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Transmission and spreading of tauopathy in transgenic mouse brain
Open accessAbstract
Hyperphosphorylated tau makes up the filamentous intracellular inclusions of several neurodegenerative diseases, including Alzheimer's disease. In the disease process, neuronal tau inclusions first appear in the transentorhinal cortex from where they seem to spread to the hippocampal formation and neocortex. Cognitive impairment becomes manifest when inclusions reach the hippocampus, with abundant neocortical tau inclusions and extracellular beta-amyloid deposits being the defining pathological hallmarks of Alzheimer's disease. An abundance of tau inclusions, in the absence of beta-amyloid deposits, defines Pick's disease, progressive supranuclear palsy, corticobasal degeneration and other diseases. Tau mutations cause familial forms of frontotemporal dementia, establishing that tau protein dysfunction is sufficient to cause neurodegeneration and dementia. Thus, transgenic mice expressing mutant (for example, P301S) human tau in nerve cells show the essential features of tauopathies, including neurodegeneration and abundant filaments made of hyperphosphorylated tau protein. By contrast, mouse lines expressing single isoforms of wild-type human tau do not produce tau filaments or show neurodegeneration. Here we have used tau-expressing lines to investigate whether experimental tauopathy can be transmitted. We show that injection of brain extract from mutant P301S tau-expressing mice into the brain of transgenic wild-type tau-expressing animals induces assembly of wild-type human tau into filaments and spreading of pathology from the site of injection to neighbouring brain regions.
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In the citing paper
“The pathogenic tau can be released from diseased neurons, then uptake by previously unaffected normal neurons, inducing pathogenic tau production in normal neurons.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [42]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Proteopathic tau seeds are capable of entering a cell and promoting aggregation in a prion-like manner (Clavaguera et al., 2009; Frost et al., 2009).”
From Network analysis identifies strain-dependent response to tau and tau seeding-associated genes (2023) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“inoculation of mice with tauopathy homogenates produces local pathology that spreads beyond the injection site (Clavaguera et al., 2009).”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“This may be important as we know that tau aggregates can transfer and propagate/spread within synaptic circuits (Clavaguera et al., 2009, de Calignon et al., 2012).”
From In vivo imaging of tau pathology using multi-parametric quantitative MRI (2015) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“We are thus unable to explain how Aβ peptides—despite being a part of the amyloid cascade—may participate in the neuron-to-neuron propagation of Tau pathology [20].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [20]
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“According to the amyloid cascade hypothesis, Aβ peptides are neurotoxic and supposed to lead to or accentuate neuron-to-neuron propagation of Tau pathology—leading to neuronal death—by a still unknown mechanism [20].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [20]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
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“Several lines of evidence indicate tau propagates pathology among neurons.”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Clavaguera et al., 2009
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In the citing paper
“The failure of these candidate drugs to date to show any improvements in the human condition has caused a shift in interest to other therapeutic pathways (Clavaguera et al., 2009).”
From In vivo imaging of tau pathology using multi-parametric quantitative MRI (2015) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredIn the citing paper
“Increasing evidence suggests the transmission of tau pathology is mediated by the release, uptake, and trafficking of pathogenic or misfolded tau aggregates within synaptically connected neurons9,10.”
From Tau Internalization is Regulated by 6-O Sulfation on Heparan Sulfate Proteoglycans (HSPGs) (2018) · cites this paper as [9]
In the citing paper
“seeded synthetic tau fibrils, or brain extracts from tau transgenic mice or human patients with tauopathy injected into the brain of tau transgenic or WT mice was found to induce pathological tau spreading at sites distal to the injection site [232–235].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [232]
In the citing paper
“The transfer of abnormal misfolded proteins, including tau and Aβ, has a common feature of the pathological propagation between cells [42, 56].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [42]
In the citing paper
“Another recent study reported that brain extracts from NFT-bearing mouse brain injected in wild-type tau expressing mice induces seeding of tau fibrils in neurons (Clavaguera et al., 2009).”
From Propagation of Tau Pathology in a Model of Early Alzheimer's Disease (2012) · cites this paper as Clavaguera et al., 2009
In the citing paper
“In living mouse brain, intracortical injections of tau aggregates seed tau fibrillization in neurons carrying the human transgene (Clavaguera et al., 2009).”
From Propagation of Tau Pathology in a Model of Early Alzheimer's Disease (2012) · cites this paper as Clavaguera et al., 2009
In the citing paper
“Using a paradigm similar to in vivo Aβ-seeding, neurofibrillary (tau) tangles can be exogenously induced by the intracerebral infusion of brain extract containing abnormal tau filaments into mice bearing a human tau transgene63.”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [63]
In the citing paper
“The current clinical trial literature is compatible with the idea that AβP-related substances kindle a self-propagating process related to neocortical NFTs, as has been hypothesized (266-269).”
From Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature (2012) · cites this paper as [268]
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Metadata
- Authors
- Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., Jucker, M., Goedert, M., & Tolnay, M.
- Affiliations
- University of Basel (CH)
- Hertie Institute for Clinical Brain Research (DE)
- MRC Laboratory of Molecular Biology (GB)
- University Hospital of Basel (CH)
- Novartis (Switzerland) (CH)
- Corresponding author
- Goedert, Michel
- Tolnay, Markus
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2009-06-07
- Volume
- 11
- Issue
- 7
- Pages
- 909-913
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC2726961
- OpenAlex
- W2099340107
- Cited by
- 1,803
- References
- 36
- Citations by year
- 2026: 76 · 2025: 85 · 2024: 96 · 2023: 94 · 2022: 114 · 2021: 130 · 2020: 135 · 2019: 128 · 2018: 115 · 2017: 105 · 2016: 113 · 2015: 121 · 2014: 107 · 2013: 122 · 2012: 98
- FWCI
- 56.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (120261)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- tauopathy, tau protein, hyperphosphorylated tau, transgenic mice, Alzheimer's disease, Pick's disease, progressive supranuclear palsy, corticobasal degeneration, frontotemporal dementia, neurodegeneration, transentorhinal cortex, hippocampus
- MeSH terms
- Animals, Brain, Humans, Immunohistochemistry, Mice, Transgenic, Blotting, Western, tau Proteins, Tauopathies, Mice
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