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Volumn 2, Issue 1, 2011, Pages

Rapid cell-surface prion protein conversion revealed using a novel cell system

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; MEMBRANE PROTEIN;

EID: 79955050582     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1282     Document Type: Article
Times cited : (117)

References (53)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144 (1982). (Pubitemid 12089840)
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 2
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • DOI 10.1146/annurev.neuro.24.1.519
    • Collinge, J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519-550 (2001). (Pubitemid 32695238)
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 519-550
    • Collinge, J.1
  • 3
    • 48249108696 scopus 로고    scopus 로고
    • Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease
    • White, M. D. et al. Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease. Proc. Natl Acad. Sci. USA 105, 10238-10243 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 10238-10243
    • White, M.D.1
  • 4
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert, M., Clavaguera, F. & Tolnay, M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 33, 317-325 (2010).
    • (2010) Trends Neurosci. , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 5
    • 53349177064 scopus 로고    scopus 로고
    • Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles
    • Alais, S. et al. Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles. Biol. Cell 100, 603-615 (2008).
    • (2008) Biol. Cell , vol.100 , pp. 603-615
    • Alais, S.1
  • 6
    • 61849178720 scopus 로고    scopus 로고
    • Prions hijack tunnelling nanotubes for intercellular spread
    • Gousset, K. et al. Prions hijack tunnelling nanotubes for intercellular spread. Nat. Cell Biol. 11, 328-336 (2009).
    • (2009) Nat. Cell Biol. , vol.11 , pp. 328-336
    • Gousset, K.1
  • 7
    • 67249099366 scopus 로고    scopus 로고
    • Identification of an intracellular site of prion conversion
    • Marijanovic, Z., Caputo, A., Campana, V. & Zurzolo, C. Identification of an intracellular site of prion conversion. PLoS Pathog. 5, e1000426 (2009).
    • (2009) PLoS Pathog. , vol.5
    • Marijanovic, Z.1    Caputo, A.2    Campana, V.3    Zurzolo, C.4
  • 8
    • 33644850940 scopus 로고    scopus 로고
    • Prion infection of mouse neurospheres
    • Giri, R. K. et al. Prion infection of mouse neurospheres. Proc. Natl Acad. Sci. USA 103, 3875-3880 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 3875-3880
    • Giri, R.K.1
  • 10
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cell sublines highly susceptible to prion infection
    • DOI 10.1128/JVI.74.9.4377-4386.2000
    • Bosque, P. J. & Prusiner, S. B. Cultured cell sublines highly susceptible to prion infection. J. Virol. 74, 4377-4386 (2000). (Pubitemid 30214445)
    • (2000) Journal of Virology , vol.74 , Issue.9 , pp. 4377-4386
    • Bosque, P.J.1    Prusiner, S.B.2
  • 12
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • DOI 10.1016/S0968-0004(01)01792-3, PII S0968000401017923
    • Caughey, B. Interactions between prion protein isoforms: the kiss of death? Trends Biochem. Sci. 26, 235-242 (2001). (Pubitemid 32289242)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.4 , pp. 235-242
    • Caughey, B.1
  • 13
    • 0028364192 scopus 로고
    • Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells
    • Priola, S. A., Caughey, B., Race, R. E. & Chesebro, B. Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells. J. Virol. 68, 4873-4878 (1994).
    • (1994) J. Virol. , vol.68 , pp. 4873-4878
    • Priola, S.A.1    Caughey, B.2    Race, R.E.3    Chesebro, B.4
  • 14
    • 20544459159 scopus 로고    scopus 로고
    • Visualization of prion infection in transgenic mice expressing green fluorescent protein-tagged prion protein
    • DOI 10.1523/JNEUROSCI.1192-05.2005
    • Barmada, S. J. & Harris, D. A. Visualization of prion infection in transgenic mice expressing green fluorescent protein-tagged prion protein. J. Neurosci. 25, 5824-5832 (2005). (Pubitemid 40847895)
    • (2005) Journal of Neuroscience , vol.25 , Issue.24 , pp. 5824-5832
    • Barmada, S.J.1    Harris, D.A.2
  • 15
    • 84887212358 scopus 로고    scopus 로고
    • The comprehensive native interactome of a fully functional tagged prion protein
    • Rutishauser, D. et al. The comprehensive native interactome of a fully functional tagged prion protein. PLoS One 4, e4446 (2009).
    • (2009) PLoS One , vol.4
    • Rutishauser, D.1
  • 18
    • 0023928927 scopus 로고
    • Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins
    • Butler, D. A. et al. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J. Virol. 62, 1558-1564 (1988).
    • (1988) J. Virol. , vol.62 , pp. 1558-1564
    • Butler, D.A.1
  • 21
    • 57249089081 scopus 로고    scopus 로고
    • Immunolocalisation of PrP(Sc) in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy
    • Veith, N. M., Plattner, H., Stuermer, C. A., Schulz-Schaeffer, W. J. & Burkle, A. Immunolocalisation of PrP(Sc) in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy. Eur. J. Cell Biol. 88, 45-63 (2008).
    • (2008) Eur. J. Cell Biol. , vol.88 , pp. 45-63
    • Veith, N.M.1    Plattner, H.2    Stuermer, C.A.3    Schulz-Schaeffer, W.J.4    Burkle, A.5
  • 22
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey, B. & Raymond, G. J. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-and phospholipase-sensitive. J. Biol. Chem. 266, 18217-18223 (1991). (Pubitemid 21908068)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.27 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 23
    • 0029346911 scopus 로고
    • The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain
    • Arnold, J. E. et al. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 176, 403-411 (1995).
    • (1995) J. Pathol. , vol.176 , pp. 403-411
    • Arnold, J.E.1
  • 24
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • DOI 10.1038/nature05294, PII NATURE05294
    • Caughey, B. & Baron, G. S. Prions and their partners in crime. Nature 443, 803-810 (2006). (Pubitemid 44622685)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 25
    • 0028085865 scopus 로고
    • Quantification of low density lipoprotein and transferrin endocytic sorting in HEp2 cells using confocal microscopy
    • Ghosh, R. N., Gelman, D. L. & Maxfield, F. R. Quantification of low density lipoprotein and transferrin endocytic sorting HEp2 cells using confocal microscopy. J. Cell Sci. 107 (Pt 8), 2177-2189 (1994). (Pubitemid 24273484)
    • (1994) Journal of Cell Science , vol.107 , Issue.8 , pp. 2177-2189
    • Ghosh, R.N.1    Gelman, D.L.2    Maxfield, F.R.3
  • 26
    • 0021451232 scopus 로고
    • Initial steps in receptor-mediated endocytosis. The influence of temperature on the shape and distribution of plasma membrane clathrin-coated pits in cultured mammalian cells
    • Goldenthal, K. L., Pastan, I. & Willingham, M. C. Initial steps in receptor-mediated endocytosis. The influence of temperature on the shape and distribution of plasma membrane clathrin-coated pits in cultured mammalian cells. Exp. Cell Res. 152, 558-564 (1984).
    • (1984) Exp. Cell Res. , vol.152 , pp. 558-564
    • Goldenthal, K.L.1    Pastan, I.2    Willingham, M.C.3
  • 27
    • 33646892646 scopus 로고    scopus 로고
    • Dynasore, a cell-permeable inhibitor of dynamin
    • Macia, E. et al. Dynasore, a cell-permeable inhibitor of dynamin. Dev. Cell 10, 839-850 (2006).
    • (2006) Dev. Cell , vol.10 , pp. 839-850
    • MacIa, E.1
  • 30
    • 73549083896 scopus 로고    scopus 로고
    • Glypican-1 mediates both prion protein lipid raft association and disease isoform formation
    • Taylor, D. R., Whitehouse, I. J. & Hooper, N. M. Glypican-1 mediates both prion protein lipid raft association and disease isoform formation. PLoS Pathog. 5, e1000666 (2009).
    • (2009) PLoS Pathog. , vol.5
    • Taylor, D.R.1    Whitehouse, I.J.2    Hooper, N.M.3
  • 31
    • 77952956256 scopus 로고    scopus 로고
    • Cellular factors implicated in prion replication
    • Abid, K., Morales, R. & Soto, C. Cellular factors implicated in prion replication. FEBS Lett. 584, 2409-2414 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 2409-2414
    • Abid, K.1    Morales, R.2    Soto, C.3
  • 32
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor, D. R. & Hooper, N. M. The prion protein and lipid rafts. Mol. Membr. Biol. 23, 89-99 (2006).
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 33
    • 0026559095 scopus 로고
    • Caveolin, a protein component of caveolae membrane coats
    • Rothberg, K. G. et al. Caveolin, a protein component of caveolae membrane coats. Cell 68, 673-682 (1992).
    • (1992) Cell , vol.68 , pp. 673-682
    • Rothberg, K.G.1
  • 34
    • 67349166918 scopus 로고    scopus 로고
    • Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes
    • Cenedella, R. J. Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes. Lipids 44, 477-487 (2009).
    • (2009) Lipids , vol.44 , pp. 477-487
    • Cenedella, R.J.1
  • 35
    • 73849129337 scopus 로고    scopus 로고
    • Neuronal low-density lipoprotein receptor-related protein 1 binds and endocytoses prion fibrils via receptor cluster 4
    • Jen, A. et al. Neuronal low-density lipoprotein receptor-related protein 1 binds and endocytoses prion fibrils via receptor cluster 4. J. Cell Sci. 123, 246-255 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 246-255
    • Jen, A.1
  • 36
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang, F., Wang, X., Yuan, C. G. & Ma, J. Generating a prion with bacterially expressed recombinant prion protein. Science 327, 1132-1135 (2010).
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 38
    • 0033947543 scopus 로고    scopus 로고
    • Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy
    • DOI 10.1002/1096-9896(200007)191:3<323::AID-PATH629>3.0.CO;2-Z
    • Jeffrey, M., McGovern, G., Goodsir, C. M., Brown, K. L. & Bruce, M. E. Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy. J. Pathol. 191, 323-332 (2000). (Pubitemid 30441258)
    • (2000) Journal of Pathology , vol.191 , Issue.3 , pp. 323-332
    • Jeffrey, M.1    McGovern, G.2    Goodsir, C.M.3    Brown, K.L.4    Bruce, M.E.5
  • 40
    • 66149125943 scopus 로고    scopus 로고
    • Cells expressing anchorless prion protein are resistant to scrapie infection
    • McNally, K. L., Ward, A. E. & Priola, S. A. Cells expressing anchorless prion protein are resistant to scrapie infection. J. Virol. 83, 4469-4475 (2009).
    • (2009) J. Virol. , vol.83 , pp. 4469-4475
    • McNally, K.L.1    Ward, A.E.2    Priola, S.A.3
  • 41
    • 53749088102 scopus 로고    scopus 로고
    • Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis
    • Wadia, J. S., Schaller, M., Williamson, R. A. & Dowdy, S. F. Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis. PLoS One 3, e3314 (2008).
    • (2008) PLoS One , vol.3
    • Wadia, J.S.1    Schaller, M.2    Williamson, R.A.3    Dowdy, S.F.4
  • 42
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore, N. et al. Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J. 18, 6917-6926 (1999). (Pubitemid 30000445)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6917-6926
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 44
    • 0037067743 scopus 로고    scopus 로고
    • Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release
    • DOI 10.1074/jbc.M203248200
    • Marella, M., Lehmann, S., Grassi, J. & Chabry, J. Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release. J. Biol. Chem. 277, 25457-25464 (2002). (Pubitemid 34951859)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25457-25464
    • Marella, M.1    Lehmann, S.2    Grassi, J.3    Chabry, J.4
  • 45
    • 32244434927 scopus 로고    scopus 로고
    • The prion protein requires cholesterol for cell surface localization
    • DOI 10.1016/j.mcn.2005.10.008, PII S1044743105002502
    • Gilch, S., Kehler, C. & Schatzl, H. M. The prion protein requires cholesterol for cell surface localization. Mol. Cell Neurosci. 31, 346-353 (2006). (Pubitemid 43214544)
    • (2006) Molecular and Cellular Neuroscience , vol.31 , Issue.2 , pp. 346-353
    • Gilch, S.1    Kehler, C.2    Schatzl, H.M.3
  • 46
    • 0037195617 scopus 로고    scopus 로고
    • Sc-like conformation in the cytosol
    • DOI 10.1126/science.1073619
    • Ma, J. & Lindquist, S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298, 1785-1788 (2002). (Pubitemid 35404121)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 47
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D. R., Taraboulos, A. & Prusiner, S. B. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267, 16188-16199 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 48
    • 0037064026 scopus 로고    scopus 로고
    • Sc in prion-infected cells
    • DOI 10.1074/jbc.M205110200
    • Beranger, F., Mange, A., Goud, B. & Lehmann, S. Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J. Biol. Chem. 277, 38972-38977 (2002). (Pubitemid 35154763)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38972-38977
    • Beranger, F.1    Mange, A.2    Goud, B.3    Lehmann, S.4
  • 50
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., Krummel, B. & Saiki, R. K. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16, 7351-7367 (1988).
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 51
    • 0034613188 scopus 로고    scopus 로고
    • Involvement of p38 mitogen-activated protein kinase signaling pathway in osteoclastogenesis mediated by receptor activator of NF-kappa B ligand (RANKL)
    • Matsumoto, M., Sudo, T., Saito, T., Osada, H. & Tsujimoto, M. Involvement of p38 mitogen-activated protein kinase signaling pathway in osteoclastogenesis mediated by receptor activator of NF-kappa B ligand (RANKL). J. Biol. Chem. 275, 31155-31161 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 31155-31161
    • Matsumoto, M.1    Sudo, T.2    Saito, T.3    Osada, H.4    Tsujimoto, M.5
  • 52
    • 77956276348 scopus 로고    scopus 로고
    • Spontaneous generation of mammalian prions
    • Edgeworth, J. A. et al. Spontaneous generation of mammalian prions. Proc. Natl Acad. Sci. USA 107, 14402-14406 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 14402-14406
    • Edgeworth, J.A.1
  • 53
    • 58149280203 scopus 로고    scopus 로고
    • Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin
    • Cronier, S. et al. Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin. Biochem J. 416, 297-305 (2008).
    • (2008) Biochem J. , vol.416 , pp. 297-305
    • Cronier, S.1


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