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Volumn 23, Issue 10, 2014, Pages 2629-2638

An enhanced integrated stress response ameliorates mutant SOD1-induced ALS

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 34; INITIATION FACTOR 2ALPHA; PKR LIKE LOCALIZED EIF2 KINASE; PROTEIN KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BIOLOGICAL MARKER; INITIATION FACTOR 2; PHOSPHOPROTEIN PHOSPHATASE 1; PPP1R15A PROTEIN, MOUSE; SUPEROXIDE DISMUTASE;

EID: 84898817967     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddt658     Document Type: Article
Times cited : (77)

References (60)
  • 1
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein, J.D. (2009) Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol., 65, S3-S9.
    • (2009) Ann. Neurol. , vol.65
    • Rothstein, J.D.1
  • 2
    • 79952840767 scopus 로고    scopus 로고
    • Control of redox state and redox signaling by neural antioxidant systems
    • Lewerenz, J. and Maher, P. (2011) Control of redox state and redox signaling by neural antioxidant systems. Antioxid. Redox Signal., 14, 1449-1465.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1449-1465
    • Lewerenz, J.1    Maher, P.2
  • 3
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D. and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol., 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 4
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani, M., Sik, A., Sakurai, T., Nukina, N., Takahashi, R. and Julien, J.P. (2006) Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci., 9, 108-118.
    • (2006) Nat. Neurosci. , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.P.6
  • 5
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • Turner, B.J., Atkin, J.D., Farg, M.A., Zang, D.W., Rembach, A., Lopes, E.C., Patch, J.D., Hill, A.F. and Cheema, S.S. (2005) Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J. Neurosci., 25, 108-117.
    • (2005) J. Neurosci. , vol.25 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3    Zang, D.W.4    Rembach, A.5    Lopes, E.C.6    Patch, J.D.7    Hill, A.F.8    Cheema, S.S.9
  • 6
    • 46749107070 scopus 로고    scopus 로고
    • The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS
    • Urushitani, M., Ezzi, S.A., Matsuo, A., Tooyama, I. and Julien, J.P. (2008) The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS. FASEB J., 22, 2476-2487.
    • (2008) FASEB J. , vol.22 , pp. 2476-2487
    • Urushitani, M.1    Ezzi, S.A.2    Matsuo, A.3    Tooyama, I.4    Julien, J.P.5
  • 8
    • 78149339310 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway
    • Nassif, M., Matus, S., Castillo, K. and Hetz, C. (2010) Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway. Antioxid. Redox Signal., 13, 1955-1989.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1955-1989
    • Nassif, M.1    Matus, S.2    Castillo, K.3    Hetz, C.4
  • 9
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: a glimpse into the ER
    • Matus, S., Glimcher, L.H. and Hetz, C. (2011) Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr. Opin. Cell Biol., 23, 239-252.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 10
    • 66149156941 scopus 로고    scopus 로고
    • ER stress and unfolded protein response in amyotrophic lateral sclerosis
    • Kanekura, K., Suzuki, H., Aiso, S. and Matsuoka, M. (2009) ER stress and unfolded protein response in amyotrophic lateral sclerosis. Mol. Neurobiol., 39, 81-89.
    • (2009) Mol. Neurobiol. , vol.39 , pp. 81-89
    • Kanekura, K.1    Suzuki, H.2    Aiso, S.3    Matsuoka, M.4
  • 12
    • 34247098374 scopus 로고    scopus 로고
    • Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders
    • Uehara, T. (2007) Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders. Antioxid. Redox Signal., 9, 597-601.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 597-601
    • Uehara, T.1
  • 13
    • 33644858343 scopus 로고    scopus 로고
    • The unfolded protein response: a stress signaling pathway critical for health and disease
    • Zhang, K. and Kaufman, R.J. (2006) The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology, 66, S102-S109.
    • (2006) Neurology , vol.66
    • Zhang, K.1    Kaufman, R.J.2
  • 14
    • 38449116842 scopus 로고    scopus 로고
    • Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells
    • Oh, Y.K., Shin, K.S., Yuan, J. and Kang, S.J. (2008) Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells. J. Neurochem., 104, 993-1005.
    • (2008) J. Neurochem. , vol.104 , pp. 993-1005
    • Oh, Y.K.1    Shin, K.S.2    Yuan, J.3    Kang, S.J.4
  • 16
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin, J.D., Farg, M.A., Turner, B.J., Tomas, D., Lysaght, J.A., Nunan, J., Rembach, A., Nagley, P., Beart, P.M., Cheema, S.S. et al. (2006) Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem., 281, 30152-30165.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3    Tomas, D.4    Lysaght, J.A.5    Nunan, J.6    Rembach, A.7    Nagley, P.8    Beart, P.M.9    Cheema, S.S.10
  • 19
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E. and Caroni, P. (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci., 12, 627-636.
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 20
    • 28844507918 scopus 로고    scopus 로고
    • Expression of an endoplasmic reticulum-resident chaperone, glucose-regulated stress protein 78, in the spinal cord of a mouse model of amyotrophic lateral sclerosis
    • Wate, R., Ito, H., Zhang, J.H., Ohnishi, S., Nakano, S. and Kusaka, H. (2005) Expression of an endoplasmic reticulum-resident chaperone, glucose-regulated stress protein 78, in the spinal cord of a mouse model of amyotrophic lateral sclerosis. Acta Neuropathol., 110, 557-562.
    • (2005) Acta Neuropathol. , vol.110 , pp. 557-562
    • Wate, R.1    Ito, H.2    Zhang, J.H.3    Ohnishi, S.4    Nakano, S.5    Kusaka, H.6
  • 22
  • 24
    • 34250177650 scopus 로고    scopus 로고
    • Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation
    • Ezzi, S.A., Urushitani, M. and Julien, J.P. (2007) Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation. J. Neurochem., 102, 170-178.
    • (2007) J. Neurochem. , vol.102 , pp. 170-178
    • Ezzi, S.A.1    Urushitani, M.2    Julien, J.P.3
  • 26
    • 37849007550 scopus 로고    scopus 로고
    • Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?
    • Kabashi, E., Valdmanis, P.N., Dion, P. and Rouleau, G.A. (2007) Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Ann. Neurol., 62, 553-559.
    • (2007) Ann. Neurol. , vol.62 , pp. 553-559
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Rouleau, G.A.4
  • 28
    • 84859512071 scopus 로고    scopus 로고
    • Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis
    • Pokrishevsky, E., Grad, L.I., Yousefi, M., Wang, J., Mackenzie, I.R. and Cashman, N.R. (2012) Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PLoS ONE, 7, e35050.
    • (2012) PLoS ONE , vol.7
    • Pokrishevsky, E.1    Grad, L.I.2    Yousefi, M.3    Wang, J.4    Mackenzie, I.R.5    Cashman, N.R.6
  • 33
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded response in familial amyotrophic lateral sclerosis
    • Wang, L., Popko, B. and Roos, R.P. (2011) The unfolded response in familial amyotrophic lateral sclerosis. Hum. Mol. Genet., 20, 1008-1015.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 35
    • 64549124726 scopus 로고    scopus 로고
    • Wild-typeSOD1overexpression accelerates disease onset of a G85R SOD1 mouse
    • Wang, L., Deng, H.X., Grisotti, G., Zhai, H., Siddique, T. and Roos, R.P. (2009) Wild-typeSOD1overexpression accelerates disease onset of a G85R SOD1 mouse. Hum. Mol. Genet., 18, 1642-1651.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1642-1651
    • Wang, L.1    Deng, H.X.2    Grisotti, G.3    Zhai, H.4    Siddique, T.5    Roos, R.P.6
  • 36
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in perk-/-mice reveals a role for translational control in secretory cell survival
    • Harding, H.P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D.D. and Ron, D. (2001) Diabetes mellitus and exocrine pancreatic dysfunction in perk-/-mice reveals a role for translational control in secretory cell survival. Mol. Cell, 7, 1153-1163.
    • (2001) Mol. Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 37
    • 33749056809 scopus 로고    scopus 로고
    • ALS: a disease of motor neurons and their nonneuronal neighbors
    • Boillee, S., Vande Velde, C. and Cleveland, D.W. (2006) ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron, 52, 39-59.
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 39
    • 80052081196 scopus 로고    scopus 로고
    • Stress signaling from the endoplasmic reticulum: a central player in the pathogenesis of amyotrophic lateral sclerosis
    • Walker, A.K. and Atkin, J.D. (2011) Stress signaling from the endoplasmic reticulum: a central player in the pathogenesis of amyotrophic lateral sclerosis. IUBMB Life, 63, 754-763.
    • (2011) IUBMB Life , vol.63 , pp. 754-763
    • Walker, A.K.1    Atkin, J.D.2
  • 40
    • 84863012403 scopus 로고    scopus 로고
    • Differential effects of unfolded protein response pathways on axon injury-induced death of retinal ganglion cells
    • Hu, Y., Park, K.K., Yang, L., Wei, X., Yang, Q., Cho, K.S., Thielen, P., Lee, A.H., Cartoni, R., Glimcher, L.H. et al. (2012) Differential effects of unfolded protein response pathways on axon injury-induced death of retinal ganglion cells. Neuron, 73, 445-452.
    • (2012) Neuron , vol.73 , pp. 445-452
    • Hu, Y.1    Park, K.K.2    Yang, L.3    Wei, X.4    Yang, Q.5    Cho, K.S.6    Thielen, P.7    Lee, A.H.8    Cartoni, R.9    Glimcher, L.H.10
  • 41
    • 67649486844 scopus 로고    scopus 로고
    • The effect of mutant SOD1 dismutase activity on non-cell autonomous degeneration in familial amyotrophic lateral sclerosis
    • Wang, L., Sharma, K., Grisotti, G. and Roos, R.P. (2009) The effect of mutant SOD1 dismutase activity on non-cell autonomous degeneration in familial amyotrophic lateral sclerosis. Neurobiol. Dis., 35, 234-240.
    • (2009) Neurobiol. Dis. , vol.35 , pp. 234-240
    • Wang, L.1    Sharma, K.2    Grisotti, G.3    Roos, R.P.4
  • 42
    • 84863737109 scopus 로고    scopus 로고
    • Selective knockdown of mutant SOD1 in Schwann cells ameliorates disease in G85R mutant SOD1 transgenic mice
    • Wang, L., Pytel, P., Feltri, M.L., Wrabetz, L. and Roos, R.P. (2012) Selective knockdown of mutant SOD1 in Schwann cells ameliorates disease in G85R mutant SOD1 transgenic mice. Neurobiol. Dis., 48, 52-57.
    • (2012) Neurobiol. Dis. , vol.48 , pp. 52-57
    • Wang, L.1    Pytel, P.2    Feltri, M.L.3    Wrabetz, L.4    Roos, R.P.5
  • 43
    • 78650550891 scopus 로고    scopus 로고
    • Astrocyte loss of mutant SOD1 delays ALS disease onset and progression in G85R transgenic mice
    • Wang, L., Gutmann, D.H. and Roos, R.P. (2011) Astrocyte loss of mutant SOD1 delays ALS disease onset and progression in G85R transgenic mice. Hum. Mol. Genet., 20, 286-293.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 286-293
    • Wang, L.1    Gutmann, D.H.2    Roos, R.P.3
  • 44
    • 77749264823 scopus 로고    scopus 로고
    • MutantSOD1knockdown in all cell types ameliorates disease in G85R SOD1 mice with a limited additional effect over knockdown restricted to motor neurons
    • Wang, L., Grisotti, G. and Roos, R.P. (2010) MutantSOD1knockdown in all cell types ameliorates disease in G85R SOD1 mice with a limited additional effect over knockdown restricted to motor neurons. J. Neurochem., 113, 166-174.
    • (2010) J. Neurochem. , vol.113 , pp. 166-174
    • Wang, L.1    Grisotti, G.2    Roos, R.P.3
  • 46
    • 63649109017 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disorders of myelinating cells
    • Lin, W. and Popko, B. (2009) Endoplasmic reticulum stress in disorders of myelinating cells. Nat. Neurosci., 12, 379-385.
    • (2009) Nat. Neurosci. , vol.12 , pp. 379-385
    • Lin, W.1    Popko, B.2
  • 48
    • 67049172152 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response and aging
    • Naidoo, N. (2009) The endoplasmic reticulum stress response and aging. Rev. Neurosci., 20, 23-37.
    • (2009) Rev. Neurosci. , vol.20 , pp. 23-37
    • Naidoo, N.1
  • 49
    • 84856710131 scopus 로고    scopus 로고
    • Life-or-death decisions upon axonal damage
    • Roselli, F. and Caroni, P. (2012) Life-or-death decisions upon axonal damage. Neuron, 73, 405-407.
    • (2012) Neuron , vol.73 , pp. 405-407
    • Roselli, F.1    Caroni, P.2
  • 50
    • 77954377779 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response factor CHOP-10 protects against hypoxia-induced neuronal death
    • Halterman, M.W., Gill, M., DeJesus, C., Ogihara, M., Schor, N.F. and Federoff, H.J. (2010) The endoplasmic reticulum stress response factor CHOP-10 protects against hypoxia-induced neuronal death. J. Biol. Chem., 285, 21329-21340.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21329-21340
    • Halterman, M.W.1    Gill, M.2    DeJesus, C.3    Ogihara, M.4    Schor, N.F.5    Federoff, H.J.6
  • 51
    • 70450214826 scopus 로고    scopus 로고
    • CHOPand the endoplasmic reticulum stress response in myelinating glia
    • Gow, A. and Wrabetz, L. (2009)CHOPand the endoplasmic reticulum stress response in myelinating glia. Curr. Opin. Neurobiol., 19, 505-510.
    • (2009) Curr. Opin. Neurobiol. , vol.19 , pp. 505-510
    • Gow, A.1    Wrabetz, L.2
  • 54
    • 84883453343 scopus 로고    scopus 로고
    • Suppression of eIF2alpha kinases alleviates Alzheimer's disease-related plasticity and memory deficits
    • Ma, T., Trinh, M.A., Wexler, A.J., Bourbon, C., Gatti, E., Pierre, P., Cavener, D.R. and Klann, E. (2013) Suppression of eIF2alpha kinases alleviates Alzheimer's disease-related plasticity and memory deficits. Nat. Neurosci., 16, 1299-1305.
    • (2013) Nat. Neurosci. , vol.16 , pp. 1299-1305
    • Ma, T.1    Trinh, M.A.2    Wexler, A.J.3    Bourbon, C.4    Gatti, E.5    Pierre, P.6    Cavener, D.R.7    Klann, E.8
  • 56
    • 34948897411 scopus 로고    scopus 로고
    • The transcription factor XBP-1 is essential for the development and survival of dendritic cells
    • Iwakoshi, N.N., Pypaert, M. and Glimcher, L.H. (2007) The transcription factor XBP-1 is essential for the development and survival of dendritic cells. J. Exp. Med., 204, 2267-2275.
    • (2007) J. Exp. Med. , vol.204 , pp. 2267-2275
    • Iwakoshi, N.N.1    Pypaert, M.2    Glimcher, L.H.3
  • 58
    • 34250656185 scopus 로고    scopus 로고
    • Toxicity from different SOD1 mutants dysregulates the complement system and the neuronal regenerative response in ALS motor neurons
    • Lobsiger, C.S., Boillee, S. and Cleveland, D.W. (2007) Toxicity from different SOD1 mutants dysregulates the complement system and the neuronal regenerative response in ALS motor neurons. Proc. Natl Acad. Sci. USA, 104, 7319-7326.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 7319-7326
    • Lobsiger, C.S.1    Boillee, S.2    Cleveland, D.W.3
  • 59
    • 0037104725 scopus 로고    scopus 로고
    • Neuroprotective effects of glial cell line-derived neurotrophic factor mediated by an adeno-associated virus vector in a transgenic animal model of amyotrophic lateral sclerosis
    • Wang, L.J., Lu, Y.Y., Muramatsu, S., Ikeguchi, K., Fujimoto, K., Okada, T., Mizukami, H., Matsushita, T., Hanazono, Y., Kume, A. et al. (2002) Neuroprotective effects of glial cell line-derived neurotrophic factor mediated by an adeno-associated virus vector in a transgenic animal model of amyotrophic lateral sclerosis. J. Neurosci., 22, 6920-6928.
    • (2002) J. Neurosci. , vol.22 , pp. 6920-6928
    • Wang, L.J.1    Lu, Y.Y.2    Muramatsu, S.3    Ikeguchi, K.4    Fujimoto, K.5    Okada, T.6    Mizukami, H.7    Matsushita, T.8    Hanazono, Y.9    Kume, A.10
  • 60
    • 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., Zhai, H., Fu, R., Liu, E., Gorrie, G.H., Khan, M.S., Hung, W.Y., Bigio, E.H. 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    Zhai, H.4    Fu, R.5    Liu, E.6    Gorrie, G.H.7    Khan, M.S.8    Hung, W.Y.9    Bigio, E.H.10


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