in amyotrophic lateral sclerosis. Ann. Neurol. 49, 176-185.
    • (2001) Ann. Neurol. , vol.49 , pp. 176-185
    • Almer, G.1    Guegan, C.2    Teismann, P.3
  • 3
    • 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. et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602-611.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3
  • 4
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • Borchelt D.R., Ratovitski T., van Lare J. et al. (1997) Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 19, 939-945.
    • (1997) Neuron , vol.19 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    van Lare, J.3
  • 5
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn L.I., Houseweart M.K., Kato S. et al. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science, 281, 1851-1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1    Houseweart, M.K.2    Kato, S.3
  • 6
    • 0001011390 scopus 로고
    • Clinical and Pathological Studies of an Hereditary Neuropathy in Mice (Dystonia Musculorum)
    • Duchen L.W., Strich S.J., Falconer D.S. (1964) Clinical and Pathological Studies of an Hereditary Neuropathy in Mice (Dystonia Musculorum). Brain 87, 367-378.
    • (1964) Brain , vol.87 , pp. 367-378
    • Duchen, L.W.1    Strich, S.J.2    Falconer, D.S.3
  • 7
    • 80855138138 scopus 로고    scopus 로고
    • Rodent models of TDP-43 proteinopathy: investigating the mechanisms of TDP-43-mediated neurodegeneration
    • Gendron T.F., Petrucelli L. (2011) Rodent models of TDP-43 proteinopathy: investigating the mechanisms of TDP-43-mediated neurodegeneration. J. Mol. Neurosci. 45, 486-499.
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 486-499
    • Gendron, T.F.1    Petrucelli, L.2
  • 8
    • 41949119043 scopus 로고    scopus 로고
    • TDP-43 A315T mutation in familial motor neuron disease
    • Gitcho M.A., Baloh R.H., Chakraverty S. et al. (2008) TDP-43 A315T mutation in familial motor neuron disease. Ann. Neurol. 63, 535-538.
    • (2008) Ann. Neurol. , vol.63 , pp. 535-538
    • Gitcho, M.A.1    Baloh, R.H.2    Chakraverty, S.3
  • 9
    • 84861636497 scopus 로고    scopus 로고
    • HO-1 induction in motor cortex and intestinal dysfunction in TDP-43 A315T transgenic mice
    • Guo Y., Wang Q., Zhang K. et al. (2012) HO-1 induction in motor cortex and intestinal dysfunction in TDP-43 A315T transgenic mice. Brain Res. 1460, 88-95.
    • (2012) Brain Res. , vol.1460 , pp. 88-95
    • Guo, Y.1    Wang, Q.2    Zhang, K.3
  • 10
    • 0041833409 scopus 로고    scopus 로고
    • Message and protein-level elevation of tumor necrosis factor alpha (TNF alpha) and TNF alpha-modulating cytokines in spinal cords of the G93A-SOD1 mouse model for amyotrophic lateral sclerosis
    • Hensley K., Fedynyshyn J., Ferrell S. et al. (2003) Message and protein-level elevation of tumor necrosis factor alpha (TNF alpha) and TNF alpha-modulating cytokines in spinal cords of the G93A-SOD1 mouse model for amyotrophic lateral sclerosis. Neurobiol. Dis. 14, 74-80.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 74-80
    • Hensley, K.1    Fedynyshyn, J.2    Ferrell, S.3
  • 11
    • 3042515545 scopus 로고    scopus 로고
    • Focal dysfunction of the proteasome: a pathogenic factor in a mouse model of amyotrophic lateral sclerosis
    • Kabashi E., Agar J.N., Taylor D.M., Minotti S., Durham H.D. (2004) Focal dysfunction of the proteasome: a pathogenic factor in a mouse model of amyotrophic lateral sclerosis. J. Neurochem. 89, 1325-1335.
    • (2004) J. Neurochem. , vol.89 , pp. 1325-1335
    • Kabashi, E.1    Agar, J.N.2    Taylor, D.M.3    Minotti, S.4    Durham, H.D.5
  • 12
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E., Valdmanis P.N., Dion P. et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 40, 572-574.
    • (2008) Nat. Genet. , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3
  • 13
    • 17444367702 scopus 로고    scopus 로고
    • Integrative role of cPLA with COX-2 and the effect of non-steroidal anti-inflammatory drugs in a transgenic mouse model of amyotrophic lateral sclerosis
    • Kiaei M., Kipiani K., Petri S. et al. (2005) Integrative role of cPLA with COX-2 and the effect of non-steroidal anti-inflammatory drugs in a transgenic mouse model of amyotrophic lateral sclerosis. J. Neurochem. 93, 403-411.
    • (2005) J. Neurochem. , vol.93 , pp. 403-411
    • Kiaei, M.1    Kipiani, K.2    Petri, S.3
  • 14
    • 33645642112 scopus 로고    scopus 로고
    • Thalidomide and lenalidomide extend survival in a transgenic mouse model of amyotrophic lateral sclerosis
    • Kiaei M., Petri S., Kipiani K. et al. (2006) Thalidomide and lenalidomide extend survival in a transgenic mouse model of amyotrophic lateral sclerosis. J. Neurosci. 26, 2467-2473.
    • (2006) J. Neurosci. , vol.26 , pp. 2467-2473
    • Kiaei, M.1    Petri, S.2    Kipiani, K.3
  • 15
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T.J. Jr, Bosco D.A., Leclerc A.L. et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 16
    • 0348011603 scopus 로고    scopus 로고
    • Functions of intermediate filaments in neuronal development and disease
    • Lariviere R.C., Julien J.P. (2004) Functions of intermediate filaments in neuronal development and disease. J. Neurobiol. 58, 131-148.
    • (2004) J. Neurobiol. , vol.58 , pp. 131-148
    • Lariviere, R.C.1    Julien, J.P.2
  • 17
    • 0035105962 scopus 로고    scopus 로고
    • Glutamate transporters in neurologic disease
    • Maragakis N.J., Rothstein J.D. (2001) Glutamate transporters in neurologic disease. Arch. Neurol. 58, 365-370.
    • (2001) Arch. Neurol. , vol.58 , pp. 365-370
    • Maragakis, N.J.1    Rothstein, J.D.2
  • 18
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M., Sampathu D.M., Kwong L.K. 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.M.2    Kwong, L.K.3
  • 19
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli P., Brown R.H. (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 7, 710-723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 20
    • 0942287085 scopus 로고    scopus 로고
    • Programmed cell death in amyotrophic lateral sclerosis: a mechanism of pathogenic and therapeutic importance
    • Przedborski S. (2004) Programmed cell death in amyotrophic lateral sclerosis: a mechanism of pathogenic and therapeutic importance. Neurologist 10, 1-7.
    • (2004) Neurologist , vol.10 , pp. 1-7
    • Przedborski, S.1
  • 21
    • 0037068836 scopus 로고    scopus 로고
    • Motoneuron death triggered by a specific pathway downstream of Fas. potentiation by ALS-linked SOD1 mutations
    • Raoul C., Estevez A.G., Nishimune H. et al. (2002) Motoneuron death triggered by a specific pathway downstream of Fas. potentiation by ALS-linked SOD1 mutations. Neuron, 35, 1067-1083.
    • (2002) Neuron , vol.35 , pp. 1067-1083
    • Raoul, C.1    Estevez, A.G.2    Nishimune, H.3
  • 22
    • 0029435316 scopus 로고
    • Excitotoxicity and neurodegeneration in amyotrophic lateral sclerosis
    • Rothstein J.D. (1995) Excitotoxicity and neurodegeneration in amyotrophic lateral sclerosis. Clin. Neurosci. 3, 348-359.
    • (1995) Clin. Neurosci. , vol.3 , pp. 348-359
    • Rothstein, J.D.1
  • 23
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan X., Chiang P.M., Price D.L., Wong P.C. (2010) Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl Acad. Sci. U.S.A. 107, 16325-16330.
    • (2010) Proc. Natl Acad. Sci. U.S.A. , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 24
    • 42049120518 scopus 로고    scopus 로고
    • Progranulin genetic variability contributes to amyotrophic lateral sclerosis
    • Sleegers K., Brouwers N., Maurer-Stroh S. et al. (2008) Progranulin genetic variability contributes to amyotrophic lateral sclerosis. Neurology 71, 253-259.
    • (2008) Neurology , vol.71 , pp. 253-259
    • Sleegers, K.1    Brouwers, N.2    Maurer-Stroh, S.3
  • 26
    • 84855515796 scopus 로고    scopus 로고
    • Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor kappaB-mediated pathogenic pathways
    • Swarup V., Phaneuf D., Dupre N. et al. (2011) Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor kappaB-mediated pathogenic pathways. J. Exp. Med. 208, 2429-2447.
    • (2011) J. Exp. Med. , vol.208 , pp. 2429-2447
    • Swarup, V.1    Phaneuf, D.2    Dupre, N.3
  • 27
    • 63949083624 scopus 로고    scopus 로고
    • Mimicking aspects of frontotemporal lobar degeneration and Lou Gehrig's disease in rats via TDP-43 overexpression
    • Tatom J.B., Wang D.B., Dayton R.D. et al. (2009) Mimicking aspects of frontotemporal lobar degeneration and Lou Gehrig's disease in rats via TDP-43 overexpression. Mol. Ther. 17, 607-613.
    • (2009) Mol. Ther. , vol.17 , pp. 607-613
    • Tatom, J.B.1    Wang, D.B.2    Dayton, R.D.3
  • 28
    • 3042817421 scopus 로고    scopus 로고
    • CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
    • Urushitani M., Kurisu J., Tateno M. et al. (2004) CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70. J. Neurochem. 90, 231-244.
    • (2004) J. Neurochem. , vol.90 , pp. 231-244
    • Urushitani, M.1    Kurisu, J.2    Tateno, M.3
  • 29
    • 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. 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
  • 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. et al. (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
  • 31
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I., Bell S., Cairns N.J., Miller T.M., Baloh R.H. (2009) TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. U.S.A. 106, 18809-18814.
    • (2009) Proc. Natl Acad. Sci. U.S.A. , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 32
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • Wils H., Kleinberger G., Janssens J. et al. (2010) TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. U.S.A. 107, 3858-3863.
    • (2010) Proc. Natl Acad. Sci. U.S.A. , vol.107 , pp. 3858-3863
    • Wils, H.1    Kleinberger, G.2    Janssens, J.3
  • 35
    • 42949094584 scopus 로고    scopus 로고
    • TDP-43 mutation in familial amyotrophic lateral sclerosis
    • Yokoseki A., Shiga A., Tan C.F. et al. (2008) TDP-43 mutation in familial amyotrophic lateral sclerosis. Ann. Neurol. 63, 538-542.
    • (2008) Ann. Neurol. , vol.63 , pp. 538-542
    • Yokoseki, A.1    Shiga, A.2    Tan, C.F.3


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