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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APPNL-G-F/MAPT do not develop neurofibrillary tangles and neuronal loss until 24 months, and remain transcriptomically undercharacterized.
“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]
In “Humanization of Mapt gene in App KI mice” (page unavailable), the paper reports that APPNL-G-F/MAPT mice had no neurofibrillary tangles at 24 months, contrary to the claimed onset at that age. The “Propagation of AD brain-derived pathological tau proteins” section (page unavailable) also reports no neurodegeneration after pathological tau inoculation. The transcriptomic characterization statement follows the citation and is not attributed to this source. (LLM, conf=0.87)
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Experimental — accuracy not yet measuredMore physiological double knock-in models express humanized mutant APP and MAPT under endogenous promoters.
“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]
The Abstract describes crossing humanized MAPT knock-in mice with App knock-in mice to produce double knock-in mice. The Mutant mice section identifies mutations in the App mice, and the Discussion contrasts the knock-in approach with transgenic overexpression. Our copy does not establish that APP itself was humanized, so that part of the claim remains unsupported. (LLM, conf=0.82)
Experimental — accuracy not yet measuredHuman MAPT KI models exhibit delayed tau pathology, as does a cross between the two KI models.
“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
The Discussion (page unavailable) says the App/MAPT double-KI mice lacked apparent tauopathy and neurodegeneration despite amyloid pathology, and discusses the timing of subsequent pathological events. This is consistent with pathology developing slowly, but the paper does not demonstrate a delayed onset of tau pathology in either the single MAPT KI or double-KI mice. (LLM, conf=0.82)
Experimental — accuracy not yet measuredThe APPNL-G-F/MAPTP301S model provides an appealing alternative to the double APPNL-G-F × MAPT KI model, which develops both MAPT pathologies very slowly.
“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
In the Discussion (page unavailable), Saito et al. report that the App/MAPT double knock-in mice lacked apparent tauopathy and neurodegeneration despite substantial amyloid pathology. But the Humanization of Mapt gene in App KI mice section reports increased tau phosphorylation by six months; the paper does not establish that two MAPT pathologies both develop very slowly. The description of the citing authors’ model as an appealing alternative is their own assessment, not a finding attributed to Saito et al. (LLM, conf=0.82)
Experimental — accuracy not yet measuredExpressing physiological levels of tau transgene is overall benign and only produces pathology very late in life.
“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]
The Discussion says humanizing the murine Mapt gene has little effect on physiological or pathological measures in the mice studied, supporting the broadly benign characterization. But this is a knock-in model rather than a conventional tau transgene, and the paper does not establish that pathology arises only very late in life: the “Humanization of Mapt gene in App KI mice” section reports increased tau phosphorylation and plaque-associated dystrophic neurites at six months in mice also carrying an App mutation. (LLM, conf=0.87)
Experimental — accuracy not yet measured
WT tau is not generally amenable to form NFT.
“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]
The Abstract (page unavailable) reports that NFTs did not appear during the lifespan of the authors’ mouse models. The propagation section (page unavailable) also reports no NFT formation after inoculation with AD-derived pathological tau. These findings support difficulty inducing NFTs in the studied mice, but not the broader claim that wild-type tau generally cannot form them. (LLM, conf=0.84)
Experimental — accuracy not yet measured
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Self-citation
- 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
- 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
- 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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