메뉴 건너뛰기




Volumn 5, Issue 1, 1996, Pages 1-11

Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, Aβ25-35

Author keywords

Amyloid; Circular dichroism; Cytotoxicity; MTT reduction; Prion protein

Indexed keywords

AMYLOID;

EID: 0029964280     PISSN: 10558330     EISSN: None     Source Type: Journal    
DOI: 10.1006/neur.1996.0001     Document Type: Article
Times cited : (65)

References (49)
  • 2
    • 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
  • 3
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown DR, Herms J, Kretzchmar HA (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    Kretzchmar, H.A.3
  • 6
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of β-amyloid neurotoxicity
    • Busciglio J, Lorenzo A, Yankner BA (1992) Methodological variables in the assessment of β-amyloid neurotoxicity. Neurobiology of Aging 13:609-612
    • (1992) Neurobiology of Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 7
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell-surface precursor that is both proteasesensitive and phospholipase-sensitive
    • Caughey B, Raymond GJ (1991) The scrapie-associated form of PrP is made from a cell-surface precursor that is both proteasesensitive 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
  • 8
    • 0027535855 scopus 로고
    • Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells
    • Caughey B, Raymond GJ (1993) Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J Virol 67:643-650
    • (1993) J Virol , vol.67 , pp. 643-650
    • Caughey, B.1    Raymond, G.J.2
  • 10
    • 0027394220 scopus 로고
    • Synaptic degeneration is the primary neuropathological feature in prion disease: A preliminary study
    • Clinton J, Forsyth C, Royston MC, Roberts GW (1993) Synaptic degeneration is the primary neuropathological feature in prion disease: a preliminary study. Neuroreport 4:65-68
    • (1993) Neuroreport , vol.4 , pp. 65-68
    • Clinton, J.1    Forsyth, C.2    Royston, M.C.3    Roberts, G.W.4
  • 11
    • 0026713423 scopus 로고
    • β-amyloid neurotoxicity - A discussion of in vitro findings
    • Cotman CW, Pike CJ, Copani A (1992) β-amyloid neurotoxicity - a discussion of in vitro findings. Neurobiology of Aging 13:587-590
    • (1992) Neurobiology of Aging , vol.13 , pp. 587-590
    • Cotman, C.W.1    Pike, C.J.2    Copani, A.3
  • 12
    • 0028301577 scopus 로고
    • Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
    • Degioia L, Selvaggini C, Ghibaudi E, Diomede L, Bugiani O. Forloni G, Tagliavini F, Salmona M (1994) Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J Biol Chem 269:7859-7862
    • (1994) J Biol Chem , vol.269 , pp. 7859-7862
    • Degioia, L.1    Selvaggini, C.2    Ghibaudi, E.3    Diomede, L.4    Bugiani, O.5    Forloni, G.6    Tagliavini, F.7    Salmona, M.8
  • 15
    • 0027741445 scopus 로고
    • Diversity in the neuropathology of scrapie-like diseases in animals
    • Fraser H (1993) Diversity in the neuropathology of scrapie-like diseases in animals. British Medical Bulletin 49:792-809
    • (1993) British Medical Bulletin , vol.49 , pp. 792-809
    • Fraser, H.1
  • 17
    • 0027717592 scopus 로고
    • PrP gene and its association with spongiform encephalopathies
    • Goldmann W (1993) PrP gene and its association with spongiform encephalopathies. British Medical Bulletin 49:839-859
    • (1993) British Medical Bulletin , vol.49 , pp. 839-859
    • Goldmann, W.1
  • 18
    • 0026017096 scopus 로고
    • Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein coding exon
    • Goldmann W, Hunter N, Martin T, Dawson M, Hope J (1991) Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein coding exon. J Gen Virol 72:201-204
    • (1991) J Gen Virol , vol.72 , pp. 201-204
    • Goldmann, W.1    Hunter, N.2    Martin, T.3    Dawson, M.4    Hope, J.5
  • 19
    • 0028801680 scopus 로고
    • Loss of synaptophysin-like immunoreactivity in the hippocampal-formation is an early phenomenon in Alzheimer's disease
    • Heinonen O, Soininen H, Sorvari H, Kosunen O, Paljarvi L, Koivisto E, Riekkinen PJ (1995) Loss of synaptophysin-like immunoreactivity in the hippocampal-formation is an early phenomenon in Alzheimer's disease. Neuroscience 64:375-384
    • (1995) Neuroscience , vol.64 , pp. 375-384
    • Heinonen, O.1    Soininen, H.2    Sorvari, H.3    Kosunen, O.4    Paljarvi, L.5    Koivisto, E.6    Riekkinen, P.J.7
  • 20
    • 0028218378 scopus 로고
    • Scrapie, Creutzfeldt-Jakob disease and bovine spongiform encephalopathy - The key role of a nerve membrane protein (PrP)
    • Hope J, Chong A (1994) Scrapie, Creutzfeldt-Jakob disease and bovine spongiform encephalopathy - the key role of a nerve membrane protein (PrP). Biochemical Society Transactions 22:159-163
    • (1994) Biochemical Society Transactions , vol.22 , pp. 159-163
    • Hope, J.1    Chong, A.2
  • 21
    • 0025880864 scopus 로고
    • The scrapie fibril protein and its cellular isoform
    • Hope J, Manson J (1991) The scrapie fibril protein and its cellular isoform. Curr Top Micro Immun 172:57-74
    • (1991) Curr Top Micro Immun , vol.172 , pp. 57-74
    • Hope, J.1    Manson, J.2
  • 22
    • 0022802258 scopus 로고
    • The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge-distribution and Nterminal protein-sequence as predicted for the normal brain protein (PrP)
    • Hope J, Morton LJD, Farquhar CF, Multhaup G, Beyreuther K, Kimberlin RH (1986) The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge-distribution and Nterminal protein-sequence as predicted for the normal brain protein (PrP). Embo J 5:2591-2597
    • (1986) Embo J , vol.5 , pp. 2591-2597
    • Hope, J.1    Morton, L.J.D.2    Farquhar, C.F.3    Multhaup, G.4    Beyreuther, K.5    Kimberlin, R.H.6
  • 23
    • 0023975851 scopus 로고
    • Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie
    • Hope J, Multhaup G, Reekie LJ, KimberlinRH, Beyreuther K (1988a) Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie. Eur J Biochem 172:271-277
    • (1988) Eur J Biochem , vol.172 , pp. 271-277
    • Hope, J.1    Multhaup, G.2    Reekie, L.J.3    Kimberlin, R.H.4    Beyreuther, K.5
  • 26
    • 0026739272 scopus 로고
    • Are Sine and the PrP gene congruent? Evidence from PrP gene analysis in Sine congenic mice
    • Hunter N, Dann JC, Bennett AD, Somerville RA, McConnell I, Hope J (1992) Are Sine and the PrP gene congruent? Evidence from PrP gene analysis in Sine congenic mice. J Gen Virol 73:2751-2755
    • (1992) J Gen Virol , vol.73 , pp. 2751-2755
    • Hunter, N.1    Dann, J.C.2    Bennett, A.D.3    Somerville, R.A.4    McConnell, I.5    Hope, J.6
  • 28
    • 0028263412 scopus 로고
    • Murine scrapie-infected neurons in vivo release excess prion protein into the extracellular space
    • Jeffrey M, Goodsir CM, Bruce ME, McBride PA, Fowler N, Scott JR (1994b) Murine scrapie-infected neurons in vivo release excess prion protein into the extracellular space. Neuroscience Let 174:39-42
    • (1994) Neuroscience Let , vol.174 , pp. 39-42
    • Jeffrey, M.1    Goodsir, C.M.2    Bruce, M.E.3    McBride, P.A.4    Fowler, N.5    Scott, J.R.6
  • 31
    • 0026542737 scopus 로고
    • From slow virus to prion: A review of transmissible spongiform encephalopathies
    • Lantos PL (1992) From slow virus to prion: a review of transmissible spongiform encephalopathies. Histopathology 20:1-11
    • (1992) Histopathology , vol.20 , pp. 1-11
    • Lantos, P.L.1
  • 32
    • 0028703452 scopus 로고
    • PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology
    • Manson JC, Clarke AR, McBride PA, McConnell I, Hope J (1994) PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegen 3:331-340
    • (1994) Neurodegen , vol.3 , pp. 331-340
    • Manson, J.C.1    Clarke, A.R.2    McBride, P.A.3    McConnell, I.4    Hope, J.5
  • 34
    • 0027511905 scopus 로고
    • The role of synaptic proteins in the pathogenesis of disorders of the central-nervous-system
    • Masliah E, Terry R (1993) The role of synaptic proteins in the pathogenesis of disorders of the central-nervous-system. Brain Pathology 3:77-85
    • (1993) Brain Pathology , vol.3 , pp. 77-85
    • Masliah, E.1    Terry, R.2
  • 35
    • 0027495192 scopus 로고
    • The synaptic organization of the neocortex in Alzheimers disease
    • Masliah E, Miller A, Terry RD (1993) The synaptic organization of the neocortex in Alzheimers disease. Medical Hypotheses 41:334-340
    • (1993) Medical Hypotheses , vol.41 , pp. 334-340
    • Masliah, E.1    Miller, A.2    Terry, R.D.3
  • 38
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW (1991) In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity Brain Res 563:311-314
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 40
    • 0028870182 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β-amyloid in rat PC12 cells
    • Pollack SJ, Sadler UJ, Hawtin SR, Tailor VJ, Shearman MS (1995) Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β-amyloid in rat PC12 cells. Neuroscience Let 184:113-116
    • (1995) Neuroscience Let , vol.184 , pp. 113-116
    • Pollack, S.J.1    Sadler, U.J.2    Hawtin, S.R.3    Tailor, V.J.4    Shearman, M.S.5
  • 41
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S, Glockner J (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33-37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.1    Glockner, J.2
  • 45
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • USA
    • Shearman MS, Ragan CI, Iversen LL (1994) Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc Natl Acad Sci, USA 91:1470-1474
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 46
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides
    • Shearman MS, Hawtin SR, Tailor VJ (1995) The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides. Journal of Neurochemistry 65:218-227
    • (1995) Journal of Neurochemistry , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.