Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport
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A mechanism for the protective effects of tau reduction in mouse models of Alzheimer’s disease.
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Deletion of the tau gene fails to induce problems in axonal transport, suggesting that other proteins associated with microtubule binding or regulation may compensate for tau.
“However, deletion of the tau gene fails to induce problems in axonal transport, suggesting that other proteins associated with microtubule binding or regulation, such as MAP1 and MAP2 may compensate for tau [127].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [127]
Data from cell and animal models show that tau is a mediator of Aβ-induced toxicity.
“Data from cell and animal models show that tau is also a mediator of Aβ-induced toxicity46–48.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [47]
Some data suggest that Aβ toxicity is partially mediated through tau, as tau knockout mice are protected against Aβ-induced insults including cognitive effects, seizures, survival, axonal transport, and DNA double-stranded breaks.
“Some data suggest that Aβ toxicity is partially mediated through tau (50–52) as the tau knockout mouse has proven to be protected against a growing number of Aβ-induced insults, including those affecting cognition (50, 53), seizures (14, 50, 51, 54, 55), survival (50, 51, 54), axonal transport (52), and double-stranded breaks in DNA (55).”
From Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy (2017) · cites this paper as [52]
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- Authors
- Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L.
- Affiliations
- Gladstone Institutes (US)
- Stanford University (US)
- Corresponding author
- Vossel, Keith A.
- Mucke, Lennart
- ORCID
- Venue
- Science
- Published
- 2010-10-08
- Volume
- 330
- Issue
- 6001
- Pages
- 198-198
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3024010
- OpenAlex
- W2030602441
- Cited by
- 486
- References
- 12
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 17 · 2023: 26 · 2022: 21 · 2021: 24 · 2020: 31 · 2019: 32 · 2018: 33 · 2017: 30 · 2016: 42 · 2015: 33 · 2014: 46 · 2013: 36 · 2012: 46
- FWCI
- 27.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1c06rr018928-01)
- National Institute on Aging (AG011385, R37AG011385, R01AG011385)
- National Institute of Neurological Disorders and Stroke (K99NS057906, R01NS041787, R00NS057906, NS041787, NS057906)
- National Center for Research Resources (C06-RR-018928)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, tau protein, axonal transport, Alzheimer's disease, mitochondrial transport, TrkA, neurotrophin receptors, amyloid-beta oligomers
- MeSH terms
- Animals, Axonal Transport, Cells, Cultured, Hippocampus, Mitochondria, Neurons, Peptide Fragments, Amyloid beta-Peptides, tau Proteins, Receptor, trkA, Mice
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