Lack of Tau Proteins Rescues Neuronal Cell Death and Decreases Amyloidogenic Processing of APP in APP/PS1 Mice
Open accessAbstract
Lack of tau expression has been reported to protect against excitotoxicity and to prevent memory deficits in mice expressing mutant amyloid precursor protein (APP) identified in familial Alzheimer disease. In APP mice, mutant presenilin 1 (PS1) enhances generation of Aβ42 and inhibits cell survival pathways. It is unknown whether the deficient phenotype induced by concomitant expression of mutant PS1 is rescued by absence of tau. In this study, we have analyzed the effect of tau deletion in mice expressing mutant APP and PS1. Although APP/PS1/tau(+/+) mice had a reduced survival, developed spatial memory deficits at 6 months and motor impairments at 12 months, these deficits were rescued in APP/PS1/tau(-/-) mice. Neuronal loss and synaptic loss in APP/PS1/tau(+/+) mice were rescued in the APP/PS1/tau(-/-) mice. The amyloid plaque burden was decreased by roughly 50% in the cortex and the spinal cord of the APP/PS1/tau(-/-) mice. The levels of soluble and insoluble Aβ40 and Aβ42, and the Aβ42/Aβ40 ratio were reduced in APP/PS1/tau(-/-) mice. Levels of phosphorylated APP, of β-C-terminal fragments (CTFs), and of β-secretase 1 (BACE1) were also reduced, suggesting that β-secretase cleavage of APP was reduced in APP/PS1/tau(-/-) mice. Our results indicate that tau deletion had a protective effect against amyloid induced toxicity even in the presence of mutant PS1 and reduced the production of Aβ.
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In AD models, absence of tau rescues behavioral impairments and reduces neurotoxicity despite no significant changes in Aβ levels.
“For example, in AD models, the absence of tau has been shown to rescue behavioral impairments and reduce neurotoxicity, despite no significant changes in Aβ levels [75–79].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [79]
The Abstract reports that tau deletion rescued memory and motor impairments, neuronal loss, and synaptic loss in APP/PS1 mice. But it also reports reduced soluble and insoluble Aβ40 and Aβ42; the Discussion describes an approximately 50% decrease in amyloid burden. Thus this paper does not support the claim that these benefits occurred without significant changes in Aβ levels. (LLM, conf=0.91)
Experimental — accuracy not yet measuredIn 5xFAD mice lacking endogenous Tau, motor and working memory deficits are rescued, as well as neuron numbers in the Ammon's horn of the hippocampus.
“In good agreement, motor and working memory deficits are rescued in 5xFAD mice lacking endogenous Tau (5xFAD/Tau−/−), as well as neuron numbers in the Ammon’s horn of the hippocampus [85].”
From Neuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models (2020) · cites this paper as [85]
In multiple mouse disease models, tau ablation is associated with protective effects.
“Interestingly, in multiple mouse disease models, tau ablation has been associated with protective effects.”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [79]
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 [53]
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- Roberson ED, Halabisky B, Yoo JW, Yao J, Chin J, Yan F, Wu T, Hamto P, Devidze N, Yu GQ, Palop JJ, Noebels JL, Mucke L: Amy- loid-{beta}/Fyn-induced synaptic. Network, and cognitive impair- ments depend on tau levels in multiple mousemodels of Alzheimer's disease, J Neurosci 2011, 31:700 -711
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- Authors
- Leroy, K., Ando, K., Laporte, V., Dedecker, R., Suain, V., Authelet, M., Héraud, C., Pierrot, N., Yilmaz, Z., Octave, J.-N., & Brion, J.-P.
- Affiliations
- Université Libre de Bruxelles (BE)
- UCLouvain (BE)
- Corresponding author
- Brion, Jean-Pierre
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 2012-12
- Volume
- 181
- Issue
- 6
- Pages
- 1928-1940
- ISSN
- 0002-9440 (ISSN-L)
- OpenAlex
- W2053460912
- Cited by
- 161
- References
- 49
- Citations by year
- 2026: 6 · 2025: 17 · 2024: 19 · 2023: 12 · 2022: 6 · 2021: 8 · 2020: 23 · 2019: 13 · 2018: 9 · 2017: 12 · 2016: 9 · 2015: 10 · 2014: 9 · 2013: 8
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed (publishedVersion)
- Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles) (submittedVersion)
- Digital Access to Libraries (submittedVersion, other-oa)
- Funders
- Northwestern University
- Institut National de la Santé et de la Recherche Médicale
- Universiteit Antwerpen
- 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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, APP/PS1 mice, familial Alzheimer's disease, amyloid precursor protein, presenilin 1, amyloid-beta, Aβ42/Aβ40 ratio, neuronal cell death, synaptic loss, spatial memory impairment, motor impairment, amyloid plaques, beta-secretase, BACE1, APP phosphorylation
- MeSH terms
- Animals, Humans, Memory, Short-Term, Mice, Transgenic, Motor Activity, Neuroglia, Neurons, Phosphorylation, Phosphothreonine, Protein Processing, Post-Translational, Solubility, Synapses, Survival Analysis, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, tau Proteins, Cell Death, Dendritic Spines, Mice, Presenilin-1, Amyloid Precursor Protein Secretases, Plaque, Amyloid
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