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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Proteopathic tau seeds are capable of entering a cell and promoting aggregation in a prion-like manner.
“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
In the supplied passage labeled Abstract (page unavailable), the paper reports that insoluble tau induces aggregation and compares the spreading of tau pathology to prions. It does not establish that tau seeds enter cells: it presents entry as one possible mechanism and induction from outside cells as another. (LLM, conf=0.90)
Experimental — accuracy not yet measuredInoculation of mice with tauopathy homogenates produces local pathology that spreads beyond the injection site.
“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
The paper reports that brain extract from P301S tau mice induced pathology that spread beyond the injection site in transgenic mice expressing human wild-type tau. It also reports that pathology in non-transgenic mice remained confined to the injection site, so the claim needs that qualification. (LLM, conf=0.86)
Experimental — accuracy not yet measuredTau aggregates can transfer and propagate/spread within synaptic circuits.
“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
The paper reports experimental transmission of tau pathology and its spread to anatomically connected brain regions after injection of tau-containing extract (Abstract; page unavailable). It does not establish that tau aggregates transfer through synapses or propagate specifically within synaptic circuits; the mechanism of cell-to-cell spread is presented as a question for further investigation. (LLM, conf=0.87)
Experimental — accuracy not yet measuredWe are unable to explain how Aβ peptides, despite being part of the amyloid cascade, may participate in the neuron-to-neuron propagation of Tau pathology.
“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]
The discussion of spreading in the supplied copy (labelled Abstract; page unavailable) says the mechanism by which tau aggregates induce intracellular pathology remains to be investigated. It also reports that extracellular β-amyloid aggregates potentiated tau pathology in mutant-tau mice, but not wild-type-tau mice. It does not establish that Aβ peptides participate in neuron-to-neuron propagation of tau pathology or discuss their role in the amyloid cascade. (LLM, conf=0.82)
Experimental — accuracy not yet measuredAccording to the amyloid cascade hypothesis, Aβ peptides are neurotoxic and are supposed to lead to or accentuate neuron-to-neuron propagation of Tau pathology, leading to neuronal death, by a still unknown mechanism.
“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]
The discussion passage labeled Abstract (page unavailable) reports that extracellular β-amyloid aggregates potentiated tau pathology in mice expressing mutant human tau, but that no such effect was observed in mice expressing wild-type human tau. The paper also describes spreading tau pathology, but does not establish that Aβ drives neuron-to-neuron propagation or that this Aβ-related process leads to neuronal death; it reports no obvious neurodegeneration in the recipient mice. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Tau propagates pathology among neurons.
“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
The failure of candidate drugs to show improvements in the human condition has caused a shift in interest to other therapeutic pathways.
“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
The paper’s account of its findings describes transmission and spreading of tau pathology in mice, not outcomes of candidate drugs in humans. A search of our copy for failed drugs, clinical improvement, and a shift in therapeutic approaches found no passage addressing that claim. (LLM, conf=0.77)
Experimental — accuracy not yet measuredIncreasing evidence suggests the transmission of tau pathology is mediated by the release, uptake, and trafficking of pathogenic or misfolded tau aggregates within synaptically connected neurons.
“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]
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 induce pathological tau spreading at sites distal to the injection site.
“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]
Transfer of abnormal misfolded proteins, including tau and Aβ, has a common feature of pathological propagation between cells.
“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]
Pathogenic tau can be released from diseased neurons, taken up by previously unaffected normal neurons, and induce pathogenic tau production in normal neurons.
“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]
A prior study reported that brain extracts from NFT-bearing mouse brain injected into wild-type tau expressing mice induce seeding of tau fibrils in neurons.
“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 living mouse brain, intracortical injections of tau aggregates seed tau fibrillization in neurons carrying the human transgene.
“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
Neurofibrillary (tau) tangles can be exogenously induced by the intracerebral infusion of brain extract containing abnormal tau filaments into mice bearing a human tau transgene.
“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]
The current clinical trial literature is compatible with the idea that AβP-related substances kindle a self-propagating process related to neocortical NFTs.
“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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- 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
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › 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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