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Volumn 92, Issue 2, 2012, Pages 194-201

Prion-induced toxicity in PrP transgenic Drosophila

Author keywords

Conformation; Drosophila; Neurotoxicity; Prion disease; PrP; Transgenic

Indexed keywords

PRION PROTEIN;

EID: 84862787748     PISSN: 00144800     EISSN: 10960945     Source Type: Journal    
DOI: 10.1016/j.yexmp.2012.01.005     Document Type: Article
Times cited : (29)

References (65)
  • 1
    • 34250796761 scopus 로고    scopus 로고
    • Insights into prion strains and neurotoxicity
    • Aguzzi A., et al. Insights into prion strains and neurotoxicity. Nature Reviews Molecular Cell Biology 2007, 8:552-561.
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , pp. 552-561
    • Aguzzi, A.1
  • 2
    • 48249126806 scopus 로고    scopus 로고
    • The prion's elusive reason for being
    • Aguzzi A., et al. The prion's elusive reason for being. Annual Review of Neuroscience 2008, 31:439-477.
    • (2008) Annual Review of Neuroscience , vol.31 , pp. 439-477
    • Aguzzi, A.1
  • 3
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy
    • Anderson M., et al. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. Journal of Molecular Biology 2006, 358:580-596.
    • (2006) Journal of Molecular Biology , vol.358 , pp. 580-596
    • Anderson, M.1
  • 5
    • 0034740298 scopus 로고    scopus 로고
    • Autonomic nervous system innervation of lymphoid territories in spleen: a possible involvement of noradrenergic neurons for prion neuroinvasion in natural scrapie
    • Bencsik A., et al. Autonomic nervous system innervation of lymphoid territories in spleen: a possible involvement of noradrenergic neurons for prion neuroinvasion in natural scrapie. Journal of Neurovirology 2001, 7:447-453.
    • (2001) Journal of Neurovirology , vol.7 , pp. 447-453
    • Bencsik, A.1
  • 6
    • 29444455075 scopus 로고    scopus 로고
    • Drosophila as a model for human neurodegenerative disease
    • Bilen J., Bonini N.M. Drosophila as a model for human neurodegenerative disease. Annual Review of Genetics 2005, 39:153-171.
    • (2005) Annual Review of Genetics , vol.39 , pp. 153-171
    • Bilen, J.1    Bonini, N.M.2
  • 7
    • 0032746253 scopus 로고    scopus 로고
    • Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells
    • Brown K.L., et al. Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells. Nature Medicine 1999, 5:1308-1312.
    • (1999) Nature Medicine , vol.5 , pp. 1308-1312
    • Brown, K.L.1
  • 8
    • 0027740178 scopus 로고
    • Scrapie strain variation and mutation
    • Bruce M.E. Scrapie strain variation and mutation. British Medical Bulletin 1993, 49:822-838.
    • (1993) British Medical Bulletin , vol.49 , pp. 822-838
    • Bruce, M.E.1
  • 9
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002, 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1
  • 10
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H., et al. Mice devoid of PrP are resistant to scrapie. Cell 1993, 73:1339-1347.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1
  • 11
    • 0028535880 scopus 로고
    • High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene
    • Bueler H., et al. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Molecular Medicine 1994, 1:19-30.
    • (1994) Molecular Medicine , vol.1 , pp. 19-30
    • Bueler, H.1
  • 12
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J., et al. In vitro generation of infectious scrapie prions. Cell 2005, 121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1
  • 13
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey B., Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annual Review of Neuroscience 2003, 26:267-298.
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 14
    • 0038128629 scopus 로고    scopus 로고
    • Molecular distinction between pathogenic and infectious properties of the prion protein
    • Chiesa R., et al. Molecular distinction between pathogenic and infectious properties of the prion protein. Journal of Virology 2003, 77:7611-7622.
    • (2003) Journal of Virology , vol.77 , pp. 7611-7622
    • Chiesa, R.1
  • 15
    • 77958462553 scopus 로고    scopus 로고
    • A Drosophila model of GSS syndrome suggests defects in active zones are responsible for pathogenesis of GSS syndrome
    • Choi J.K., et al. A Drosophila model of GSS syndrome suggests defects in active zones are responsible for pathogenesis of GSS syndrome. Human Molecular Genetics 2010, 19:4474-4489.
    • (2010) Human Molecular Genetics , vol.19 , pp. 4474-4489
    • Choi, J.K.1
  • 16
    • 0029161777 scopus 로고
    • Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie
    • Clouscard C., et al. Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie. The Journal of General Virology 1995, 76(Pt 8):2097-2101.
    • (1995) The Journal of General Virology , vol.76 , Issue.PART 8 , pp. 2097-2101
    • Clouscard, C.1
  • 17
    • 0033600407 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease
    • Collinge J. Variant Creutzfeldt-Jakob disease. Lancet 1999, 354:317-323.
    • (1999) Lancet , vol.354 , pp. 317-323
    • Collinge, J.1
  • 18
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: their causes and molecular basis
    • Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annual Review of Neuroscience 2001, 24:519-550.
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 519-550
    • Collinge, J.1
  • 19
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J., Clarke A.R. A general model of prion strains and their pathogenicity. Science 2007, 318:930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 20
    • 0035025625 scopus 로고    scopus 로고
    • Efficient transmission of two different sheep scrapie isolates in transgenic mice expressing the ovine PrP gene
    • Crozet C., et al. Efficient transmission of two different sheep scrapie isolates in transgenic mice expressing the ovine PrP gene. Journal of Virology 2001, 75:5328-5334.
    • (2001) Journal of Virology , vol.75 , pp. 5328-5334
    • Crozet, C.1
  • 23
    • 15744401372 scopus 로고    scopus 로고
    • Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells
    • Feraudet C., et al. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. The Journal of Biological Chemistry 2005, 280:11247-11258.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 11247-11258
    • Feraudet, C.1
  • 24
    • 67651047286 scopus 로고    scopus 로고
    • In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms
    • Fernandez-Funez P., et al. In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms. PLoS Genetics 2009, 5:e1000507.
    • (2009) PLoS Genetics , vol.5
    • Fernandez-Funez, P.1
  • 25
    • 78449260181 scopus 로고    scopus 로고
    • Sequence-dependent prion protein misfolding and neurotoxicity
    • Fernandez-Funez P., et al. Sequence-dependent prion protein misfolding and neurotoxicity. The Journal of Biological Chemistry 2010, 285:36897-36908.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 36897-36908
    • Fernandez-Funez, P.1
  • 26
    • 35549006674 scopus 로고    scopus 로고
    • The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections
    • Ferrandon D., et al. The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections. Nature Reviews Immunology 2007, 7:862-874.
    • (2007) Nature Reviews Immunology , vol.7 , pp. 862-874
    • Ferrandon, D.1
  • 27
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost B., Diamond M.I. Prion-like mechanisms in neurodegenerative diseases. Nature Reviews Neuroscience 2010, 11:155-159.
    • (2010) Nature Reviews Neuroscience , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 28
    • 33845234260 scopus 로고    scopus 로고
    • Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Straussler-Scheinker syndrome
    • Gavin B.A., et al. Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Straussler-Scheinker syndrome. The Journal of Neuroscience 2006, 26:12408-12414.
    • (2006) The Journal of Neuroscience , vol.26 , pp. 12408-12414
    • Gavin, B.A.1
  • 29
    • 0034116880 scopus 로고    scopus 로고
    • Peripheral pathogenesis of prion diseases
    • Glatzel M., Aguzzi A. Peripheral pathogenesis of prion diseases. Microbes and Infection 2000, 2:613-619.
    • (2000) Microbes and Infection , vol.2 , pp. 613-619
    • Glatzel, M.1    Aguzzi, A.2
  • 30
    • 0033763178 scopus 로고    scopus 로고
    • PrP(C) expression in the peripheral nervous system is a determinant of prion neuroinvasion
    • Glatzel M., Aguzzi A. PrP(C) expression in the peripheral nervous system is a determinant of prion neuroinvasion. The Journal of General Virology 2000, 81:2813-2821.
    • (2000) The Journal of General Virology , vol.81 , pp. 2813-2821
    • Glatzel, M.1    Aguzzi, A.2
  • 31
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert M., et al. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends in Neurosciences 2010, 33:317-325.
    • (2010) Trends in Neurosciences , vol.33 , pp. 317-325
    • Goedert, M.1
  • 32
    • 0028349264 scopus 로고
    • PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie
    • Goldmann W., et al. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. The Journal of General Virology 1994, 75(Pt 5):989-995.
    • (1994) The Journal of General Virology , vol.75 , Issue.PART 5 , pp. 989-995
    • Goldmann, W.1
  • 35
    • 0033179767 scopus 로고    scopus 로고
    • Conserved genetic programs in insect and mammalian brain development
    • Hirth F., Reichert H. Conserved genetic programs in insect and mammalian brain development. Bioessays 1999, 21:677-684.
    • (1999) Bioessays , vol.21 , pp. 677-684
    • Hirth, F.1    Reichert, H.2
  • 36
    • 0030856447 scopus 로고    scopus 로고
    • PrP genetics in sheep and the applications for scrapie and BSE
    • Hunter N. PrP genetics in sheep and the applications for scrapie and BSE. Trends in Microbiology 1997, 5:331-334.
    • (1997) Trends in Microbiology , vol.5 , pp. 331-334
    • Hunter, N.1
  • 37
    • 34447132913 scopus 로고    scopus 로고
    • Classical sheep transmissible spongiform encephalopathies: pathogenesis, pathological phenotypes and clinical disease
    • Jeffrey M., Gonzalez L. Classical sheep transmissible spongiform encephalopathies: pathogenesis, pathological phenotypes and clinical disease. Neuropathology and Applied Neurobiology 2007, 33:373-394.
    • (2007) Neuropathology and Applied Neurobiology , vol.33 , pp. 373-394
    • Jeffrey, M.1    Gonzalez, L.2
  • 38
    • 0035659971 scopus 로고    scopus 로고
    • Differential diagnosis of infections with the bovine spongiform encephalopathy (BSE) and scrapie agents in sheep
    • Jeffrey M., et al. Differential diagnosis of infections with the bovine spongiform encephalopathy (BSE) and scrapie agents in sheep. Journal of Comparative Pathology 2001, 125:271-284.
    • (2001) Journal of Comparative Pathology , vol.125 , pp. 271-284
    • Jeffrey, M.1
  • 39
    • 3442889359 scopus 로고    scopus 로고
    • Synthetic mammalian prions
    • Legname G., et al. Synthetic mammalian prions. Science 2004, 305:673-676.
    • (2004) Science , vol.305 , pp. 673-676
    • Legname, G.1
  • 42
    • 66149135641 scopus 로고    scopus 로고
    • Drosophila models of neurodegenerative diseases
    • Lu B., Vogel H. Drosophila models of neurodegenerative diseases. Annual Review of Pathology 2009, 4:315-342.
    • (2009) Annual Review of Pathology , vol.4 , pp. 315-342
    • Lu, B.1    Vogel, H.2
  • 43
    • 0028703452 scopus 로고
    • PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology
    • Manson J.C., et al. PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 1994, 3:331-340.
    • (1994) Neurodegeneration , vol.3 , pp. 331-340
    • Manson, J.C.1
  • 44
    • 77951016608 scopus 로고    scopus 로고
    • Alzheimer's disease: insights from Drosophila melanogaster models
    • Moloney A., et al. Alzheimer's disease: insights from Drosophila melanogaster models. Trends in Biochemical Sciences 2010, 35:228-235.
    • (2010) Trends in Biochemical Sciences , vol.35 , pp. 228-235
    • Moloney, A.1
  • 45
    • 0034686002 scopus 로고    scopus 로고
    • Impaired prion replication in spleens of mice lacking functional follicular dendritic cells
    • Montrasio F., et al. Impaired prion replication in spleens of mice lacking functional follicular dendritic cells. Science 2000, 288:1257-1259.
    • (2000) Science , vol.288 , pp. 1257-1259
    • Montrasio, F.1
  • 46
    • 11444271002 scopus 로고    scopus 로고
    • Polymorphisms at codons 141 and 154 in the ovine prion protein gene are associated with scrapie Nor98 cases
    • Moum T., et al. Polymorphisms at codons 141 and 154 in the ovine prion protein gene are associated with scrapie Nor98 cases. The Journal of General Virology 2005, 86:231-235.
    • (2005) The Journal of General Virology , vol.86 , pp. 231-235
    • Moum, T.1
  • 47
    • 68649118065 scopus 로고    scopus 로고
    • Cells and prions: a license to replicate
    • Nuvolone M., et al. Cells and prions: a license to replicate. FEBS Letters 2009, 583:2674-2684.
    • (2009) FEBS Letters , vol.583 , pp. 2674-2684
    • Nuvolone, M.1
  • 48
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 50
    • 0029016205 scopus 로고
    • Expression and targeting of Syrian hamster prion protein induced by heat shock in transgenic Drosophila melanogaster
    • Raeber A.J., et al. Expression and targeting of Syrian hamster prion protein induced by heat shock in transgenic Drosophila melanogaster. Mechanisms of Development 1995, 51:317-327.
    • (1995) Mechanisms of Development , vol.51 , pp. 317-327
    • Raeber, A.J.1
  • 51
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • Saa P., et al. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. The Journal of Biological Chemistry 2006, 281:35245-35252.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 35245-35252
    • Saa, P.1
  • 52
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg M.K., et al. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011, 470:540-542.
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1
  • 53
    • 0037442530 scopus 로고    scopus 로고
    • Detection of bovine spongiform encephalopathy, ovine scrapie prion-related protein (PrPSc) and normal PrPc by monoclonal antibodies raised to copper-refolded prion protein
    • Thackray A.M., et al. Detection of bovine spongiform encephalopathy, ovine scrapie prion-related protein (PrPSc) and normal PrPc by monoclonal antibodies raised to copper-refolded prion protein. The Biochemical Journal 2003, 370:81-90.
    • (2003) The Biochemical Journal , vol.370 , pp. 81-90
    • Thackray, A.M.1
  • 54
    • 25144467420 scopus 로고    scopus 로고
    • Modification of blood cell PrP epitope exposure during prion disease
    • Thackray A.M., et al. Modification of blood cell PrP epitope exposure during prion disease. The Biochemical Journal 2005, 390:563-571.
    • (2005) The Biochemical Journal , vol.390 , pp. 563-571
    • Thackray, A.M.1
  • 55
    • 33845208359 scopus 로고    scopus 로고
    • Ovine plasma prion protein levels show genotypic variation detected by C-terminal epitopes not exposed in cell-surface PrPC
    • Thackray A.M., et al. Ovine plasma prion protein levels show genotypic variation detected by C-terminal epitopes not exposed in cell-surface PrPC. The Biochemical Journal 2006, 400:349-358.
    • (2006) The Biochemical Journal , vol.400 , pp. 349-358
    • Thackray, A.M.1
  • 56
    • 33846490771 scopus 로고    scopus 로고
    • Proteinase K-sensitive disease-associated ovine prion protein revealed by conformation-dependent immunoassay
    • Thackray A.M., et al. Proteinase K-sensitive disease-associated ovine prion protein revealed by conformation-dependent immunoassay. The Biochemical Journal 2007, 401:475-483.
    • (2007) The Biochemical Journal , vol.401 , pp. 475-483
    • Thackray, A.M.1
  • 57
    • 55549130472 scopus 로고    scopus 로고
    • Molecular and transmission characteristics of primary-passaged ovine scrapie isolates in conventional and ovine PrP transgenic mice
    • Thackray A.M., et al. Molecular and transmission characteristics of primary-passaged ovine scrapie isolates in conventional and ovine PrP transgenic mice. Journal of Virology 2008, 82:11197-11207.
    • (2008) Journal of Virology , vol.82 , pp. 11197-11207
    • Thackray, A.M.1
  • 58
    • 79956332419 scopus 로고    scopus 로고
    • Emergence of multiple prion strains from single isolates of ovine scrapie
    • Thackray A.M., et al. Emergence of multiple prion strains from single isolates of ovine scrapie. The Journal of General Virology 2011, 92:1482-1491.
    • (2011) The Journal of General Virology , vol.92 , pp. 1482-1491
    • Thackray, A.M.1
  • 59
    • 84862811107 scopus 로고    scopus 로고
    • Ovine PrP transgenic Drosophila show reduced locomotor activity and decreased survival
    • Submitted for publication.
    • Thackray, A. M., et al., 2011b. Ovine PrP transgenic Drosophila show reduced locomotor activity and decreased survival. Submitted for publication.
    • (2011)
    • Thackray, A.M.1
  • 60
    • 0034973230 scopus 로고    scopus 로고
    • Markedly increased susceptibility to natural sheep scrapie of transgenic mice expressing ovine prp
    • Vilotte J.L., et al. Markedly increased susceptibility to natural sheep scrapie of transgenic mice expressing ovine prp. Journal of Virology 2001, 75:5977-5984.
    • (2001) Journal of Virology , vol.75 , pp. 5977-5984
    • Vilotte, J.L.1
  • 61
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002, 416:535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 62
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F., et al. Generating a prion with bacterially expressed recombinant prion protein. Science 2010, 327:1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1
  • 63
    • 34547096014 scopus 로고    scopus 로고
    • Generation of genuine prion infectivity by serial PMCA
    • Weber P., et al. Generation of genuine prion infectivity by serial PMCA. Veterinary Microbiology 2007, 123:346-357.
    • (2007) Veterinary Microbiology , vol.123 , pp. 346-357
    • Weber, P.1
  • 64
    • 84891730000 scopus 로고    scopus 로고
    • The dopaminergic system in the aging brain of Drosophila
    • White K.E., et al. The dopaminergic system in the aging brain of Drosophila. Frontiers in Neuroscience 2010, 4:205.
    • (2010) Frontiers in Neuroscience , vol.4 , pp. 205
    • White, K.E.1
  • 65
    • 34247103287 scopus 로고    scopus 로고
    • Drosophila hemopoiesis and cellular immunity
    • Williams M.J. Drosophila hemopoiesis and cellular immunity. Journal of Immunology 2007, 178:4711-4716.
    • (2007) Journal of Immunology , vol.178 , pp. 4711-4716
    • Williams, M.J.1


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