Unique pathological tau conformers from Alzheimer’s brains transmit tau pathology in nontransgenic mice
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Filamentous tau aggregates are hallmark lesions in numerous neurodegenerative diseases, including Alzheimer’s disease (AD). Cell culture and animal studies showed that tau fibrils can undergo cell-to-cell transmission and seed aggregation of soluble tau, but this phenomenon was only robustly demonstrated in models overexpressing tau. In this study, we found that intracerebral inoculation of tau fibrils purified from AD brains (AD-tau), but not synthetic tau fibrils, resulted in the formation of abundant tau inclusions in anatomically connected brain regions in nontransgenic mice. Recombinant human tau seeded by AD-tau revealed unique conformational features that are distinct from synthetic tau fibrils, which could underlie the differential potency in seeding physiological levels of tau to aggregate. Therefore, our study establishes a mouse model of sporadic tauopathies and points to important differences between tau fibrils that are generated artificially and authentic ones that develop in AD brains.
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Methanol fixation has previously been used to remove soluble proteins, including tau.
“Methanol fixation has previously been used to remove soluble proteins, including tau (20, 46).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [46]
The Immunocytochemistry methods state that neurons were fixed with methanol to remove soluble tau. This supports the tau example, but the passage does not say that methanol fixation was used to remove soluble proteins more generally. (LLM, conf=0.83)
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“Models based on seeding tau pathology with exogenous material sometimes use recombinant tau fibrils, but human tauon strains are best replicated by utilizing genuine brain homogenates from human disease (Guo et al., 2016).”
BackgroundMethodCytosolic antibody receptor TRIM21 is required for effective tau immunotherapy in mouse models
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“Methanol fixation has previously been used to remove soluble proteins, including tau (20, 46).”
All (animal) models (of neurodegeneration) are wrong. Are they also useful?
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Alzheimer’s disease brain contains tau fractions with differential prion-like activities
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- Authors
- Guo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., & Lee, V. M. Y.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Lee, Virginia M.Y.
- ORCID
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2016-10-17
- Volume
- 213
- Issue
- 12
- Pages
- 2635-2654
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC5110027
- OpenAlex
- W2534587007
- Cited by
- 440
- References
- 60
- Citations by year
- 2026: 30 · 2025: 35 · 2024: 53 · 2023: 50 · 2022: 47 · 2021: 62 · 2020: 57 · 2019: 45 · 2018: 40 · 2017: 20 · 2013: 1
- FWCI
- 28.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AG10124, AG17586)
- CurePSP
- BrightFocus Foundation (A2014005F)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- tau pathology, Alzheimer's disease, tau fibrils, cell-to-cell transmission, intracerebral injection, tau inclusions
- MeSH terms
- Aging, Alzheimer Disease, Animals, Brain, Heparin, Mice, Inbred C57BL, Mice, Transgenic, Neurons, Phosphorylation, Protein Conformation, Tissue Extracts, Neurofibrillary Tangles, tau Proteins, Protein Isoforms, Tauopathies, Protein Aggregates
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