메뉴 건너뛰기




Volumn 23, Issue 18, 2003, Pages 7183-7193

Cytosolic prion protein in neurons

Author keywords

Cytosolic; Hippocampus; Immunogold; Localization; Membrane; Prion protein

Indexed keywords

PRION PROTEIN;

EID: 0042855745     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.23-18-07183.2003     Document Type: Article
Times cited : (191)

References (69)
  • 1
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution
    • Amit AG, Mariuzza RA, Phillips SE, Poljak RJ (1986) Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233:747-753.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.3    Poljak, R.J.4
  • 2
    • 0029346911 scopus 로고
    • The abnormal isoform of the prion protein accumulates in late-endosomelike organelles in scrapie-infected mouse brain
    • Arnold JE, Tipler C, Laszlo L, Hope J, Landon M, Mayer RJ (1995) The abnormal isoform of the prion protein accumulates in late-endosomelike organelles in scrapie-infected mouse brain. J Pathol 176:403-411.
    • (1995) J Pathol , vol.176 , pp. 403-411
    • Arnold, J.E.1    Tipler, C.2    Laszlo, L.3    Hope, J.4    Landon, M.5    Mayer, R.J.6
  • 3
    • 0032885694 scopus 로고    scopus 로고
    • Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease
    • Belichenko PV, Miklossy J, Belser B, Budka H, Celio MR (1999) Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease. Neurobiol Dis 6:269-279.
    • (1999) Neurobiol Dis , vol.6 , pp. 269-279
    • Belichenko, P.V.1    Miklossy, J.2    Belser, B.3    Budka, H.4    Celio, M.R.5
  • 4
    • 0030064680 scopus 로고    scopus 로고
    • A two-step recognition of signal sequences determines the translocation efficiency of proteins
    • Belin D, Bost S, Vassalli JD, Strub K (1996) A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J 15:468-478.
    • (1996) EMBO J , vol.15 , pp. 468-478
    • Belin, D.1    Bost, S.2    Vassalli, J.D.3    Strub, K.4
  • 6
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt DR, Taraboulos A, Prusiner SB (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
  • 7
    • 0034714012 scopus 로고    scopus 로고
    • Selective neuronal vulnerability during experimental scrapie infection: Insights from an ultrastructural investigation
    • Bouzamondo E, DeArmond SJ, Ralston HJ, Prusiner SB, Milroy AM (2000) Selective neuronal vulnerability during experimental scrapie infection: insights from an ultrastructural investigation. Brain Res 874:210-215.
    • (2000) Brain Res , vol.874 , pp. 210-215
    • Bouzamondo, E.1    DeArmond, S.J.2    Ralston, H.J.3    Prusiner, S.B.4    Milroy, A.M.5
  • 8
    • 0035158321 scopus 로고    scopus 로고
    • Antioxidant activity related to copper binding of native prion protein
    • Brown DR, Clive C, Haswell SJ (2001) Antioxidant activity related to copper binding of native prion protein. J Neurochem 76:69-76.
    • (2001) J Neurochem , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.J.3
  • 11
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B, Raymond GJ, Ernst D, Race RE (1991) N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 65:6597-6603.
    • (1991) J Virol , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 12
    • 0035794533 scopus 로고    scopus 로고
    • GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment
    • Chatterjee S, Smith ER, Hanada K, Stevens VL, Mayor S (2001) GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment. EMBO J 20:1583-1592.
    • (2001) EMBO J , vol.20 , pp. 1583-1592
    • Chatterjee, S.1    Smith, E.R.2    Hanada, K.3    Stevens, V.L.4    Mayor, S.5
  • 17
    • 0034235594 scopus 로고    scopus 로고
    • Ultrastructural localization of prion proteins: Physiological and pathological implications
    • Fournier JG, Escaig-Haye F, Grigoriev V (2000) Ultrastructural localization of prion proteins: physiological and pathological implications. Microsc Res Tech 50:76-88.
    • (2000) Microsc Res Tech , vol.50 , pp. 76-88
    • Fournier, J.G.1    Escaig-Haye, F.2    Grigoriev, V.3
  • 20
    • 0032919804 scopus 로고    scopus 로고
    • Assessing apoptosis: A critical survey
    • Hall PA (1999) Assessing apoptosis: a critical survey. Endocr Relat Cancer 6:3-8.
    • (1999) Endocr Relat Cancer , vol.6 , pp. 3-8
    • Hall, P.A.1
  • 21
    • 0032904215 scopus 로고    scopus 로고
    • Regulation of protein biogenesis at the endoplasmic reticulum membrane
    • Hegde RS, Lingappa VR (1999) Regulation of protein biogenesis at the endoplasmic reticulum membrane. Trends Cell Biol 9:132-137.
    • (1999) Trends Cell Biol , vol.9 , pp. 132-137
    • Hegde, R.S.1    Lingappa, V.R.2
  • 24
    • 0035918202 scopus 로고    scopus 로고
    • Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus
    • Holscher C, Bach UC, Dobberstein B (2001) Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus. J Biol Chem 276:13388-13394.
    • (2001) J Biol Chem , vol.276 , pp. 13388-13394
    • Holscher, C.1    Bach, U.C.2    Dobberstein, B.3
  • 25
    • 0035854696 scopus 로고    scopus 로고
    • Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain
    • Kim SJ, Rahbar R, Hegde RS (2001) Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain. J Biol Chem 276:26132-26140.
    • (2001) J Biol Chem , vol.276 , pp. 26132-26140
    • Kim, S.J.1    Rahbar, R.2    Hegde, R.S.3
  • 26
    • 0036759121 scopus 로고    scopus 로고
    • Unhampered prion neuroinvasion despite impaired fast axonal transport in transgenic mice overexpressing four-repeat tau
    • Kunzi V, Glatzel M, Nakano MY, Greber UF, Van Leuven F, Aguzzi A (2002) Unhampered prion neuroinvasion despite impaired fast axonal transport in transgenic mice overexpressing four-repeat tau. J Neurosci 22:7471-7477.
    • (2002) J Neurosci , vol.22 , pp. 7471-7477
    • Kunzi, V.1    Glatzel, M.2    Nakano, M.Y.3    Greber, U.F.4    Van Leuven, F.5    Aguzzi, A.6
  • 28
    • 0034899833 scopus 로고    scopus 로고
    • Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum
    • Laine J, Marc ME, Sy MS, Axelrad H (2001) Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum. Eur J Neurosci 14:47-56.
    • (2001) Eur J Neurosci , vol.14 , pp. 47-56
    • Laine, J.1    Marc, M.E.2    Sy, M.S.3    Axelrad, H.4
  • 29
    • 0035794531 scopus 로고    scopus 로고
    • Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form
    • Leclerc E, Peretz D, Ball H, Sakurai H, Legname G, Serban A, Prusiner SB, Burton DR, Williamson RA (2001) Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J 20:1547-1554.
    • (2001) EMBO J , vol.20 , pp. 1547-1554
    • Leclerc, E.1    Peretz, D.2    Ball, H.3    Sakurai, H.4    Legname, G.5    Serban, A.6    Prusiner, S.B.7    Burton, D.R.8    Williamson, R.A.9
  • 31
    • 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, Lindquist S (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
  • 32
    • 0037195617 scopus 로고    scopus 로고
    • Sc-like conformation in the cytosol
    • Sc-like conformation in the cytosol. Science 298:1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 33
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J, Wollmann R, Lindquist S (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
  • 34
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore N, Smith KL, Graham CH, Jen A, Brady K, Hall S, Morris R (1999) Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J 18:6917-6926.
    • (1999) EMBO J , vol.18 , 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
  • 36
    • 0036125418 scopus 로고    scopus 로고
    • Relative labelling index: A novel stereological approach to test for non-random immunogold labelling of organelles and membranes on transmission electron microscopy thin sections
    • Mayhew TM, Lucocq JM, Griffiths (2002) Relative labelling index: a novel stereological approach to test for non-random immunogold labelling of organelles and membranes on transmission electron microscopy thin sections. J Microsc 205:153-164.
    • (2002) J Microsc , vol.205 , pp. 153-164
    • Mayhew, T.M.1    Lucocq, J.M.2    Griffiths3
  • 37
    • 0032541423 scopus 로고    scopus 로고
    • Cholesterol-dependent retention of GPI-anchored proteins in endosomes
    • Mayor S, Sabharanjak S, Maxfield FR (1998) Cholesterol-dependent retention of GPI-anchored proteins in endosomes. EMBO J 17:4626-4638.
    • (1998) EMBO J , vol.17 , pp. 4626-4638
    • Mayor, S.1    Sabharanjak, S.2    Maxfield, F.R.3
  • 39
    • 0016335085 scopus 로고
    • Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy
    • McLean IW, Nakane PK (1974) Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem 22:1077-1083.
    • (1974) J Histochem Cytochem , vol.22 , pp. 1077-1083
    • McLean, I.W.1    Nakane, P.K.2
  • 40
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • Moser M, Colello RJ, Pott U, Oesch B (1995) Developmental expression of the prion protein gene in glial cells. Neuron 14:509-517.
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 43
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly PC, Harris DA (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
  • 47
    • 0006684399 scopus 로고    scopus 로고
    • Cryo-immunogold electron microscopy
    • (Bonifacino JS, ed). New York: Wiley
    • Peters PJ (2001) Cryo-immunogold electron microscopy, In: Current protocols in cell biology (Bonifacino JS, ed), pp 4.7.1-4.7.12. New York: Wiley.
    • (2001) Current Protocols in Cell Biology , pp. 471-4712
    • Peters, P.J.1
  • 49
    • 0025219885 scopus 로고
    • Immunohistochemical localization of prion protein in spongiform encephalopathies and normal brain tissue
    • Piccardo P, Safar J, Ceroni M, Gajdusek DC, Gibbs Jr CJ (1990) Immunohistochemical localization of prion protein in spongiform encephalopathies and normal brain tissue. Neurology 40:518-522.
    • (1990) Neurology , vol.40 , pp. 518-522
    • Piccardo, P.1    Safar, J.2    Ceroni, M.3    Gajdusek, D.C.4    Gibbs C.J., Jr.5
  • 50
    • 0030478022 scopus 로고    scopus 로고
    • Molecular biology and pathogenesis of prion diseases
    • Prusiner SB (1996) Molecular biology and pathogenesis of prion diseases. Trends Biochem Sci 252:482-487.
    • (1996) Trends Biochem Sci , vol.252 , pp. 482-487
    • Prusiner, S.B.1
  • 51
    • 0030687649 scopus 로고    scopus 로고
    • Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation
    • Raposo G, Tenza D, Mecheri S, Peronet R, Bonnerot C, Desaymard C (1997) Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation. Mol Biol Cell 8:2631-2645.
    • (1997) Mol Biol Cell , vol.8 , pp. 2631-2645
    • Raposo, G.1    Tenza, D.2    Mecheri, S.3    Peronet, R.4    Bonnerot, C.5    Desaymard, C.6
  • 53
    • 0033082870 scopus 로고    scopus 로고
    • Role of the 37 kDa laminin receptor precursor in the life cycle of prions
    • Rieger R, Lasmezas CI, Weiss S (1999) Role of the 37 kDa laminin receptor precursor in the life cycle of prions. Transfus Clin Biol 6:7-16.
    • (1999) Transfus Clin Biol , vol.6 , pp. 7-16
    • Rieger, R.1    Lasmezas, C.I.2    Weiss, S.3
  • 54
    • 0025237593 scopus 로고
    • Subcellular distribution and physicochemical properties of scrapie associated precursor protein and relationship with scrapie agent
    • Safar J, Ceroni M, Piccardo P, Liberski PP, Miyazaki M, Gajdusek DC, Gibbs Jr Cj (1990) Subcellular distribution and physicochemical properties of scrapie associated precursor protein and relationship with scrapie agent. Neurology 40:503-508.
    • (1990) Neurology , vol.40 , pp. 503-508
    • Safar, J.1    Ceroni, M.2    Piccardo, P.3    Liberski, P.P.4    Miyazaki, M.5    Gajdusek, D.C.6    Gibbs C.J., Jr.7
  • 57
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng SL, Huber MT, Harris DA (1993) A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J Biol Chem 21:15922-15928.
    • (1993) J Biol Chem , vol.21 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 58
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein
    • Smith MJ, Koch GL (1989) Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J 8:3581-3586.
    • (1989) EMBO J , vol.8 , pp. 3581-3586
    • Smith, M.J.1    Koch, G.L.2
  • 59
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N, Borchelt DR, Hsiao K, Prusiner SB (1987) Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51:229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 60
    • 0030731674 scopus 로고    scopus 로고
    • Dual topology of the large envelope protein of duck hepatitis B virus: Determinants preventing pre-S translocation and glycosylation
    • Swameye I, Schaller H (1997) Dual topology of the large envelope protein of duck hepatitis B virus: determinants preventing pre-S translocation and glycosylation. J Virol 71:9434-9441.
    • (1997) J Virol , vol.71 , pp. 9434-9441
    • Swameye, I.1    Schaller, H.2
  • 63
    • 0029740354 scopus 로고    scopus 로고
    • Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice
    • Telling GC, Haga T, Torchia M, Tremblay P, DeArmond SJ, Prusiner SB (1996) Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev 10:1736-1750.
    • (1996) Genes Dev , vol.10 , pp. 1736-1750
    • Telling, G.C.1    Haga, T.2    Torchia, M.3    Tremblay, P.4    DeArmond, S.J.5    Prusiner, S.B.6
  • 65
    • 0018679527 scopus 로고
    • Morphometry of the human lung: The state of the art after two decades
    • Weibel ER (1979) Morphometry of the human lung: the state of the art after two decades. Bull Physiopathol Respir (Nancy) 15:999-1013.
    • (1979) Bull Physiopathol Respir (Nancy) , vol.15 , pp. 999-1013
    • Weibel, E.R.1
  • 68
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A (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
  • 69
    • 0029116124 scopus 로고
    • Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences
    • Zhang JT, Ling V (1995) Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences. Biochemistry 34:9159-9165.
    • (1995) Biochemistry , vol.34 , pp. 9159-9165
    • Zhang, J.T.1    Ling, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.