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Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Open accessAbstract
Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-β (Aβ)–containing brain extracts from humans with Alzheimer's disease or β-amyloid precursor protein (APP) transgenic mice induced cerebral β-amyloidosis and associated pathology in APP transgenic mice in a time- and concentration-dependent manner. The seeding activity of brain extracts was reduced or abolished by Aβ immunodepletion, protein denaturation, or by Aβ immunization of the host. The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic Aβ strains with varying biological activities reminiscent of prion strains.
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“Experimentally, cerebral β-amyloidosis can be exogenously induced by exposure to dilute brain extracts containing aggregated Aβ seeds.”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [51]
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
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
Self-citationDiffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
Self-citationSelf-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
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507
Self-citationCherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
Folding proteins in fatal ways
Selkoe, D. J. (2003) · Nature · doi:10.1038/nature02264 · Cited by 1,432
Legname, G., Baskakov, I. V., Nguyen, H.-O. B., Riesner, D., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2004) · Science · doi:10.1126/science.1100195 · Cited by 1,022
Aβ42‐driven cerebral amyloidosis in transgenic mice reveals early and robust pathology
Radde, R., Bolmont, T., Kaeser, S. A., Coomaraswamy, J., Lindau, D., Stoltze, L., Calhoun, M. E., Jäggi, F., Wolburg, H., Gengler, S., et al. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400784 · Cited by 986
Self-citationRoher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799
Anchorless Prion Protein Results in Infectious Amyloid Disease Without Clinical Scrapie
Chesebro, B. W., Trifilo, M. J., Race, R., Meade-White, K. D., Teng, C., LaCasse, R. A., Raymond, L. D., Favara, C., Baron, G. S., Priola, S. A., et al. (2005) · Science · doi:10.1126/science.1110837 · Cited by 662
Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559
Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
Guela, C., Wu, C.-K., Saroff, D., Lorenzo, A., Yuan, M., & Yankner, B. A. (1998) · Nature Medicine · doi:10.1038/nm0798-827 · Cited by 520
Calhoun, M. E., Burgermeister, P., Phinney, A. L., Stalder, M., Tolnay, M., Wiederhold, K.-H., Abramowski, D., Sturchler-Pierrat, C., Sommer, B., Staufenbiel, M., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.14088 · Cited by 410
Self-citationKane, M. D., Lipinski, W. J., Callahan, M. J., Bian, F., Durham, R. A., Schwarz, R. D., Roher, A. E., & Walker, L. C. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-10-03606.2000 · Cited by 394
Self-citationCommon structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
Glabe, C. G., & Kayed, R. (2006) · Neurology · doi:10.1212/01.wnl.0000192103.24796.42 · Cited by 367
Emerging Principles of Conformation-Based Prion Inheritance
Chien, P., Weissman, J. S., & DePace, A. H. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161837 · Cited by 327
Jones, E. M., & Surewicz, W. K. (2005) · Cell · doi:10.1016/j.cell.2005.01.034 · Cited by 251
Stéphan, A., Laroche, S., & Davis, S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-15-05703.2001 · Cited by 228
Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease
Aguzzi, A., & Haass, C. (2003) · Science · doi:10.1126/science.1087348 · Cited by 223
Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion
Prinz, M., Heikenwälder, M. F., Junt, T., Schwarz, P., Glatzel, M., Heppner, F. L., Fu, Y., Lipp, M., & Aguzzi, A. (2003) · Nature · doi:10.1038/nature02072 · Cited by 217
β-Amyloid Is Different in Normal Aging and in Alzheimer Disease
Piccini, A., Russo, C., Gliozzi, A., Relini, A., Vitali, A., Borghi, R., Giliberto, L., Armirotti, A., D’Arrigo, C., Bachi, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501694200 · Cited by 192
Very long term studies of the seeding of β-amyloidosis in primates
Ridley, R. M., Baker, H. F., Windle, C. P., & Cummings, R. M. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0385-2 · Cited by 190
Schmechel, A., Zentgraf, H., Scheuermann, S., Fritz, G., Pipkorn, R., Reed, J., Beyreuther, K. T., Bayer, T. A., & Multhaup, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303547200 · Cited by 69
Mohajeri, M. H., Wollmer, M. A., & Nitsch, R. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202899200 · Cited by 66
DeMattos, R. B. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:255 · Cited by 55
Research works printed but not linked: 1
- C. G. Glabe, R. Kayed, Neurology66, S74 (2006).
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Metadata
- Authors
- Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., Vigouret, J.-M., Paganetti, P., Walsh, D. M., Mathews, P. M., Ghiso, J., Staufenbiel, M., Walker, L. C., & Jucker, M.
- Affiliations
- Department of Cellular Neurology, Hertie-Institute for Clinical Brain Research, University of Tübingen, D-72076 Tübingen, Germany.
- University College Dublin (IE)
- Corresponding author
- Coomaraswamy, Janaky
- Bolmont, Tristan
- Walker, Lary C.
- Jucker, Mathias
- ORCID
- Venue
- Science
- Published
- 2006-09-22
- Volume
- 313
- Issue
- 5794
- Pages
- 1781-1784
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2098022922
- Cited by
- 971
- References
- 31
- Citations by year
- 2026: 22 · 2025: 18 · 2024: 34 · 2023: 31 · 2022: 52 · 2021: 50 · 2020: 47 · 2019: 59 · 2018: 67 · 2017: 57 · 2016: 63 · 2015: 64 · 2014: 73 · 2013: 71 · 2012: 65
- FWCI
- 21.65
- Type
- journal article
- Language
- en
- Open access
- green
- infoscience.epfl.ch
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Wellcome Trust
- National Institute of Neurological Disorders and Stroke (R21NS045357, NS45357)
- National Center for Research Resources (RR-00 165, P51RR000165)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, Alzheimer's disease, brain extracts, protein aggregation, immunodepletion, immunization, host-pathogen interaction
- MeSH terms
- Aged, Aged, 80 and over, Aging, Alzheimer Disease, Amyloidosis, Animals, Brain, Brain Chemistry, Brain Diseases, Female, Hippocampus, Humans, Male, Mice, Transgenic, Protein Denaturation, Time Factors, Tissue Extracts, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Mice
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