The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation
Open accessAbstract
Despite the importance of the aberrant polymerization of Aβ in the early pathogenic cascade of Alzheimer's disease, little is known about the induction of Aβ aggregation in vivo. Here we show that induction of cerebral β-amyloidosis can be achieved in many different brain areas of APP23 transgenic mice through the injection of dilute Aβ-containing brain extracts. Once the amyloidogenic process has been exogenously induced, the nature of the induced Aβ-deposition is determined by the brain region of the host. Because these observations are reminiscent of a prion-like mechanism, we then investigated whether cerebral β-amyloidosis also can be induced by peripheral and systemic inoculations or by the intracerebral implantation of stainless steel wires previously coated with minute amounts of Aβ-containing brain extract. Results reveal that oral, intravenous, intraocular, and intranasal inoculations yielded no detectable induction of cerebral β-amyloidosis in APP23 transgenic mice. In contrast, transmission of cerebral β-amyloidosis through the Aβ-contaminated steel wires was demonstrated. Notably, plasma sterilization, but not boiling of the wires before implantation, prevented the induction of β-amyloidosis. Our results suggest that minute amounts of Aβ-containing brain material in direct contact with the CNS can induce cerebral β-amyloidosis, but that systemic cellular mechanisms of prion uptake and transport to the CNS may not apply to Aβ.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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 [52]
In the citing paper
“Experimentally, β-amyloid induction can be triggered in transgenic mice by intracerebrally implanted stainless steel wires coated with minute amounts of brain extract rich in aggregated Aβ52 (Fig 2).”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [52]
Citations
Cites
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-citationFolding proteins in fatal ways
Selkoe, D. J. (2003) · Nature · doi:10.1038/nature02264 · Cited by 1,432
A General Model of Prion Strains and Their Pathogenicity
Collinge, J., & Clarke, A. R. (2007) · Science · doi:10.1126/science.1138718 · Cited by 1,075
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
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Self-citationAlzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
Selkoe, D. J., & Schenk, D. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140248 · Cited by 829
Normal host prion protein necessary for scrapie-induced neurotoxicity
Brandner, S., Isenmann, S., Raeber, A. J., Fischer, M., Sailer, A. W., Kobayashi, Y., Marino, S., Weissmann, C., & Aguzzi, A. (1996) · Nature · doi:10.1038/379339a0 · Cited by 813
Self-citationPrusiner, S. B. (1991) · PubMed · Cited by 641
DANGER OF ACCIDENTAL PERSON-TO-PERSON TRANSMISSION OF CREUTZFELDT-JAKOB DISEASE BY SURGERY
Bernoulli, C., Siegfried, J., Baumgartner, G., Regli, F., Rabinowicz, T., Gajdusek, D. C., & Gibbs, C. J. (1977) · The Lancet · doi:10.1016/s0140-6736(77)91958-4 · Cited by 508
Neuron loss in APP transgenic mice
Calhoun, M. E., Wiederhold, K.-H., Abramowski, D., Phinney, A. L., Probst, A., Sturchler-Pierrat, C., Staufenbiel, M., Sommer, B., & Jucker, M. (1998) · Nature · doi:10.1038/27351 · Cited by 502
Self-citationLymphatic drainage of the brain and the pathophysiology of neurological disease
Weller, R. O., Djuanda, E., Yow, H.-Y., & Carare, R. O. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0457-0 · Cited by 488
Kane, 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-citationHerzig, M. C., Winkler, D. T., Burgermeister, P., Pfeifer, M., Kohler, E., Schmidt, S. D., Danner, S., Abramowski, D., Stürchler-Pierrat, C., Bürki, K., et al. (2004) · Nature Neuroscience · doi:10.1038/nn1302 · Cited by 391
Self-citationMolecular Mechanisms of Prion Pathogenesis
Aguzzi, A., Sigurdson, C. J., & Heikenwaelder, M. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.154326 · Cited by 366
Self-citationLundmark, K., Westermark, G. T., Olsén, A., & Westermark, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501814102 · Cited by 305
Amyloid-β Deposits Lead to Retinal Degeneration in a Mouse Model of Alzheimer Disease
Ning, A., Cui, J., To, E., Ashe, K. H., & Matsubara, J. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.08-1849 · Cited by 303
PrP-expressing tissue required for transfer of scrapie infectivity from spleen to brain
Blättler, T., Brandner, S., Raeber, A. J., Klein, M. A., Voigtländer, T., Weissmann, C., & Aguzzi, A. (1997) · Nature · doi:10.1038/37981 · Cited by 267
Self-citationNormal host prion protein (PrP C ) is required for scrapie spread within the central nervous system
Brandner, S., Raeber, A. J., Sailer, A. W., Blättler, T., Fischer, M., Weissmann, C., & Aguzzi, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.13148 · Cited by 252
Self-citationThe Development of Amyloid β Protein Deposits in the Aged Brain
Thal, D. R., Capetillo-Zarate, E., Del Tredici, K., & Braak, H. (2006) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2006.6.re1 · Cited by 234
Infectivity of Scrapie Prions Bound to a Stainless Steel Surface
Zobeley, E., Flechsig, E., Cozzio, A., Enari, M., & Weissmann, C. (1999) · Molecular Medicine · doi:10.1007/bf03402121 · Cited by 225
Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes
Legname, G., Nguyen, H.-O. B., Peretz, D., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608970103 · Cited by 219
Transmission of Scrapie by Steel-surface-bound Prions
Flechsig, E., Hegyi, I., Enari, M., Schwarz, P., Collinge, J., & Weissmann, C. (2001) · Molecular Medicine · doi:10.1007/bf03401958 · Cited by 199
Crossing the Species Barrier by PrPSc Replication In Vitro Generates Unique Infectious Prions
Castilla, J., Gonzalez-Romero, D., Saá, P., Morales, R., de Castro, J., & Soto, C. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.030 · Cited by 198
Prions and their lethal journey to the brain
Mabbott, N. A., & MacPherson, G. G. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1346 · Cited by 194
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
Invasion of Hematopoietic Cells into the Brain of Amyloid Precursor Protein Transgenic Mice
Stalder, A. K., Ermini, F., Bondolfi, L., Krenger, W., Burbach, G. J., Deller, T., Coomaraswamy, J., Staufenbiel, M., Landmann, R. M., & Jucker, M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2545-05.2005 · Cited by 185
Self-citationRapid Prion Neuroinvasion following Tongue Infection
Bartz, J. C., Kincaid, A. E., & Bessen, R. A. (2002) · Journal of Virology · doi:10.1128/jvi.77.1.583-591.2003 · Cited by 168
Induction of β(A4)-amyloid in primates by injection of Alzheimer’s disease brain homogenate
Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J., & Bruton, C. J. (1994) · Molecular Neurobiology · doi:10.1007/bf02778005 · Cited by 153
Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils
Johan, K., Westermark, G. T., Engström, U., Gustavsson, Å., Hultman, P. A., & Westermark, P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2558 · Cited by 147
Gibbs, C. J., Asher, D. M., Kobrine, A. I., Amyx, H. L., Sulima, M. P., & Gajdusek, D. C. (1994) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.57.6.757 · Cited by 124
Wadsworth, J. D. F., & Collinge, J. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.02.010 · Cited by 118
THE PUBLIC HEALTH IMPACT OF PRION DISEASES
Belay, E. D., & Schonberger, L. B. (2005) · Annual Review of Public Health · doi:10.1146/annurev.publhealth.26.021304.144536 · Cited by 116
McKintosh, E., Tabrizi, S. J., & Collinge, J. (2003) · Journal of NeuroVirology · doi:10.1080/13550280390194082 · Cited by 104
Koch’s postulates and infectious proteins
Walker, L. C., LeVine, H., & Jucker, M. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0072-x · Cited by 101
Self-citationYan, Z.-X., Stitz, L., Heeg, P., Pfaff, E., & Roth, K. (2004) · Infection Control and Hospital Epidemiology · doi:10.1086/502392 · Cited by 96
Self-citationWalker, L. C., LeVine, H., Mattson, M. P., & Jucker, M. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.06.010 · Cited by 90
Self-citationThe Nasal Cavity Is a Route for Prion Infection in Hamsters
Kincaid, A. E., & Bartz, J. C. (2007) · Journal of Virology · doi:10.1128/jvi.02649-06 · Cited by 81
Antiprion immunotherapy: to suppress or to stimulate?
Aguzzi, A., & Sigurdson, C. J. (2004) · Nature reviews. Immunology · doi:10.1038/nri1437 · Cited by 78
Self-citationTurner, M. L., & Ludlam, C. A. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07376.x · Cited by 76
Shimazawa, M., Inokuchi, Y., Okuno, T., Nakajima, Y., Sakaguchi, G., Kato, A., Oku, H., Sugiyama, T., Kudo, T., Ikeda, T., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05606.x · Cited by 65
Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils
Fu, X., Korenaga, T., Fu, L., Xing, Y., Guo, Z., Matsushita, T., Hosokawa, M., Naiki, H., Baba, S., Kawata, Y., et al. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00295-9 · Cited by 44
Infectious Alzheimer's disease?
Riek, R. (2006) · Nature · doi:10.1038/444429a · Cited by 34
Sbriccoli, M., Cardone, F., Valanzano, A., Lü, M., Graziano, S., Pascalis, A. D., Ingrosso, L., Zanusso, G., Monaco, S., Bentivoglio, M., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0474-z · Cited by 25
Reflections on amyloidosis in Papua New Guinea
Westermark, P., & Westermark, G. T. (2008) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.0073 · Cited by 16
Cited by
Sorted by citations
Alzheimer Disease: An Update on Pathobiology and Treatment Strategies
Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Goedert, M. (2015) · Science · doi:10.1126/science.1255555 · Cited by 1,028
Protein transmission in neurodegenerative disease
Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0333-7 · Cited by 625
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622
Self-citation
Metadata
- Authors
- Eisele, Y. S., Bolmont, T., Heikenwalder, M., Langer, F., Jacobson, L. H., Yan, Z.-X., Roth, K., Aguzzi, A., Staufenbiel, M., Walker, L. C., & Jucker, M.
- Affiliations
- Hertie Institute for Clinical Brain Research (DE)
- Department of Pathology, Institute for Neuropathology, University Hospital, Zürich, CH-8091 Switzerland;
- Novartis (Switzerland) (CH)
- SMP GmbH, D-72072 Tübingen, Germany;
- University Hospital Zurich (CH)
- Emory University (US)
- German Center for Neurodegenerative Diseases (DE)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-08-04
- Volume
- 106
- Issue
- 31
- Pages
- 12926-12931
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2722323
- OpenAlex
- W1928837524
- Cited by
- 279
- References
- 44
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 14 · 2023: 6 · 2022: 10 · 2021: 15 · 2020: 22 · 2019: 17 · 2018: 18 · 2017: 18 · 2016: 21 · 2015: 21 · 2014: 20 · 2013: 28 · 2012: 17
- FWCI
- 12.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Funders
- 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
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- beta-amyloidosis, Alzheimer's disease, amyloid-beta aggregation, APP23 transgenic mice, intracerebral injection, prion-like transmission, plasma sterilization, brain region specificity, amyloid deposition
- MeSH terms
- Amyloidosis, Animals, Brain Diseases, Female, Male, Mice, Inbred C57BL, Mice, Transgenic, Amyloid beta-Peptides, Prion Diseases, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
