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Volumn 7, Issue 11, 2012, Pages

Hsp40 Gene Therapy Exerts Therapeutic Effects on Polyglutamine Disease Mice via a Non-Cell Autonomous Mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 40; PARVOVIRUS VECTOR; POLYGLUTAMINE; POLYGLUTAMINE BINDING PEPTIDE 1; UNCLASSIFIED DRUG;

EID: 84870581997     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051069     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 0034329159 scopus 로고    scopus 로고
    • Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease
    • Gusella JF, MacDonald ME, (2000) Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat Rev Neurosci 1: 109-115.
    • (2000) Nat Rev Neurosci , vol.1 , pp. 109-115
    • Gusella, J.F.1    MacDonald, M.E.2
  • 2
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr HT, Zoghbi HY, (2007) Trinucleotide repeat disorders. Annu Rev Neurosci 30: 575-621.
    • (2007) Annu Rev Neurosci , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 3
    • 0141891215 scopus 로고    scopus 로고
    • Pathogenesis of polyglutamine disorders: aggregation revisited
    • Michalik A, Van Broeckhoven C, (2003) Pathogenesis of polyglutamine disorders: aggregation revisited. Hum Mol Genet 12 Spec No 2: R173-186.
    • (2003) Hum Mol Genet 12 Spec No , vol.2
    • Michalik, A.1    Van Broeckhoven, C.2
  • 4
    • 37849030901 scopus 로고    scopus 로고
    • Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum Mol Genet 16 Spec No
    • Shao J, Diamond MI, (2007) Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum Mol Genet 16 Spec No. 2: R115-123.
    • (2007) , vol.2
    • Shao, J.1    Diamond, M.I.2
  • 5
    • 58949102251 scopus 로고    scopus 로고
    • Conformational changes and aggregation of expanded polyglutamine proteins as therapeutic targets of the polyglutamine diseases: exposed β-sheet hypothesis
    • Nagai Y, Popiel HA, (2008) Conformational changes and aggregation of expanded polyglutamine proteins as therapeutic targets of the polyglutamine diseases: exposed β-sheet hypothesis. Curr Pharm Des 14: 3267-3279.
    • (2008) Curr Pharm Des , vol.14 , pp. 3267-3279
    • Nagai, Y.1    Popiel, H.A.2
  • 6
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: protein misfolding revisited
    • Williams AJ, Paulson HL, (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci 31: 521-528.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 7
    • 69949170793 scopus 로고    scopus 로고
    • The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies
    • Bauer PO, Nukina N, (2009) The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies. J Neurochem 110: 1737-1765.
    • (2009) J Neurochem , vol.110 , pp. 1737-1765
    • Bauer, P.O.1    Nukina, N.2
  • 8
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A, Rajendran L, (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64: 783-790.
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 9
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R, (2010) Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 11: 301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 11
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost B, Diamond MI, (2010) Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 11: 155-159.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 12
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates G, (2003) Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361: 1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 13
    • 33745750191 scopus 로고    scopus 로고
    • Therapeutic approaches to polyglutamine diseases: combating protein misfolding and aggregation
    • Herbst M, Wanker EE, (2006) Therapeutic approaches to polyglutamine diseases: combating protein misfolding and aggregation. Curr Pharm Des 12: 2543-2555.
    • (2006) Curr Pharm Des , vol.12 , pp. 2543-2555
    • Herbst, M.1    Wanker, E.E.2
  • 14
    • 0034615932 scopus 로고    scopus 로고
    • Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening
    • Nagai Y, Tucker T, Ren H, Kenan DJ, Henderson BS, et al. (2000) Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J Biol Chem 275: 10437-10442.
    • (2000) J Biol Chem , vol.275 , pp. 10437-10442
    • Nagai, Y.1    Tucker, T.2    Ren, H.3    Kenan, D.J.4    Henderson, B.S.5
  • 16
    • 84870326617 scopus 로고    scopus 로고
    • The aggregation inhibitor peptide QBP1 as a therapeutic molecule for the polyglutamine neurodegenerative diseases
    • Popiel HA, Burke JR, Strittmatter WJ, Oishi S, Fujii N, et al. (2011) The aggregation inhibitor peptide QBP1 as a therapeutic molecule for the polyglutamine neurodegenerative diseases. J Amino Acids 2011: 265084.
    • (2011) J Amino Acids , vol.2011 , pp. 265084
    • Popiel, H.A.1    Burke, J.R.2    Strittmatter, W.J.3    Oishi, S.4    Fujii, N.5
  • 17
    • 12444292683 scopus 로고    scopus 로고
    • Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila
    • Nagai Y, Fujikake N, Ohno K, Higashiyama H, Popiel HA, et al. (2003) Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila. Hum Mol Genet 12: 1253-1259.
    • (2003) Hum Mol Genet , vol.12 , pp. 1253-1259
    • Nagai, Y.1    Fujikake, N.2    Ohno, K.3    Higashiyama, H.4    Popiel, H.A.5
  • 18
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek K, Lewandowska A, Zietkiewicz S, (2008) Chaperones in control of protein disaggregation. EMBO J 27: 328-335.
    • (2008) EMBO J , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 19
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA, (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11: 579-592.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 20
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M, (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 21
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, et al. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 23: 425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5
  • 22
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P, Benzer S, (2000) Genetic suppression of polyglutamine toxicity in Drosophila. Science 287: 1837-1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 24
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila
    • Chan HY, Warrick JM, Gray-Board GL, Paulson HL, Bonini NM, (2000) Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum Mol Genet 9: 2811-2820.
    • (2000) Hum Mol Genet , vol.9 , pp. 2811-2820
    • Chan, H.Y.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson, H.L.4    Bonini, N.M.5
  • 26
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings CJ, Sun Y, Opal P, Antalffy B, Mestril R, et al. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum Mol Genet 10: 1511-1518.
    • (2001) Hum Mol Genet , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5
  • 27
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H, Katsuno M, Minamiyama M, Sang C, Pagoulatos G, et al. (2003) Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J Neurosci 23: 2203-2211.
    • (2003) J Neurosci , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5
  • 28
    • 0347928859 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression
    • Hansson O, Nylandsted J, Castilho RF, Leist M, Jaattela M, et al. (2003) Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression. Brain Res 970: 47-57.
    • (2003) Brain Res , vol.970 , pp. 47-57
    • Hansson, O.1    Nylandsted, J.2    Castilho, R.F.3    Leist, M.4    Jaattela, M.5
  • 29
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay DG, Sathasivam K, Tobaben S, Stahl B, Marber M, et al. (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum Mol Genet 13: 1389-1405.
    • (2004) Hum Mol Genet , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5
  • 31
    • 0036428818 scopus 로고    scopus 로고
    • Adeno-associated virus vectors for gene transfer to the brain
    • Okada T, Nomoto T, Shimazaki K, Lijun W, Lu Y, et al. (2002) Adeno-associated virus vectors for gene transfer to the brain. Methods 28: 237-247.
    • (2002) Methods , vol.28 , pp. 237-247
    • Okada, T.1    Nomoto, T.2    Shimazaki, K.3    Lijun, W.4    Lu, Y.5
  • 32
    • 0037868094 scopus 로고    scopus 로고
    • Viral vectors for gene delivery to the nervous system
    • Davidson BL, Breakefield XO, (2003) Viral vectors for gene delivery to the nervous system. Nat Rev Neurosci 4: 353-364.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 353-364
    • Davidson, B.L.1    Breakefield, X.O.2
  • 33
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini L, Sathasivam K, Seller M, Cozens B, Harper A, et al. (1996) Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87: 493-506.
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5
  • 35
    • 75949094261 scopus 로고    scopus 로고
    • A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation
    • Hageman J, Rujano MA, van Waarde MA, Kakkar V, Dirks RP, et al. (2010) A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. Mol Cell 37: 355-369.
    • (2010) Mol Cell , vol.37 , pp. 355-369
    • Hageman, J.1    Rujano, M.A.2    van Waarde, M.A.3    Kakkar, V.4    Dirks, R.P.5
  • 36
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross CA, Poirier MA, (2005) Opinion: What is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol 6: 891-898.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 37
    • 34249286265 scopus 로고    scopus 로고
    • Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease
    • Howarth JL, Kelly S, Keasey MP, Glover CP, Lee YB, et al. (2007) Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease. Mol Ther 15: 1100-1105.
    • (2007) Mol Ther , vol.15 , pp. 1100-1105
    • Howarth, J.L.1    Kelly, S.2    Keasey, M.P.3    Glover, C.P.4    Lee, Y.B.5
  • 38
    • 77956262279 scopus 로고    scopus 로고
    • A phase I study of aromatic L-amino acid decarboxylase gene therapy for Parkinson's disease
    • Muramatsu S, Fujimoto K, Kato S, Mizukami H, Asari S, et al. (2010) A phase I study of aromatic L-amino acid decarboxylase gene therapy for Parkinson's disease. Mol Ther 18: 1731-1735.
    • (2010) Mol Ther , vol.18 , pp. 1731-1735
    • Muramatsu, S.1    Fujimoto, K.2    Kato, S.3    Mizukami, H.4    Asari, S.5
  • 39
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, et al. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 11: 219-225.
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5
  • 40
    • 84866322000 scopus 로고    scopus 로고
    • Visualization of cell-to-cell transmission of mutant huntingtin oligomers
    • Herrera F, Tenreiro S, Miller-Fleming L, Outeiro TF, (2011) Visualization of cell-to-cell transmission of mutant huntingtin oligomers. PLoS Curr 3: RRN1210.
    • (2011) PLoS Curr , vol.3
    • Herrera, F.1    Tenreiro, S.2    Miller-Fleming, L.3    Outeiro, T.F.4
  • 43
    • 77749319356 scopus 로고    scopus 로고
    • Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
    • Bauer PO, Goswami A, Wong HK, Okuno M, Kurosawa M, et al. (2010) Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein. Nat Biotechnol 28: 256-263.
    • (2010) Nat Biotechnol , vol.28 , pp. 256-263
    • Bauer, P.O.1    Goswami, A.2    Wong, H.K.3    Okuno, M.4    Kurosawa, M.5
  • 44
    • 0027486385 scopus 로고
    • Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ
    • Ohtsuka K, (1993) Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. Biochem Biophys Res Commun 197: 235-240.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 235-240
    • Ohtsuka, K.1


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