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Volumn 81, Issue 6, 2007, Pages 2831-2837

Cytosolic prion protein toxicity is independent of cellular prion protein expression and prion propagation

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; SIALOGLYCOPROTEIN;

EID: 33947407685     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02157-06     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D. R., A. Taraboulos, and S. B. Prusiner. 1992. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267:16188-16199.
    • (1992) J. Biol. Chem , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 2
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown, D. R., J. Herms, and H. A. Kretzschmar. 1994. Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. Neuroreport 5:2057-2060.
    • (1994) Neuroreport , vol.5 , pp. 2057-2060
    • Brown, D.R.1    Herms, J.2    Kretzschmar, H.A.3
  • 3
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown, D. R., W. J. Schulz-Schaeffer, B. Schmidt, and H. A. Kretzschmar. 1997. Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146:104-112.
    • (1997) Exp. Neurol , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 4
    • 0032570091 scopus 로고    scopus 로고
    • 1755 and all that: A historical primer of transmissible spongiform encephalopathy
    • Brown, P., and R. Bradley. 1998. 1755 and all that: a historical primer of transmissible spongiform encephalopathy. BMJ 317:1688-1692.
    • (1998) BMJ , vol.317 , pp. 1688-1692
    • Brown, P.1    Bradley, R.2
  • 6
    • 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., A. Raeber, A. Sailer, M. Fischer, A. Aguzzi, and C. Weissmann. 1994. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol. Med. 1:19-30.
    • (1994) Mol. Med , vol.1 , pp. 19-30
    • Bueler, H.1    Raeber, A.2    Sailer, A.3    Fischer, M.4    Aguzzi, A.5    Weissmann, C.6
  • 7
    • 13244295520 scopus 로고    scopus 로고
    • The highways and byways of prion protein trafficking
    • Campana, V., D. Sarnataro, and C. Zurzolo. 2005. The highways and byways of prion protein trafficking. Trends Cell Biol. 15:102-111.
    • (2005) Trends Cell Biol , vol.15 , pp. 102-111
    • Campana, V.1    Sarnataro, D.2    Zurzolo, C.3
  • 8
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla, J., P. Saa, C. Hetz, and C. Soto. 2005. In vitro generation of infectious scrapie prions. Cell 121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 9
    • 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., and G. J. Raymond. 1991. 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) J. Biol. Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 11
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman, S. K., G. J. Raymond, B. Caughey, and S. Lindquist. 1997. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. USA 94:13938-13943.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13938-13943
    • DebBurman, S.K.1    Raymond, G.J.2    Caughey, B.3    Lindquist, S.4
  • 12
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault, N. R., R. W. Lucassen, and S. Supattapone. 2003. RNA molecules stimulate prion protein conversion. Nature 425:717-720.
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 13
    • 15744395826 scopus 로고    scopus 로고
    • Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations
    • Fioriti, L., S. Dossena, L. R. Stewart, R. S. Stewart, D. A. Harris, G. Forloni, and R. Chiesa. 2005. Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations. J. Biol. Chem. 280:11320-11328.
    • (2005) J. Biol. Chem , vol.280 , pp. 11320-11328
    • Fioriti, L.1    Dossena, S.2    Stewart, L.R.3    Stewart, R.S.4    Harris, D.A.5    Forloni, G.6    Chiesa, R.7
  • 14
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer, M., T. Rulicke, A. Raeber, A. Sailer, M. Moser, B. Oesch, S. Brandner, A. Aguzzi, and C. Weissmann. 1996. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15:1255-1264.
    • (1996) EMBO J , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5    Oesch, B.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 16
    • 0141849465 scopus 로고    scopus 로고
    • Subclinical prion infection in humans and animals
    • Hill, A. F., and J. Collinge. 2003. Subclinical prion infection in humans and animals. Br. Med. Bull. 66:161-170.
    • (2003) Br. Med. Bull , vol.66 , pp. 161-170
    • Hill, A.F.1    Collinge, J.2
  • 20
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • Ma, J., and S. Lindquist. 2002. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298:1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 21
    • 0033203242 scopus 로고    scopus 로고
    • De novo generation of a PrPSc-like conformation in living cells
    • Ma, J., and S. Lindquist. 1999. De novo generation of a PrPSc-like conformation in living cells. Nat. Cell Biol. 1:358-361.
    • (1999) Nat. Cell Biol , vol.1 , pp. 358-361
    • Ma, J.1    Lindquist, S.2
  • 22
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma, J., and S. Lindquist. 2001. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. USA 98:14955-14960.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 23
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J., R. Wollmann, and S. Lindquist. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 27
    • 22844451837 scopus 로고    scopus 로고
    • The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation
    • Norstrom, E. M., and J. A. Mastrianni. 2005. The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation. J. Biol. Chem. 280:27236-27243.
    • (2005) J. Biol. Chem , vol.280 , pp. 27236-27243
    • Norstrom, E.M.1    Mastrianni, J.A.2
  • 28
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P. C., and D. A. Harris. 1998. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273:33107-33110.
    • (1998) J. Biol. Chem , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 31
    • 0142135128 scopus 로고    scopus 로고
    • Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons
    • Roucou, X., Q. Guo, Y. Zhang, C. G. Goodyer, and A. C. LeBlanc. 2003. Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons. J. Biol. Chem. 278:40877-40881.
    • (2003) J. Biol. Chem , vol.278 , pp. 40877-40881
    • Roucou, X.1    Guo, Q.2    Zhang, Y.3    Goodyer, C.G.4    LeBlanc, A.C.5
  • 32
    • 0345687168 scopus 로고    scopus 로고
    • NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells
    • Schneider, B., V. Mutel, M. Pietri, M. Ermonval, S. Mouillet-Richard, and O. Kellermann. 2003. NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA 100:13326-13331.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13326-13331
    • Schneider, B.1    Mutel, V.2    Pietri, M.3    Ermonval, M.4    Mouillet-Richard, S.5    Kellermann, O.6
  • 33
    • 0025373111 scopus 로고
    • Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells
    • Taraboulos, A., D. Serban, and S. B. Prusiner. 1990. Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J. Cell Biol. 110:2117-2132.
    • (1990) J. Cell Biol , vol.110 , pp. 2117-2132
    • Taraboulos, A.1    Serban, D.2    Prusiner, S.B.3
  • 34
    • 12844249401 scopus 로고    scopus 로고
    • Calpain and other cytosolic proteases can contribute to the degradation of retro-translocated prion protein in the cytosol
    • Wang, X., F. Wang, M. S. Sy, and J. Ma. 2005. Calpain and other cytosolic proteases can contribute to the degradation of retro-translocated prion protein in the cytosol. J. Biol. Chem. 280:317-325.
    • (2005) J. Biol. Chem , vol.280 , pp. 317-325
    • Wang, X.1    Wang, F.2    Sy, M.S.3    Ma, J.4
  • 35
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia, Y., L. Horonchik, S. Tzaban, A. Yanai, and A. Taraboulos. 2001. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20:5383-5391.
    • (2001) EMBO J , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.