메뉴 건너뛰기




Volumn 105, Issue 6, 2008, Pages 2190-2204

Non-infectious aggregates of the prion protein react with several PrP Sc-directed antibodies

Author keywords

Monoclonal antibody; Prion; Prion protein; Protein aggregate; PrPSc

Indexed keywords

IMMUNOGLOBULIN G; IMMUNOGLOBULIN M ANTIBODY; PRION PROTEIN; RECOMBINANT PROTEIN;

EID: 44649192383     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2008.05306.x     Document Type: Article
Times cited : (48)

References (58)
  • 1
    • 3242661985 scopus 로고    scopus 로고
    • GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice
    • Barmada S., Piccardo P., Yamaguchi K., Ghetti B. Harris D. A. (2004) GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice. Neurobiol. Dis. 16, 527 537.
    • (2004) Neurobiol. Dis. , vol.16 , pp. 527-537
    • Barmada, S.1    Piccardo, P.2    Yamaguchi, K.3    Ghetti, B.4    Harris, D.A.5
  • 2
    • 34249947345 scopus 로고    scopus 로고
    • Converting the prion protein: What makes the protein infectious
    • Baskakov I. V. Breydo L. (2007) Converting the prion protein: what makes the protein infectious. Biochim. Biophys. Acta 1772, 692 703.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 692-703
    • Baskakov, I.V.1    Breydo, L.2
  • 4
    • 39749094951 scopus 로고    scopus 로고
    • Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion
    • Biasini E., Medrano A. Z., Thellung S., Chiesa R. Harris D. A. (2007) Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion. J. Neurochem. 104, 1293 1308.
    • (2007) J. Neurochem. , vol.104 , pp. 1293-1308
    • Biasini, E.1    Medrano, A.Z.2    Thellung, S.3    Chiesa, R.4    Harris, D.A.5
  • 6
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • Caughey B. (2001) Interactions between prion protein isoforms: the kiss of death? Trends Biochem. Sci. 26, 235 242.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 235-242
    • Caughey, B.1
  • 7
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey B. W., Dong A., Bhat K. S., Ernst D., Hayes S. F. Caughey W. S. (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30, 7672 7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 8
    • 0032775473 scopus 로고    scopus 로고
    • Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence
    • Chabry J., Priola S. A., Wehrly K., Nishio J., Hope J. Chesebro B. (1999) Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence. J. Virol. 73, 6245 6250.
    • (1999) J. Virol. , vol.73 , pp. 6245-6250
    • Chabry, J.1    Priola, S.A.2    Wehrly, K.3    Nishio, J.4    Hope, J.5    Chesebro, B.6
  • 9
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa R. Harris D. A. (2001) Prion diseases: what is the neurotoxic molecule? Neurobiol. Dis. 8, 743 763.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 10
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa R., Piccardo P., Ghetti B. Harris D. A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339 1351.
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 11
    • 0034625069 scopus 로고    scopus 로고
    • Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation
    • Chiesa R., Drisaldi B., Quaglio E., Migheli A., Piccardo P., Ghetti B. Harris D. A. (2000) Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation. Proc. Natl Acad. Sci. USA 97, 5574 5579.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5574-5579
    • Chiesa, R.1    Drisaldi, B.2    Quaglio, E.3    Migheli, A.4    Piccardo, P.5    Ghetti, B.6    Harris, D.A.7
  • 13
    • 0030896803 scopus 로고    scopus 로고
    • Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells
    • Daude N., Lehmann S. Harris D. A. (1997) Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272, 11604 11612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11604-11612
    • Daude, N.1    Lehmann, S.2    Harris, D.A.3
  • 14
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi B., Stewart R. S., Adles C., Stewart L. R., Quaglio E., Biasini E., Fioriti L., Chiesa R. Harris D. A. (2003) Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J. Biol. Chem. 278, 21732 21743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3    Stewart, L.R.4    Quaglio, E.5    Biasini, E.6    Fioriti, L.7    Chiesa, R.8    Harris, D.A.9
  • 15
    • 15744395826 scopus 로고    scopus 로고
    • Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations
    • Fioriti L., Dossena S., Stewart L. R., Stewart R. S., Harris D. A., Forloni G. Chiesa R. (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
  • 16
    • 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., Dolph M. J., Deleault N. R., Geoghegan J. C., Khurana V., Feany M. B., Dolph P. J. Supattapone S. (2006) Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Straussler-Scheinker syndrome. J. Neurosci. 26, 12408 12414.
    • (2006) J. Neurosci. , vol.26 , pp. 12408-12414
    • Gavin, B.A.1    Dolph, M.J.2    Deleault, N.R.3    Geoghegan, J.C.4    Khurana, V.5    Feany, M.B.6    Dolph, P.J.7    Supattapone, S.8
  • 17
    • 33646126278 scopus 로고    scopus 로고
    • New insights into prion structure and toxicity
    • Harris D. A. True H. L. (2006) New insights into prion structure and toxicity. Neuron 50, 353 357.
    • (2006) Neuron , vol.50 , pp. 353-357
    • Harris, D.A.1    True, H.L.2
  • 18
    • 0035834680 scopus 로고    scopus 로고
    • Mutant prion proteins are partially retained in the endoplasmic reticulum
    • Ivanova L., Barmada S., Kummer T. Harris D. A. (2001) Mutant prion proteins are partially retained in the endoplasmic reticulum. J. Biol. Chem. 276, 42409 42421.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42409-42421
    • Ivanova, L.1    Barmada, S.2    Kummer, T.3    Harris, D.A.4
  • 21
    • 0030613755 scopus 로고    scopus 로고
    • Sc)-specific epitope defined by a monoclonal antibody
    • Sc)-specific epitope defined by a monoclonal antibody. Nature 390, 74 77.
    • (1997) Nature , vol.390 , pp. 74-77
    • Korth, C.1    Stierli, B.2    Streit, P.3
  • 24
    • 0030006902 scopus 로고    scopus 로고
    • Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform
    • Lehmann S. Harris D. A. (1996a) Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc. Natl Acad. Sci. USA 93, 5610 5614.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5610-5614
    • Lehmann, S.1    Harris, D.A.2
  • 25
    • 0030050733 scopus 로고    scopus 로고
    • Mutant and infectious prion proteins display common biochemical properties in cultured cells
    • Lehmann S. Harris D. A. (1996b) Mutant and infectious prion proteins display common biochemical properties in cultured cells. J. Biol. Chem. 271, 1633 1637.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1633-1637
    • Lehmann, S.1    Harris, D.A.2
  • 26
    • 33846543360 scopus 로고    scopus 로고
    • Neonatal lethality in transgenic mice expressing prion protein with a deletion of residues 105-125
    • Li A., Christensen H. M., Stewart L. R., Roth K. A., Chiesa R. Harris D. A. (2007) Neonatal lethality in transgenic mice expressing prion protein with a deletion of residues 105-125. EMBO J. 26, 548 558.
    • (2007) EMBO J. , vol.26 , pp. 548-558
    • Li, A.1    Christensen, H.M.2    Stewart, L.R.3    Roth, K.A.4    Chiesa, R.5    Harris, D.A.6
  • 27
    • 34547702317 scopus 로고    scopus 로고
    • Characterization of the prion protein 3F4 epitope and its use as a molecular tag
    • Lund C., Olsen C. M., Tveit H. Tranulis M. A. (2007) Characterization of the prion protein 3F4 epitope and its use as a molecular tag. J. Neurosci. Methods 165, 183 190.
    • (2007) J. Neurosci. Methods , vol.165 , pp. 183-190
    • Lund, C.1    Olsen, C.M.2    Tveit, H.3    Tranulis, M.A.4
  • 28
    • 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
  • 29
    • 3142762315 scopus 로고    scopus 로고
    • Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils
    • Morel N., Simon S., Frobert Y., Volland H., Mourton-Gilles C., Negro A., Sorgato M. C., Creminon C. Grassi J. (2004) Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils. J. Biol. Chem. 279, 30143 30149.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30143-30149
    • Morel, N.1    Simon, S.2    Frobert, Y.3    Volland, H.4    Mourton-Gilles, C.5    Negro, A.6    Sorgato, M.C.7    Creminon, C.8    Grassi, J.9
  • 32
    • 22744448690 scopus 로고    scopus 로고
    • Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice
    • Nazor K. E., Kuhn F., Seward T. et al. (2005) Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice. EMBO J. 24, 2472 2480.
    • (2005) EMBO J. , vol.24 , pp. 2472-2480
    • Nazor, K.E.1    Kuhn, F.2    Seward, T.3
  • 34
    • 4444356433 scopus 로고    scopus 로고
    • Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion
    • Pan T., Li R., Kang S. C., Wong B. S., Wisniewski T. Sy M. S. (2004) Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion. J. Neurochem. 90, 1205 1217.
    • (2004) J. Neurochem. , vol.90 , pp. 1205-1217
    • Pan, T.1    Li, R.2    Kang, S.C.3    Wong, B.S.4    Wisniewski, T.5    Sy, M.S.6
  • 36
    • 0038717543 scopus 로고    scopus 로고
    • A prion protein epitope selective for the pathologically misfolded conformation
    • Paramithiotis E., Pinard M., Lawton T. et al. (2003) A prion protein epitope selective for the pathologically misfolded conformation. Nat. Med. 9, 893 899.
    • (2003) Nat. Med. , vol.9 , pp. 893-899
    • Paramithiotis, E.1    Pinard, M.2    Lawton, T.3
  • 37
    • 0031592937 scopus 로고    scopus 로고
    • A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
    • Peretz D., Williamson R. A., Matsunaga Y. et al. (1997) A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273, 614 622.
    • (1997) J. Mol. Biol. , vol.273 , pp. 614-622
    • Peretz, D.1    Williamson, R.A.2    Matsunaga, Y.3
  • 38
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D., Williamson R. A., Kaneko K. et al. (2001) Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412, 739 743.
    • (2001) Nature , vol.412 , pp. 739-743
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3
  • 39
    • 0032496218 scopus 로고    scopus 로고
    • Abnormal properties of prion protein with insertional mutations in different cell types
    • Priola S. A. Chesebro B. (1998) Abnormal properties of prion protein with insertional mutations in different cell types. J. Biol. Chem. 273, 11980 11985.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11980-11985
    • Priola, S.A.1    Chesebro, B.2
  • 41
    • 0003661592 scopus 로고    scopus 로고
    • ed. pp. 1050. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • Prusiner S. B., ed 2004) Prion Biology and Diseases, 2nd Edn, pp. 1050. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2004) Prion Biology and Diseases, 2nd Edn
    • Prusiner, S.B.1
  • 42
    • 0034705438 scopus 로고    scopus 로고
    • Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation
    • Qin K., Yang D.-S., Yang Y., Chishti M. A., Meng L.-J., Kretzschmar H. A., Yip C. M., Fraser P. E. Westaway D. (2000) Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation. J. Biol. Chem. 275, 19121 19131.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19121-19131
    • Qin, K.1    Yang, D.-S.2    Yang, Y.3    Chishti, M.A.4    Meng, L.-J.5    Kretzschmar, H.A.6    Yip, C.M.7    Fraser, P.E.8    Westaway, D.9
  • 43
    • 0035815738 scopus 로고    scopus 로고
    • Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform
    • Quaglio E., Chiesa R. Harris D. A. (2001) Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform. J. Biol. Chem. 276, 11432 11438.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11432-11438
    • Quaglio, E.1    Chiesa, R.2    Harris, D.A.3
  • 45
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya M. R., Sambashivan S., Nelson R. et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447, 453 457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3
  • 47
    • 0036310430 scopus 로고    scopus 로고
    • The binding of prion proteins to serum components is affected by detergent extraction conditions
    • Shaked Y., Engelstein R. Gabizon R. (2002) The binding of prion proteins to serum components is affected by detergent extraction conditions. J. Neurochem. 82, 1 5.
    • (2002) J. Neurochem. , vol.82 , pp. 1-5
    • Shaked, Y.1    Engelstein, R.2    Gabizon, R.3
  • 50
    • 4844220510 scopus 로고    scopus 로고
    • Diagnosing prion diseases: Needs, challenges and hopes
    • Soto C. (2004) Diagnosing prion diseases: needs, challenges and hopes. Nat. Rev. Microbiol. 2, 809 819.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 809-819
    • Soto, C.1
  • 51
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • Swietnicki W., Morillas M., Chen S. G., Gambetti P. Surewicz W. K. (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39, 424 431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 52
    • 34249903623 scopus 로고    scopus 로고
    • Prion recognition elements govern nucleation, strain specificity and species barriers
    • Tessier P. M. Lindquist S. (2007) Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 447, 556 561.
    • (2007) Nature , vol.447 , pp. 556-561
    • Tessier, P.M.1    Lindquist, S.2
  • 53
    • 9444267651 scopus 로고    scopus 로고
    • The state of the prion
    • Weissmann C. (2004) The state of the prion. Nat. Rev. Microbiol. 2, 861 871.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 861-871
    • Weissmann, C.1
  • 54
    • 34250644988 scopus 로고    scopus 로고
    • Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans
    • Yin S., Pham N., Yu S. et al. (2007) Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans. Proc. Natl Acad. Sci. USA 104, 7546 7551.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 7546-7551
    • Yin, S.1    Pham, N.2    Yu, S.3
  • 56
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding
    • Zahn R., Vonschroetter C. Wüthrich K. (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett. 417, 400 404.
    • (1997) FEBS Lett. , vol.417 , pp. 400-404
    • Zahn, R.1    Vonschroetter, C.2    Wüthrich, K.3
  • 57
    • 13144256747 scopus 로고    scopus 로고
    • Prion protein expression in different species: Analysis with a panel of new mAbs
    • Zanusso G., Liu D., Ferrari S. et al. (1998) Prion protein expression in different species: analysis with a panel of new mAbs. Proc. Natl Acad. Sci. USA 95, 8812 8816.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8812-8816
    • Zanusso, G.1    Liu, D.2    Ferrari, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.