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Volumn 288, Issue 22, 2013, Pages 15699-15711

Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: Implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

AMYOTROPHIC LATERAL SCLEROSIS; DISEASE SPREADING; MOTOR NEURON DISEASE; OVER-EXPRESSION; PROTEIN SECRETION; SECRETED PROTEIN; SECRETORY PATHWAYS; SUPEROXIDE DISMUTASES;

EID: 84878389217     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.425066     Document Type: Article
Times cited : (217)

References (65)
  • 1
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders. ALS and beyond
    • Ilieva, H., Polymenidou, M., and Cleveland, D. W. (2009) Non-cell autonomous toxicity in neurodegenerative disorders. ALS and beyond. J. Cell Biol. 187, 761-772
    • (2009) J. Cell Biol. , vol.187 , pp. 761-772
    • Ilieva, H.1    Polymenidou, M.2    Cleveland, D.W.3
  • 3
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein, J. D., Van Kammen, M., Levey, A. I., Martin, L. J., and Kuncl, R. W. (1995) Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann. Neurol. 38, 73-84
    • (1995) Ann. Neurol. , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 4
    • 0035189072 scopus 로고    scopus 로고
    • Transgenic SOD1 G93A mice develop reduced GLT-1 in spinal cord without alterations in cerebrospinal fluid glutamate levels
    • DOI 10.1046/j.1471-4159.2001.00572.x
    • Bendotti, C., Tortarolo, M., Suchak, S. K., Calvaresi, N., Carvelli, L., Bastone, A., Rizzi, M., Rattray, M., and Mennini, T. (2001) Transgenic SOD1 G93A mice develop reduced GLT-1 in spinal cord without alterations in cerebrospinal fluid glutamate levels. J. Neurochem. 79, 737-746 (Pubitemid 33086511)
    • (2001) Journal of Neurochemistry , vol.79 , Issue.4 , pp. 737-746
    • Bendotti, C.1    Tortarolo, M.2    Suchak, S.K.3    Calvaresi, N.4    Carvelli, L.5    Bastone, A.6    Rizzi, M.7    Rattray, M.8    Mennini, T.9
  • 7
    • 56549115885 scopus 로고    scopus 로고
    • Non-cell-autonomous effect of human SOD1 G37R astrocytes on motor neurons derived from human embryonic stem cells
    • Marchetto, M. C., Muotri, A. R., Mu, Y., Smith, A. M., Cezar, G. G., and Gage, F. H. (2008) Non-cell-autonomous effect of human SOD1 G37R astrocytes on motor neurons derived from human embryonic stem cells. Cell Stem Cell 3, 649-657
    • (2008) Cell Stem Cell , vol.3 , pp. 649-657
    • Marchetto, M.C.1    Muotri, A.R.2    Mu, Y.3    Smith, A.M.4    Cezar, G.G.5    Gage, F.H.6
  • 8
    • 34247473080 scopus 로고    scopus 로고
    • Non-cell autonomous effect of glia on motor neurons in an embryonic stem cell-based ALS model
    • DOI 10.1038/nn1885, PII NN1885
    • Di Giorgio, F. P., Carrasco, M. A., Siao, M. C., Maniatis, T., and Eggan, K. (2007) Non-cell autonomous effect of glia on motor neurons in an embryonic stem cell-based ALS model. Nat. Neurosci. 10, 608-614 (Pubitemid 46652442)
    • (2007) Nature Neuroscience , vol.10 , Issue.5 , pp. 608-614
    • Di, G.F.P.1    Carrasco, M.A.2    Siao, M.C.3    Maniatis, T.4    Eggan, K.5
  • 9
    • 34247475338 scopus 로고    scopus 로고
    • Astrocytes expressing ALS-linked mutated SOD1 release factors selectively toxic to motor neurons
    • DOI 10.1038/nn1876, PII NN1876
    • Nagai, M., Re, D. B., Nagata, T., Chalazonitis, A., Jessell, T. M., Wichterle, H., and Przedborski, S. (2007) Astrocytes expressing ALS-linked mutated SOD1release factors selectively toxic to motor neurons. Nat. Neurosci. 10, 615-622 (Pubitemid 46652435)
    • (2007) Nature Neuroscience , vol.10 , Issue.5 , pp. 615-622
    • Nagai, M.1    Re, D.B.2    Nagata, T.3    Chalazonitis, A.4    Jessell, T.M.5    Wichterle, H.6    Przedborski, S.7
  • 10
    • 33645881327 scopus 로고    scopus 로고
    • Increased glutathione biosynthesis by Nrf2 activation in astrocytes prevents p75NTR-dependent motor neuron apoptosis
    • Vargas, M. R., Pehar, M., Cassina, P., Beckman, J. S., and Barbeito, L. (2006) Increased glutathione biosynthesis by Nrf2 activation in astrocytes prevents p75NTR-dependent motor neuron apoptosis. J. Neurochem. 97, 687-696
    • (2006) J. Neurochem. , vol.97 , pp. 687-696
    • Vargas, M.R.1    Pehar, M.2    Cassina, P.3    Beckman, J.S.4    Barbeito, L.5
  • 11
    • 54949126674 scopus 로고    scopus 로고
    • Focal transplantation-based astrocyte replacement is neuroprotective in a model of motor neuron disease
    • Lepore, A. C., Rauck, B., Dejea, C., Pardo, A. C., Rao, M. S., Rothstein, J. D., and Maragakis, N. J. (2008) Focal transplantation-based astrocyte replacement is neuroprotective in a model of motor neuron disease. Nat. Neurosci. 11, 1294-1301
    • (2008) Nat. Neurosci. , vol.11 , pp. 1294-1301
    • Lepore, A.C.1    Rauck, B.2    Dejea, C.3    Pardo, A.C.4    Rao, M.S.5    Rothstein, J.D.6    Maragakis, N.J.7
  • 12
    • 58149379610 scopus 로고    scopus 로고
    • Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis
    • Vargas, M. R., Johnson, D. A., Sirkis, D. W., Messing, A., and Johnson, J. A. (2008) Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis. J. Neurosci. 28, 13574-13581
    • (2008) J. Neurosci. , vol.28 , pp. 13574-13581
    • Vargas, M.R.1    Johnson, D.A.2    Sirkis, D.W.3    Messing, A.4    Johnson, J.A.5
  • 14
    • 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
  • 16
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • DOI 10.1523/JNEUROSCI.4253-04.2005
    • 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 (Pubitemid 40110771)
    • (2005) Journal of Neuroscience , vol.25 , Issue.1 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3    Da, W.Z.4    Rembach, A.5    Lopes, E.C.6    Patch, J.D.7    Hill, A.F.8    Cheema, S.S.9
  • 17
    • 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., and Julien, J. P. (2006) Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci. 9, 108-118 (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
  • 18
    • 0034956740 scopus 로고    scopus 로고
    • Superoxide dismutase in CSF from amyotrophic lateral sclerosis patients with and without CuZn-superoxide dismutase mutations
    • Jacobsson, J., Jonsson, P. A., Andersen, P. M., Forsgren, L., and Marklund, S. L. (2001) Superoxide dismutase in CSF from amyotrophic lateral sclerosis patients with and without CuZn-superoxide dismutase mutations. Brain 124, 1461-1466 (Pubitemid 32606106)
    • (2001) Brain , vol.124 , Issue.7 , pp. 1461-1466
    • Jacobsson, J.1    Jonsson, P.A.2    Andersen, P.M.3    Forsgren, L.4    Marklund, S.L.5
  • 19
    • 79952572373 scopus 로고    scopus 로고
    • Misfolded superoxide dismutase-1 in CSF from amyotrophic lateral sclerosis patients
    • Zetterström, P., Andersen, P. M., Brännström, T., and Marklund, S. L. (2011) Misfolded superoxide dismutase-1 in CSF from amyotrophic lateral sclerosis patients. J Neurochem 117, 91-99
    • (2011) J Neurochem , vol.117 , pp. 91-99
    • Zetterström, P.1    Andersen, P.M.2    Brännström, T.3    Marklund, S.L.4
  • 20
    • 24044466722 scopus 로고    scopus 로고
    • Difference in mass analysis using labeled lysines (DIMAL-K): A new, efficient proteomic quantification method applied to the analysis of astrocytic secretomes
    • DOI 10.1074/mcp.M500040-MCP200
    • Delcourt, N., Jouin, P., Poncet, J., Demey, E., Mauger, E., Bockaert, J., Marin, P., and Galéotti, N. (2005) Difference in mass analysis using labeled lysines (DIMAL-K). A new, efficient proteomic quantification method applied to the analysis of astrocytic secretomes. Mol. Cell. Proteomics 4, 1085-1094 (Pubitemid 41223368)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.8 , pp. 1085-1094
    • Delcourt, N.1    Jouin, P.2    Poncet, J.3    Demey, E.4    Mauger, E.5    Bockaert, J.6    Marin, P.7    Galeotti, N.8
  • 21
    • 77952083750 scopus 로고    scopus 로고
    • Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion
    • Greco, T. M., Seeholzer, S. H., Mak, A., Spruce, L., and Ischiropoulos, H. (2010) Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion. J. Proteome Res. 9, 2764-2774
    • (2010) J. Proteome Res. , vol.9 , pp. 2764-2774
    • Greco, T.M.1    Seeholzer, S.H.2    Mak, A.3    Spruce, L.4    Ischiropoulos, H.5
  • 23
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta. A compendium of exosomal proteins and RNA
    • Mathivanan, S., and Simpson, R. J. (2009) ExoCarta. A compendium of exosomal proteins and RNA. Proteomics 9, 4997-5000
    • (2009) Proteomics , vol.9 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 24
    • 3142630225 scopus 로고    scopus 로고
    • Exosomes: Endosomal-derived vesicles shipping extracellular messages
    • DOI 10.1016/j.ceb.2004.06.003, PII S0955067404000729
    • Février, B., and Raposo, G. (2004) Exosomes. Endosomal-derived vesicles shipping extracellular messages. Curr. Opin. Cell Biol. 16, 415-421 (Pubitemid 38903148)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 415-421
    • Fevrier, B.1    Raposo, G.2
  • 25
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • DOI 10.1038/ncb1596, PII NCB1596
    • Valadi, H., Ekström, K., Bossios, A., Sjöstrand, M., Lee, J. J., and Lötvall, J. O. (2007) Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat. Cell Biol. 9, 654-659 (Pubitemid 47214727)
    • (2007) Nature Cell Biology , vol.9 , Issue.6 , pp. 654-659
    • Valadi, H.1    Ekstrom, K.2    Bossios, A.3    Sjostrand, M.4    Lee, J.J.5    Lotvall, J.O.6
  • 26
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes. Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?
    • Bellingham, S. A., Guo, B. B., Coleman, B. M., and Hill, A. F. (2012) Exosomes. Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases? Front. Physiol. 3, 124
    • (2012) Front. Physiol. , vol.3 , pp. 124
    • Bellingham, S.A.1    Guo, B.B.2    Coleman, B.M.3    Hill, A.F.4
  • 27
    • 0345825889 scopus 로고    scopus 로고
    • Expression of SOD1 G93A or wild-type SOD1 in primary cultures of astrocytes down-regulates the glutamate transporter GLT-1: Lack of involvement of oxidative stress
    • Tortarolo, M., Crossthwaite, A. J., Conforti, L., Spencer, J. P., Williams, R. J., Bendotti, C., and Rattray, M. (2004) Expression of SOD1 G93A or wild-type SOD1 in primary cultures of astrocytes down-regulates the glutamate transporter GLT-1. Lack of involvement of oxidative stress. J. Neurochem. 88, 481-493 (Pubitemid 38084564)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.2 , pp. 481-493
    • Tortarolo, M.1    Crossthwaite, A.J.2    Conforti, L.3    Spencer, J.P.4    Williams, R.J.5    Bendotti, C.6    Rattray, M.7
  • 29
    • 18144398928 scopus 로고    scopus 로고
    • Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: Possible multifunctional role in the pathogenesis
    • DOI 10.1074/jbc.M413111200
    • Casoni, F., Basso, M., Massignan, T., Gianazza, E., Cheroni, C., Salmona, M., Bendotti, C., and Bonetto, V. (2005) Protein nitration in a mouse model of familial amyotrophic lateral sclerosis. Possible multifunctional role in the pathogenesis. J. Biol. Chem. 280, 16295-16304 (Pubitemid 40616757)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16295-16304
    • Casoni, F.1    Basso, M.2    Massignan, T.3    Gianazzail, E.4    Cheroni, C.5    Salmona, M.6    Bendotti, C.7    Bonetto, V.8
  • 30
    • 33646728858 scopus 로고    scopus 로고
    • Analysis of the cerebellar proteome in a transgenic mouse model of inherited prion disease reveals preclinical alteration of calcineurin activity
    • Biasini, E., Massignan, T., Fioriti, L., Rossi, V., Dossena, S., Salmona, M., Forloni, G., Bonetto, V., and Chiesa, R. (2006) Analysis of the cerebellar proteome in a transgenic mouse model of inherited prion disease reveals preclinical alteration of calcineurin activity. Proteomics 6, 2823-2834
    • (2006) Proteomics , vol.6 , pp. 2823-2834
    • Biasini, E.1    Massignan, T.2    Fioriti, L.3    Rossi, V.4    Dossena, S.5    Salmona, M.6    Forloni, G.7    Bonetto, V.8    Chiesa, R.9
  • 31
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin, D. J., Hojrup, P., and Bleasby, A. J. (1993) Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 3, 327-332
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 32
  • 33
    • 0033547879 scopus 로고    scopus 로고
    • S-100β protein is upregulated in astrocytes and motor neurons in the spinal cord of patients with amyotrophic lateral sclerosis
    • DOI 10.1016/S0304-3940(98)01001-5, PII S0304394098010015
    • Migheli, A., Cordera, S., Bendotti, C., Atzori, C., Piva, R., and Schiffer, D. (1999) S-100β protein is upregulated in astrocytes and motor neurons in the spinal cord of patients with amyotrophic lateral sclerosis. Neurosci. Lett. 261, 25-28 (Pubitemid 29100067)
    • (1999) Neuroscience Letters , vol.261 , Issue.1-2 , pp. 25-28
    • Migheli, A.1    Cordera, S.2    Bendotti, C.3    Atzori, C.4    Piva, R.5    Schiffer, D.6
  • 34
    • 0032559609 scopus 로고    scopus 로고
    • Increase of glial fibrillary acidic protein fragments in the spinal cord of motor neuron degeneration mutant mouse
    • DOI 10.1016/S0006-8993(97)00612-4, PII S0006899397006124
    • Fujita, K., Yamauchi, M., Matsui, T., Titani, K., Takahashi, H., Kato, T., Isomura, G., Ando, M., and Nagata, Y. (1998) Increase of glial fibrillary acidic protein fragments in the spinal cord of motor neuron degeneration mutant mouse. Brain Res. 785, 31-40 (Pubitemid 28194751)
    • (1998) Brain Research , vol.785 , Issue.1 , pp. 31-40
    • Fujita, K.1    Yamauchi, M.2    Matsui, T.3    Titani, K.4    Takahashi, H.5    Kato, T.6    Isomura, G.7    Ando, M.8    Nagata, Y.9
  • 35
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley, A. J. (2006) Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16, 522-529
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 36
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark, H. (2009) Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513-525
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 38
    • 0026704344 scopus 로고
    • Comparison of the Coomassie brilliant blue, bicinchoninic acid and Lowry quantitation assays, using non-glycosylated and glycosylated proteins
    • DOI 10.1016/0165-022X(94)90078-7
    • Fountoulakis, M., Juranville, J. F., and Manneberg, M. (1992) Comparison of the Coomassie Brilliant Blue, bicinchoninic acid and Lowry quantitation assays, using non-glycosylated and glycosylated proteins. J. Biochem. Biophys. Methods 24, 265-274 (Pubitemid 124012610)
    • (1994) Journal of Biochemical and Biophysical Methods , vol.24 , Issue.3-4 , pp. 265-274
    • Fountoulakis, M.1
  • 39
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0. Discriminating signal peptides from transmembrane regions
    • Petersen, T. N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0. Discriminating signal peptides from transmembrane regions. Nat. Methods 8, 785-786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 40
    • 35448956015 scopus 로고    scopus 로고
    • Evidence for secretion of Cu,Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis
    • DOI 10.1016/j.neulet.2007.09.024, PII S0304394007010051
    • Gomes, C., Keller, S., Altevogt, P., and Costa, J. (2007) Evidence for secretion of Cu Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis. Neurosci. Lett. 428, 43-46 (Pubitemid 47633803)
    • (2007) Neuroscience Letters , vol.428 , Issue.1 , pp. 43-46
    • Gomes, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 42
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Théry, C., Ostrowski, M., and Segura, E. (2009) Membrane vesicles as conveyors of immune responses. Nat. Rev. Immunol. 9, 581-593
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 581-593
    • Théry, C.1    Ostrowski, M.2    Segura, E.3
  • 43
    • 84875234646 scopus 로고    scopus 로고
    • Exosomes. Vesicular carriers for intercellular communication in neurodegenerative disorders
    • Schneider, A., and Simons, M. (2013) Exosomes. Vesicular carriers for intercellular communication in neurodegenerative disorders. Cell Tissue Res. 352, 33-47
    • (2013) Cell Tissue Res. , vol.352 , pp. 33-47
    • Schneider, A.1    Simons, M.2
  • 44
    • 80055074312 scopus 로고    scopus 로고
    • Astrocytes carrying the superoxide dismutase 1 (SOD1G93A) mutation induce wild-type motor neuron degeneration in vivo
    • Papadeas, S. T., Kraig, S. E., O'Banion, C., Lepore, A. C., and Maragakis, N. J. (2011) Astrocytes carrying the superoxide dismutase 1 (SOD1G93A) mutation induce wild-type motor neuron degeneration in vivo. Proc. Natl. Acad. Sci. U.S.A. 108, 17803-17808
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17803-17808
    • Papadeas, S.T.1    Kraig, S.E.2    O'Banion, C.3    Lepore, A.C.4    Maragakis, N.J.5
  • 45
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum. Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. (1999) Stress signaling from the lumen of the endoplasmic reticulum. Coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-1233
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 47
    • 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
    • DOI 10.1074/jbc.M603393200
    • 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., and Horne, M. K. (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 (Pubitemid 44537023)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , 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    Horne, M.K.11
  • 48
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin, J. D., Farg, M. A., Walker, A. K., McLean, C., Tomas, D., and Horne, M. K. (2008) Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol. Dis. 30, 400-407
    • (2008) Neurobiol. Dis. , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5    Horne, M.K.6
  • 50
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated Tauis secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C., and Hall, G. F. (2012) Exosome-associated Tauis secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J. Biol. Chem. 287, 3842-3849
    • (2012) J. Biol. Chem. , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Saman, S.6    Jackson, B.7    McKee, A.C.8    Alvarez, V.E.9    Lee, N.C.10    Hall, G.F.11
  • 52
    • 84862274671 scopus 로고    scopus 로고
    • Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4). Potential mechanism of apoptosis induction in Alzheimer disease (AD)
    • Wang, G., Dinkins, M., He, Q., Zhu, G., Poirier, C., Campbell, A., Mayer-Proschel, M., and Bieberich, E. (2012) Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4). Potential mechanism of apoptosis induction in Alzheimer disease (AD). J. Biol. Chem. 287, 21384-21395
    • (2012) J. Biol. Chem. , vol.287 , pp. 21384-21395
    • Wang, G.1    Dinkins, M.2    He, Q.3    Zhu, G.4    Poirier, C.5    Campbell, A.6    Mayer-Proschel, M.7    Bieberich, E.8
  • 53
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M., and Bremer, S. (2012) Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117-123
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 54
    • 84864874006 scopus 로고    scopus 로고
    • The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins
    • Piccirillo, R., and Goldberg, A. L. (2012) The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins. EMBO J. 31, 3334-3350
    • (2012) EMBO J. , vol.31 , pp. 3334-3350
    • Piccirillo, R.1    Goldberg, A.L.2
  • 55
    • 79957663006 scopus 로고    scopus 로고
    • CHIP promotes the degradation of mutant SOD1 by reducing its interaction with VCP and S6/S6′ subunits of 26S proteasome
    • Choi, J. S., and Lee, D. H. (2010) CHIP promotes the degradation of mutant SOD1 by reducing its interaction with VCP and S6/S6′ subunits of 26S proteasome. Anim. Cells Syst. 14, 1-10
    • (2010) Anim. Cells Syst. , vol.14 , pp. 1-10
    • Choi, J.S.1    Lee, D.H.2
  • 59
    • 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., Larivière, R., and Julien, J. P. (2010) 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 113, 1188-1199
    • (2010) J Neurochem , vol.113 , pp. 1188-1199
    • Gros-Louis, F.1    Soucy, G.2    Larivière, R.3    Julien, J.P.4
  • 63
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Münch, C., O'Brien, J., and Bertolotti, A. (2011) Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. U.S.A. 108, 3548-3553
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3548-3553
    • Münch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 64
    • 70349581626 scopus 로고    scopus 로고
    • ALS motor phenotype heterogeneity, focality, and spread. Deconstructing motor neuron degeneration
    • Ravits, J. M., and La Spada, A. R. (2009) ALS motor phenotype heterogeneity, focality, and spread. Deconstructing motor neuron degeneration. Neurology 73, 805-811
    • (2009) Neurology , vol.73 , pp. 805-811
    • Ravits, J.M.1    La Spada, A.R.2


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