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Volumn 420, Issue 3, 2012, Pages 558-563

AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington's disease

Author keywords

Endoplasmic reticulum stress; Gene therapy; Htt aggregation; Huntington's disease; Unfolded protein response; XBP1

Indexed keywords

HUNTINGTIN; HYBRID PROTEIN; PARVOVIRUS VECTOR; X BOX BINDING PROTEIN 1;

EID: 84859577308     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.033     Document Type: Article
Times cited : (71)

References (44)
  • 1
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: protein misfolding revisited
    • Williams A.J., Paulson H.L. Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci. 2008, 31:521-528.
    • (2008) Trends Neurosci. , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 2
    • 21444443855 scopus 로고    scopus 로고
    • Dynamic mutations in human genes: a review of trinucleotide repeat disease
    • Longshore J.W., Tarleton J. Dynamic mutations in human genes: a review of trinucleotide repeat disease. J. Genetic 1996, 75:193-217.
    • (1996) J. Genetic , vol.75 , pp. 193-217
    • Longshore, J.W.1    Tarleton, J.2
  • 3
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • Zuccato C., Valenza M., Cattaneo E. Molecular mechanisms and potential therapeutical targets in Huntington's disease. Physiol. Rev. 2010, 90:905-981.
    • (2010) Physiol. Rev. , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3
  • 4
    • 78650827764 scopus 로고    scopus 로고
    • Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease
    • Vidal R., Caballero B., Couve A., Hetz C. Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease. Curr. Mol. Med. 2011, 11:1-12.
    • (2011) Curr. Mol. Med. , vol.11 , pp. 1-12
    • Vidal, R.1    Caballero, B.2    Couve, A.3    Hetz, C.4
  • 5
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: a glimpse into the ER
    • Matus S., Glimcher L.H., Hetz C. Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr. Opin. Cell Biol. 2011, 23:239-252.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 6
    • 84856111924 scopus 로고    scopus 로고
    • The Unfolded Protein Response: Controlling cell fate decisions under ER stress and beyond
    • Hetz C. The Unfolded Protein Response: Controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 2012, 13:1-14.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 1-14
    • Hetz, C.1
  • 7
    • 79958033194 scopus 로고    scopus 로고
    • Modulating stress responses by the UPRosome: A matter of life and death
    • Woehlbier U., Hetz C. Modulating stress responses by the UPRosome: A matter of life and death. Trends Biochem. Sci. 2011, 36:329-337.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 329-337
    • Woehlbier, U.1    Hetz, C.2
  • 8
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I., Ron D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 2011, 13:184-190.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 9
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 2007, 8:519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 10
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 11
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., Kaufman R.J. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 2002, 16:452-466.
    • (2002) Genes Dev. , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 13
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee A.H., Iwakoshi N.N., Glimcher L.H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell Biol. 2003, 23:7448-7459.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 16
    • 83455169115 scopus 로고    scopus 로고
    • IRE1 plays an essential role in ER stress-mediated aggregation of mutant Huntingtin via the inhibition of autophagy flux
    • Lee H., Noh J.Y., Oh Y., Kim Y., Chang J.W., Chung C.W., Lee S.T., Kim M., Ryu H., Jung Y.K. IRE1 plays an essential role in ER stress-mediated aggregation of mutant Huntingtin via the inhibition of autophagy flux. Hum. Mol. Genet. 2012, 21:101-114.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 101-114
    • Lee, H.1    Noh, J.Y.2    Oh, Y.3    Kim, Y.4    Chang, J.W.5    Chung, C.W.6    Lee, S.T.7    Kim, M.8    Ryu, H.9    Jung, Y.K.10
  • 17
    • 78349312360 scopus 로고    scopus 로고
    • Impaired ATF6alpha processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease
    • Fernandez-Fernandez M.R., Ferrer I., Lucas J.J. Impaired ATF6alpha processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease. Neurobiol. Dis. 2011, 41:23-32.
    • (2011) Neurobiol. Dis. , vol.41 , pp. 23-32
    • Fernandez-Fernandez, M.R.1    Ferrer, I.2    Lucas, J.J.3
  • 19
    • 76249091683 scopus 로고    scopus 로고
    • Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear Huntingtin fragments in a mouse model of Huntington disease
    • Cho K.J., Lee B.I., Cheon S.Y., Kim H.W., Kim H.J., Kim G.W. Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear Huntingtin fragments in a mouse model of Huntington disease. Neuroscience 2009, 163:1128-1134.
    • (2009) Neuroscience , vol.163 , pp. 1128-1134
    • Cho, K.J.1    Lee, B.I.2    Cheon, S.Y.3    Kim, H.W.4    Kim, H.J.5    Kim, G.W.6
  • 20
    • 80054037000 scopus 로고    scopus 로고
    • Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant Huntingtin
    • Lajoie P., Snapp E.L. Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant Huntingtin. J. Cell Sci. 2011, 124:3332-3343.
    • (2011) J. Cell Sci. , vol.124 , pp. 3332-3343
    • Lajoie, P.1    Snapp, E.L.2
  • 22
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald M.L., Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 2008, 22:3308-3319.
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 23
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 2002, 16:1345-1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 24
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai Y.C., Fishman P.S., Thakor N.V., Oyler G.A. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 2003, 278:22044-22055.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 26
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang H., Liu C., Zhong Y., Luo S., Monteiro M.J., Fang S. Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One 2010, 5:e8905.
    • (2010) PLoS One , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 30
    • 73449097110 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system reveals a homeostatic switch to activate autophagy
    • Matus S., Nassif M., Glimcher L.H., Hetz C. XBP-1 deficiency in the nervous system reveals a homeostatic switch to activate autophagy. Autophagy 2009, 5:1226-1228.
    • (2009) Autophagy , vol.5 , pp. 1226-1228
    • Matus, S.1    Nassif, M.2    Glimcher, L.H.3    Hetz, C.4
  • 32
    • 84859590423 scopus 로고    scopus 로고
    • H.C., Activation of the Unfolded Protein Response enhances motor recovery after spinal cord injury, Cell Death Disease, (in press).
    • V. Valenzuela, E. Collyer, D. Armentano, G. Parsons, F. Court, H. C., Activation of the Unfolded Protein Response enhances motor recovery after spinal cord injury, Cell Death Disease, (in press).
    • Valenzuela, V.1    Collyer, E.2    Armentano, D.3    Parsons, G.4    Court, F.5
  • 33
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate Huntingtin aggregation nuclear entry and toxicity
    • Atwal R.S., Xia J., Pinchev D., Taylor J., Epand R.M., Truant R. Huntingtin has a membrane association signal that can modulate Huntingtin aggregation nuclear entry and toxicity. Hum. Mol. Genet. 2007, 16:2600-2615.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 34
    • 34347252689 scopus 로고    scopus 로고
    • Production and characterization of adeno-associated viral vectors
    • Grieger J.C., Choi V.W., Samulski R.J. Production and characterization of adeno-associated viral vectors. Nat. Protocl. 2006, 1:1412-1428.
    • (2006) Nat. Protocl. , vol.1 , pp. 1412-1428
    • Grieger, J.C.1    Choi, V.W.2    Samulski, R.J.3
  • 35
    • 0036805547 scopus 로고    scopus 로고
    • Fast and reliable titration of recombinant adeno-associated virus type-2 using quantitative real-time PCR
    • Rohr U.P., Wulf M.A., Stahn S., Steidl U., Haas R., Kronenwett R. Fast and reliable titration of recombinant adeno-associated virus type-2 using quantitative real-time PCR. J. Virol. Methods 2002, 106:81-88.
    • (2002) J. Virol. Methods , vol.106 , pp. 81-88
    • Rohr, U.P.1    Wulf, M.A.2    Stahn, S.3    Steidl, U.4    Haas, R.5    Kronenwett, R.6
  • 37
    • 0036580677 scopus 로고    scopus 로고
    • Lentiviral-mediated delivery of mutant Huntingtin in the striatum of rats induces a selective neuropathology modulated by polyglutamine repeat size, Huntingtin expression levels, and protein length
    • de Almeida L.P., Ross C.A., Zala D., Aebischer P., Deglon N. Lentiviral-mediated delivery of mutant Huntingtin in the striatum of rats induces a selective neuropathology modulated by polyglutamine repeat size, Huntingtin expression levels, and protein length. J. Neurosci. 2002, 22:3473-3483.
    • (2002) J. Neurosci. , vol.22 , pp. 3473-3483
    • de Almeida, L.P.1    Ross, C.A.2    Zala, D.3    Aebischer, P.4    Deglon, N.5
  • 39
    • 42549134402 scopus 로고    scopus 로고
    • AAV vector-mediated RNAi of mutant Huntingtin expression is neuroprotective in a novel genetic rat model of Huntington's disease
    • Franich N.R., Fitzsimons H.L., Fong D.M., Klugmann M., During M.J., Young D. AAV vector-mediated RNAi of mutant Huntingtin expression is neuroprotective in a novel genetic rat model of Huntington's disease. Mol. Ther. 2008, 16:947-956.
    • (2008) Mol. Ther. , vol.16 , pp. 947-956
    • Franich, N.R.1    Fitzsimons, H.L.2    Fong, D.M.3    Klugmann, M.4    During, M.J.5    Young, D.6
  • 42
    • 33846219134 scopus 로고    scopus 로고
    • Unfolded protein response in a Drosophila model for retinal degeneration
    • Ryoo H.D., Domingos P.M., Kang M.J., Steller H. Unfolded protein response in a Drosophila model for retinal degeneration. EMBO J. 2007, 26:242-252.
    • (2007) EMBO J. , vol.26 , pp. 242-252
    • Ryoo, H.D.1    Domingos, P.M.2    Kang, M.J.3    Steller, H.4
  • 43
    • 77958529500 scopus 로고    scopus 로고
    • The unfolded protein response protects from tau neurotoxicity in vivo
    • Loewen C.A., Feany M.B. The unfolded protein response protects from tau neurotoxicity in vivo. PLoS One 2010, 5.
    • (2010) PLoS One , vol.5
    • Loewen, C.A.1    Feany, M.B.2
  • 44
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactom
    • Hetz C., Glimcher L.H. Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactom. Mol. Cell 2009, 35:551-561.
    • (2009) Mol. Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2


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