The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons
Open accessAbstract
A growing body of evidence indicates that small, soluble oligomeric species generated from a variety of proteins and peptides rather than mature amyloid fibrils are inherently highly cytotoxic. Here, we show for the first time that mature amyloid fibrils produced from full-length recombinant mammalian prion protein (rPrP) were highly toxic to cultured cells and primary hippocampal and cerebella neurons. Fibrils induced apoptotic cell death in a time- and dose-dependent manner. The toxic effect of fibrils was comparable with that exhibited by soluble small beta-oligomers generated from the same protein. Fibrils prepared from insulin were not toxic, suggesting that the toxic effect was not solely due to the highly polymeric nature of the fibrillar form. The cell death caused by rPrP fibrils or beta-oligomers was substantially reduced when expression of endogenous PrP(C) was down-regulated by small interfering RNAs. In opposition to the beta-oligomer and amyloid fibrils of rPrP, the monomeric alpha-helical form of rPrP stimulated neurite out-growth and survival of neurons. These studies illustrated that both soluble beta-oligomer and amyloid fibrils of the prion protein are intrinsically toxic and confirmed that endogenously expressed PrP(C) is required for mediating the toxicity of abnormally folded external PrP aggregates.
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Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Role of microglia in neuronal cell death in prion disease
Giese, A., Brown, D. R., Groschup, M. H., Feldmann, C., Haist, I., & Kretzschmar, H. A. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00167.x · Cited by 239
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Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
Engel, M. F. M., Khemtémourian, L., Kleijer, C. C., Meeldijk, H. J. D., Jacobs, J., Verkleij, A. J., de Kruijff, B., Killian, J. A., & Höppener, J. W. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708354105 · Cited by 466
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Metadata
- Authors
- Novitskaya, V., Bocharova, O. V., Bronstein, I., & Baskakov, I. V.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-05
- Volume
- 281
- Issue
- 19
- Pages
- 13828-13836
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1995609479
- Cited by
- 247
- References
- 6
- FWCI
- 7.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Novitskaya, V., Bocharova, O. V., Bronstein, I., & Baskakov, I. V. (2006). Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m511174200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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