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Humanization of the entire murine Mapt gene provides a murine model of pathological human tau propagation
Open accessAbstract
In cortical regions of brains from individuals with preclinical or clinical Alzheimer's disease (AD), extracellular β-amyloid (Aβ) deposition precedes the aggregation of pathological intracellular tau (the product of the gene microtubule-associated protein tau (MAPT)). To our knowledge, current mouse models of tauopathy reconstitute tau pathology by overexpressing mutant human tau protein. Here, through a homologous recombination approach that replaced the entire murine Mapt gene with the human ortholog, we developed knock-in mice with humanized Mapt to create an in vivo platform for studying human tauopathy. Of note, the humanized Mapt expressed all six tau isoforms present in humans. We next cross-bred the MAPT knock-in mice with single amyloid precursor protein (App) knock-in mice to investigate the Aβ–tau axis in AD etiology. The double-knock-in mice exhibited higher tau phosphorylation than did single MAPT knock-in mice but initially lacked apparent tauopathy and neurodegeneration, as observed in the single App knock-in mice. We further observed that tau humanization significantly accelerates cell-to-cell propagation of AD brain-derived pathological tau both in the absence and presence of Aβ-amyloidosis. In the presence of Aβ-amyloidosis, tau accumulation was intensified and closely associated with dystrophic neurites, consistently showing that Aβ-amyloidosis affects tau pathology. Our results also indicated that the pathological human tau interacts better with human tau than with murine tau, suggesting species-specific differences between these orthologous pathogenic proteins. We propose that the MAPT knock-in mice will make it feasible to investigate the behaviors and characteristics of human tau in an animal model.
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“However, APPNL‐G‐F/MAPT do not develop neurofibrillary tangles and neuronal loss until 24 months, 73 and remain transcriptomically undercharacterized.”
From Unique transcriptomic alterations in 5XFAD;PS19 mouse model identify glial lipid dysregulation and coordinated microglial–oligodendrocyte responses (2026) · cites this paper as [73]
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“More physiological double knock‐in models express humanized mutant APP and MAPT under endogenous promoters. 73 , 74”
From Unique transcriptomic alterations in 5XFAD;PS19 mouse model identify glial lipid dysregulation and coordinated microglial–oligodendrocyte responses (2026) · cites this paper as [73]
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“Human MAPT KI models exhibit delayed tau pathology, as does a cross between the two KI models (Saito et al., 2019; Islam et al., 2023).”
From β-amyloid accumulation enhances microtubule associated protein tau pathology in an APPNL-G-F/MAPTP301S mouse model of Alzheimer’s disease (2024) · cites this paper as Saito et al., 2019
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“Our results show that this model provides an appealing alternative to the double APPNL-G-F × MAPT KI model, which develop both MAPT pathologies very slowly (Saito et al., 2019).”
From β-amyloid accumulation enhances microtubule associated protein tau pathology in an APPNL-G-F/MAPTP301S mouse model of Alzheimer’s disease (2024) · cites this paper as Saito et al., 2019
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“Since expressing physiological levels of tau transgene has been shown to be overall benign and only produces pathology very late in life (37, 38), our reasoning could be justified as this was a comparative neuropathologic study of three different variants of tau, all of which had equivalent expression levels.”
From Combinatorial model of amyloid β and tau reveals synergy between amyloid deposits and tangle formation (2022) · cites this paper as [38]
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“As shown by other groups (37, 38), WT tau is not generally amenable to form NFT.”
From Combinatorial model of amyloid β and tau reveals synergy between amyloid deposits and tangle formation (2022) · cites this paper as [38]
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“The hTau-KI human MAPT knock-in mouse model lacks apparent tau pathology, but has been shown to enhance tau propagation with exposure to AD-derived tau aggregates (Hashimoto, Matsuba et al. 2019, Saito, Mihira et al. 2019).”
From SORLA up-regulation suppresses pathological effects in aged tauopathy mouse brain (2026) · cites this paper as Saito, Mihira et al. 2019
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Self-citation
Metadata
- Authors
- Saito, T., Mihira, N., Matsuba, Y., Sasaguri, H., Hashimoto, S., Narasimhan, S., Zhang, B., Murayama, S., Higuchi, M., Lee, V. M. Y., Trojanowski, J. Q., & Saido, T. C.
- Affiliations
- RIKEN Center for Brain Science (JP)
- University of Pennsylvania (US)
- Tokyo Metropolitan Geriatric Hospital (JP)
- National Institutes for Quantum Science and Technology (JP)
- Corresponding author
- Saito, Takashi
- Saido, Takaomi C.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-08
- Volume
- 294
- Issue
- 34
- Pages
- 12754-12765
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6709628
- OpenAlex
- W2954476098
- Cited by
- 248
- References
- 44
- Citations by year
- 2026: 24 · 2025: 48 · 2024: 52 · 2023: 30 · 2022: 31 · 2021: 34 · 2020: 21 · 2019: 7
- FWCI
- 16.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by-nc-nd)
- QST-Repository (National Institutes for Quantum and Radiological Science and Technology) (submittedVersion, cc-by-nc-nd)
- Funders
- MEXT | Japan Society for the Promotion of Science (JSPS) (26290019, JP16H06277)
- JST | Precursory Research for Embryonic Science and Technology (PRESTO) (110650)
- Japan Agency for Medical Research and Development (AMED) (JP18dm027001)
- HHS | National Institutes of Health (NIH) (AG10124, AG 17586)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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
- tauopathy, Alzheimer's disease, amyloid-beta, tau phosphorylation, dystrophic neurites, tau isoforms, amyloid precursor protein
- MeSH terms
- Animals, Disease Models, Animal, Humans, Mice, Inbred C57BL, Mice, Transgenic, tau Proteins, Mice
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