메뉴 건너뛰기




Volumn 274, Issue 6, 2007, Pages 1492-1502

Binding of N- and C-terminal anti-prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrPC) obtained from human, sheep, cattle and mouse

Author keywords

Antibody; Glycotyping; Prion protein; PrPC; Signal intensity

Indexed keywords

PRION PROTEIN; PROTEINASE;

EID: 33847361034     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05691.x     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • Collinge J, Sidle KC, Meads J, Ironside J & Hill AF (1996) Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383, 685-690.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 3
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB (1991) Molecular biology of prion diseases. Science 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 6
    • 0032813254 scopus 로고    scopus 로고
    • Differences in proteinase K resistance and neuronal deposition of abnormal prion proteins characterize bovine spongiform encephalopathy (BSE) and scrapie strains
    • Kuczius T & Groschup MH (1999) Differences in proteinase K resistance and neuronal deposition of abnormal prion proteins characterize bovine spongiform encephalopathy (BSE) and scrapie strains. Mol Med 5, 406-418.
    • (1999) Mol Med , vol.5 , pp. 406-418
    • Kuczius, T.1    Groschup, M.H.2
  • 8
    • 0141514771 scopus 로고    scopus 로고
    • Sporadic and familial CJD: Classification and characterisation
    • Gambetti P, Kong Q, Zou W, Parchi P & Chen SG (2003) Sporadic and familial CJD: classification and characterisation. Br Med Bull 66, 213-239.
    • (2003) Br Med Bull , vol.66 , pp. 213-239
    • Gambetti, P.1    Kong, Q.2    Zou, W.3    Parchi, P.4    Chen, S.G.5
  • 11
    • 0037071904 scopus 로고    scopus 로고
    • A journey through the species barrier
    • Chen SG & Gambetti P (2002) A journey through the species barrier. Neuron 34, 854-856.
    • (2002) Neuron , vol.34 , pp. 854-856
    • Chen, S.G.1    Gambetti, P.2
  • 12
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
    • Kocisko DA, Priola SA, Raymond GJ, Chesebro B, Lansbury PT Jr & Caughey B (1995) Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Proc Natl Acad Sci USA 92, 3923-3927.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    Lansbury Jr, P.T.5    Caughey, B.6
  • 17
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl N, Baldwin MA, Burlingame AL & Prusiner SB (1990) Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochem 29, 8879-8884.
    • (1990) Biochem , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 18
    • 0027733637 scopus 로고
    • Scrapie associated PrP accumulation and its prevention: Insights from cell culture
    • Caughey B (1993) Scrapie associated PrP accumulation and its prevention: insights from cell culture. Br Med Bull 49, 860-872.
    • (1993) Br Med Bull , vol.49 , pp. 860-872
    • Caughey, B.1
  • 24
    • 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 268, 15922-15928.
    • (1993) J Biol Chem , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 25
    • 0031765769 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues
    • Jimenez-Huete A, Lievens PM, Vidal R, Piccardo P, Ghetti B, Tagliavini F, Frangione B & Prelli F (1998) Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am J Pathol 153, 1561-1572.
    • (1998) Am J Pathol , vol.153 , pp. 1561-1572
    • Jimenez-Huete, A.1    Lievens, P.M.2    Vidal, R.3    Piccardo, P.4    Ghetti, B.5    Tagliavini, F.6    Frangione, B.7    Prelli, F.8
  • 27
    • 17144367284 scopus 로고    scopus 로고
    • Proteolytic processing and glycosylation influence formation of porcine prion protein complexes
    • Nieznanski K, Rutkowski M, Dominik M & Stepkowski D (2005) Proteolytic processing and glycosylation influence formation of porcine prion protein complexes. Biochem J 387, 93-100.
    • (2005) Biochem J , vol.387 , pp. 93-100
    • Nieznanski, K.1    Rutkowski, M.2    Dominik, M.3    Stepkowski, D.4
  • 28
    • 28844504671 scopus 로고    scopus 로고
    • Proteolytic cleavage and shedding of the bovine prion protein in two cell culture systems
    • Zhao H, Klingeborn M, Simonsson M & Linne T (2006) Proteolytic cleavage and shedding of the bovine prion protein in two cell culture systems. Virus Res 115, 43-55.
    • (2006) Virus Res , vol.115 , pp. 43-55
    • Zhao, H.1    Klingeborn, M.2    Simonsson, M.3    Linne, T.4
  • 30
    • 0042921669 scopus 로고    scopus 로고
    • Cases of scrapie with unusual features in Norway and designation of a new type Nor98
    • Benestad SL, Sarradin P, Thu B, Schonheit J, Tranulis MA & Bratberg B (2003) Cases of scrapie with unusual features in Norway and designation of a new type Nor98. Vet Rec 153, 202-208.
    • (2003) Vet Rec , vol.153 , pp. 202-208
    • Benestad, S.L.1    Sarradin, P.2    Thu, B.3    Schonheit, J.4    Tranulis, M.A.5    Bratberg, B.6
  • 33
    • 0031704901 scopus 로고    scopus 로고
    • Molecular analysis of bovine spongiform encephalopathy and scrapie strain variation
    • Kuczius T, Haist I & Groschup MH (1998) Molecular analysis of bovine spongiform encephalopathy and scrapie strain variation. J Infect Dis 178, 693-699.
    • (1998) J Infect Dis , vol.178 , pp. 693-699
    • Kuczius, T.1    Haist, I.2    Groschup, M.H.3
  • 34
    • 1842457751 scopus 로고    scopus 로고
    • Comparative molecular analysis of the abnormal prion protein in field scrapie cases and experimental bovine spongiform encephalopathy in sheep by use of western blotting and immunohistochemical methods
    • Lezmi S, Martin S, Simon S, Comoy E, Bencsik A, Deslys JP, Grassi J, Jeffrey M & Baron T (2004) Comparative molecular analysis of the abnormal prion protein in field scrapie cases and experimental bovine spongiform encephalopathy in sheep by use of western blotting and immunohistochemical methods. J Virol 78, 3654-3662.
    • (2004) J Virol , vol.78 , pp. 3654-3662
    • Lezmi, S.1    Martin, S.2    Simon, S.3    Comoy, E.4    Bencsik, A.5    Deslys, J.P.6    Grassi, J.7    Jeffrey, M.8    Baron, T.9
  • 40
    • 0032781345 scopus 로고    scopus 로고
    • Peptides and proteins in neurodegenerative disease: Helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy
    • Liu A, Riek R, Zahn R, Hornemann S, Glockshuber R & Wuthrich K (1999) Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy. Biopolymers 51, 145-152.
    • (1999) Biopolymers , vol.51 , pp. 145-152
    • Liu, A.1    Riek, R.2    Zahn, R.3    Hornemann, S.4    Glockshuber, R.5    Wuthrich, K.6
  • 43
    • 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 MC, 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
  • 45
    • 0030589822 scopus 로고    scopus 로고
    • Induction of antibodies against human prion proteins (PrP) by DNA-mediated immunization of PrP0/0 mice
    • Krasemann S, Groschup M, Hunsmann G & Bodemer W (1996) Induction of antibodies against human prion proteins (PrP) by DNA-mediated immunization of PrP0/0 mice. J Immunol Methods 199, 109-118.
    • (1996) J Immunol Methods , vol.199 , pp. 109-118
    • Krasemann, S.1    Groschup, M.2    Hunsmann, G.3    Bodemer, W.4
  • 46
    • 0345540635 scopus 로고    scopus 로고
    • Generation of monoclonal antibodies against prion proteins with an unconventional nucleic acid-based immunization strategy
    • Krasemann S, Jurgens T & Bodemer W (1999) Generation of monoclonal antibodies against prion proteins with an unconventional nucleic acid-based immunization strategy. J Biotechnol 73, 119-129.
    • (1999) J Biotechnol , vol.73 , pp. 119-129
    • Krasemann, S.1    Jurgens, T.2    Bodemer, W.3
  • 47
    • 0031957898 scopus 로고    scopus 로고
    • Synthetic peptide vaccines yield monoclonal antibodies to cellular and pathological prion proteins of ruminants
    • Harmeyer S, Pfaff E & Groschup MH (1998) Synthetic peptide vaccines yield monoclonal antibodies to cellular and pathological prion proteins of ruminants. J General Virol 79, 937-945.
    • (1998) J General Virol , vol.79 , pp. 937-945
    • Harmeyer, S.1    Pfaff, E.2    Groschup, M.H.3
  • 49
    • 4544335297 scopus 로고    scopus 로고
    • Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding
    • Kuczius T, Buschmann A, Zhang W, Karch H, Becker K, Peters G & Groschup MH (2004) Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding. Biol Chem 385, 739-747.
    • (2004) Biol Chem , vol.385 , pp. 739-747
    • Kuczius, T.1    Buschmann, A.2    Zhang, W.3    Karch, H.4    Becker, K.5    Peters, G.6    Groschup, M.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.