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Volumn 3, Issue 8, 2012, Pages

Slow development of ALS-like spinal cord pathology in mutant valosin-containing protein gene knock-in mice

Author keywords

Amyotrophic lateral sclerosis; Animal models; Motor neuron; SOD1; TDP 43

Indexed keywords

TAR DNA BINDING PROTEIN; VALOSIN CONTAINING PROTEIN; DNA BINDING PROTEIN; PEPTIDE; PROTEIN TDP-43; UBIQUITIN; VALOSIN;

EID: 84865752018     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2012.115     Document Type: Article
Times cited : (60)

References (41)
  • 1
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein JD. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann Neurol 2009; 65(Suppl 1): S3-S9.
    • (2009) Ann Neurol , vol.65 , Issue.SUPPL. 1
    • Rothstein, J.D.1
  • 2
    • 16844366080 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and its role in motor neuron degeneration in ALS
    • DOI 10.1016/j.mito.2005.01.002, PII S1567724905000346
    • Manfredi G, Xu Z. Mitochondrial dysfunction and its role in motor neuron degeneration in ALS. Mitochondrion 2005; 5: 77-87. (Pubitemid 40485768)
    • (2005) Mitochondrion , vol.5 , Issue.2 , pp. 77-87
    • Manfredi, G.1    Xu, Z.2
  • 6
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland DW. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 2010; 19: R46-R64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 7
    • 79955812764 scopus 로고    scopus 로고
    • TDP-43-based animal models of neurodegeneration: New insights into ALS pathology and pathophysiology
    • Wegorzewska I, Baloh RH. TDP-43-Based Animal Models of Neurodegeneration: New Insights into ALS Pathology and Pathophysiology. Neurodegener Dis 2011; 8: 262-274.
    • (2011) Neurodegener Dis , vol.8 , pp. 262-274
    • Wegorzewska, I.1    Baloh, R.H.2
  • 8
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43: The relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Baloh RH. TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Febs J 2011; 278: 3539-3549.
    • (2011) Febs J , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 9
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • DOI 10.1038/ng1332
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 2004; 36: 377-381. (Pubitemid 38437260)
    • (2004) Nature Genetics , vol.36 , Issue.4 , pp. 377-381
    • Watts, G.D.J.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6    Pestronk, A.7    Whyte, M.P.8    Kimonis, V.E.9
  • 12
    • 78049244477 scopus 로고    scopus 로고
    • VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease
    • e13183
    • Badadani M, Nalbandian A, Watts GD, Vesa J, Kitazawa M, Su H et al. VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease. PLoS One 2010; 5: pii: e13183.
    • (2010) PLoS One , vol.5
    • Badadani, M.1    Nalbandian, A.2    Watts, G.D.3    Vesa, J.4    Kitazawa, M.5    Su, H.6
  • 13
    • 77952486387 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone
    • Custer SK, Neumann M, Lu H, Wright AC, Taylor JP. Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone. Hum Mol Genet 2010; 19: 1741-1755.
    • (2010) Hum Mol Genet , vol.19 , pp. 1741-1755
    • Custer, S.K.1    Neumann, M.2    Lu, H.3    Wright, A.C.4    Taylor, J.P.5
  • 15
    • 0030015076 scopus 로고    scopus 로고
    • Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro
    • Carriedo SG, Yin HZ, Weiss JH. Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro. J Neurosci 1996; 16: 4069-4079. (Pubitemid 26192403)
    • (1996) Journal of Neuroscience , vol.16 , Issue.13 , pp. 4069-4079
    • Carriedo, S.G.1    Yin, H.Z.2    Weiss, J.H.3
  • 16
    • 77957966260 scopus 로고    scopus 로고
    • Pathological 43-kDa transactivation response DNA-binding protein in older adults with and without severe mental illness
    • Geser F, Robinson JL, Malunda JA, Xie SX, Clark CM, Kwong LK et al. Pathological 43-kDa transactivation response DNA-binding protein in older adults with and without severe mental illness. Arch Neurol 2010; 67: 1238-1250.
    • (2010) Arch Neurol , vol.67 , pp. 1238-1250
    • Geser, F.1    Robinson, J.L.2    Malunda, J.A.3    Xie, S.X.4    Clark, C.M.5    Kwong, L.K.6
  • 17
    • 80855130688 scopus 로고    scopus 로고
    • Making connections: Pathology and genetics link amyotrophic lateral sclerosis with frontotemporal lobe dementia
    • Fecto F, Siddique T. Making Connections: Pathology and Genetics Link Amyotrophic Lateral Sclerosis with Frontotemporal Lobe Dementia. J Mol Neurosci 2011; 45: 663-675.
    • (2011) J Mol Neurosci , vol.45 , pp. 663-675
    • Fecto, F.1    Siddique, T.2
  • 19
    • 0345269737 scopus 로고    scopus 로고
    • Disruption of glial glutamate transport by reactive oxygen species produced in motor neurons
    • Rao SD, Yin HZ, Weiss JH. Disruption of glial glutamate transport by reactive oxygen species produced in motor neurons. J Neurosci 2003; 23: 2627-2633. (Pubitemid 36418597)
    • (2003) Journal of Neuroscience , vol.23 , Issue.7 , pp. 2627-2633
    • Rao, S.D.1    Yin, H.Z.2    Weiss, J.H.3
  • 20
    • 34548752918 scopus 로고    scopus 로고
    • 2+-permeable AMPA channel blocker slows loss of both motor neurons and of the astrocyte glutamate transporter, GLT-1 in a mutant SOD1 rat model of ALS
    • DOI 10.1016/j.expneurol.2007.07.011, PII S0014488607002671
    • + permeable AMPA channel blocker slows loss of both motor neurons and of the astrocyte glutamate transporter, GLT-1 in a mutant SOD1 rat model of ALS. Exp Neurol 2007; 207: 177-185. (Pubitemid 47429666)
    • (2007) Experimental Neurology , vol.207 , Issue.2 , pp. 177-185
    • Yin, H.Z.1    Tang, D.T.2    Weiss, J.H.3
  • 21
    • 33745224935 scopus 로고    scopus 로고
    • P97: The cell's molecular purgatory?
    • Halawani D, Latterich M. p97: the cell's molecular purgatory? Mol Cell 2006; 22: 713-717.
    • (2006) Mol Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 23
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 2011; 477: 211-215.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1    Chen, W.2    Hong, S.T.3    Boycott, K.M.4    Gorrie, G.H.5    Siddique, N.6
  • 24
  • 25
    • 80855150639 scopus 로고    scopus 로고
    • SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Fecto F, Yan J, Vemula SP, Liu E, Yang Y, Chen W et al. SQSTM1 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis. Arch Neurol 2011; 68: 1440-1446.
    • (2011) Arch Neurol , vol.68 , pp. 1440-1446
    • Fecto, F.1    Yan, J.2    Vemula, S.P.3    Liu, E.4    Yang, Y.5    Chen, W.6
  • 26
    • 79951704433 scopus 로고    scopus 로고
    • Neuroinflammation in amyotrophic lateral sclerosis: Role of glial activation in motor neuron disease
    • Philips T, Robberecht W. Neuroinflammation in amyotrophic lateral sclerosis: role of glial activation in motor neuron disease. Lancet Neurol 2011; 10: 253-263.
    • (2011) Lancet Neurol , vol.10 , pp. 253-263
    • Philips, T.1    Robberecht, W.2
  • 27
    • 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 PM, Price DL, Wong PC. Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc Natl Acad Sci USA 2010; 107: 16325-16330.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 28
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice
    • Xu YF, Gendron TF, Zhang YJ, Lin WL, D'Alton S, Sheng H et al. Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J Neurosci 2010; 30: 10851-10859.
    • (2010) J Neurosci , vol.30 , pp. 10851-10859
    • Xu, Y.F.1    Gendron, T.F.2    Zhang, Y.J.3    Lin, W.L.4    D'Alton, S.5    Sheng, H.6
  • 30
    • 0027946813 scopus 로고
    • The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis
    • DOI 10.1002/ana.410360608
    • Alexianu ME, Ho BK, Mohamed AH, La Bella V, Smith RG, Appel SH. The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis. Ann Neurol 1994; 36: 846-858. (Pubitemid 24370923)
    • (1994) Annals of Neurology , vol.36 , Issue.6 , pp. 846-858
    • Alexianu, M.E.1    Ho, B.-K.2    Mohamed, A.H.3    La Bella, V.4    Smith, R.G.5    Appel, S.H.6
  • 31
    • 0034212794 scopus 로고    scopus 로고
    • Calcium dynamics and buffering in oculomotor neurones from mouse that are particularly resistant during amyotrophic lateral sclerosis (ALS)-related motoneurone disease
    • Vanselow BK, Keller BU. Calcium dynamics and buffering in oculomotor neurones from mouse that are particularly resistant during amyotrophic lateral sclerosis (ALS)-related motoneurone disease. J Physiol 2000; 525(Pt 2): 433-445. (Pubitemid 30398372)
    • (2000) Journal of Physiology , vol.525 , Issue.2 , pp. 433-445
    • Vanselow, B.K.1    Keller, B.U.2
  • 32
    • 0034004476 scopus 로고    scopus 로고
    • 2+ overload and ROS generation in spinal motor neurons in vitro
    • Carriedo SG, Sensi SL, Yin HZ, Weiss JH. AMPA exposures induce mitochondrial Ca(2+) overload and ROS generation in spinal motor neurons in vitro. J Neurosci 2000; 20: 240-250. (Pubitemid 30220511)
    • (2000) Journal of Neuroscience , vol.20 , Issue.1 , pp. 240-250
    • Carriedo, S.G.1    Sensi, S.L.2    Yin, H.Z.3    Weiss, J.H.4
  • 33
    • 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 HX, Siddique T, O'Halloran TV. 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 2006; 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
  • 36
    • 80054714793 scopus 로고    scopus 로고
    • Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: Implications in ALS
    • Ayala V, Granado-Serrano AB, Cacabelos D, Naudi A, Ilieva EV, Boada J et al. Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: implications in ALS. Acta Neuropathol 2011; 122: 259-270.
    • (2011) Acta Neuropathol , vol.122 , pp. 259-270
    • Ayala, V.1    Granado-Serrano, A.B.2    Cacabelos, D.3    Naudi, A.4    Ilieva, E.V.5    Boada, J.6
  • 37
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • Deng HX, Shi Y, Furukawa Y, Zhai H, Fu R, Liu E et al. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc Natl Acad Sci USA 2006; 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
  • 38
    • 77958495868 scopus 로고    scopus 로고
    • Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity
    • Ferri A, Fiorenzo P, Nencini M, Cozzolino M, Pesaresi MG, Valle C et al. Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity. Hum Mol Genet 2010; 19: 4529-4542.
    • (2010) Hum Mol Genet , vol.19 , pp. 4529-4542
    • Ferri, A.1    Fiorenzo, P.2    Nencini, M.3    Cozzolino, M.4    Pesaresi, M.G.5    Valle, C.6
  • 39
    • 77955423158 scopus 로고    scopus 로고
    • Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell
    • Duan W, Li X, Shi J, Guo Y, Li Z, Li C. Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell. Neuroscience 2010; 169: 1621-1629.
    • (2010) Neuroscience , vol.169 , pp. 1621-1629
    • Duan, W.1    Li, X.2    Shi, J.3    Guo, Y.4    Li, Z.5    Li, C.6
  • 40
    • 79957583304 scopus 로고    scopus 로고
    • Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast
    • Braun RJ, Sommer C, Carmona-Gutierrez D, Khoury CM, Ring J, Buttner S et al. Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast. J Biol Chem 2011; 286: 19958-19972.
    • (2011) J Biol Chem , vol.286 , pp. 19958-19972
    • Braun, R.J.1    Sommer, C.2    Carmona-Gutierrez, D.3    Khoury, C.M.4    Ring, J.5    Buttner, S.6
  • 41
    • 0346156083 scopus 로고    scopus 로고
    • Excitotoxic and oxidative cross-talk between motor neurons and glia in ALS pathogenesis
    • DOI 10.1016/j.tins.2003.11.001
    • Rao SD, Weiss JH. Excitotoxic and oxidative cross-talk between motor neurons and glia in ALS pathogenesis. Trends Neurosci 2004; 27: 17-23. (Pubitemid 38036974)
    • (2004) Trends in Neurosciences , vol.27 , Issue.1 , pp. 17-23
    • Rao, S.D.1    Weiss, J.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.