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Tau Filament Formation in Transgenic Mice Expressing P301L Tau
Open accessAbstract
Mutations in the microtubule-associated protein tau, including P301L, are genetically coupled to hereditary frontotemporal dementia with parkinsonism linked to chromosome 17. To determine whether P301L is associated with fibril formation in mice, we expressed the longest human tau isoform, human tau40, with this mutation in transgenic mice by using the neuron-specific mouse Thy1.2 promoter. We obtained mice with high expression of human P301L tau in cortical and hippocampal neurons. Accumulated tau was hyperphosphorylated and translocated from axonal to somatodendritic compartments and was accompanied by astrocytosis and neuronal apoptosis indicated by terminal deoxynucleotidyl transferase-mediated biotinylated dUTP nick end-labeling staining. Moreover, P301L tau formed abnormal filaments. Electron microscopy of sarcosyl-insoluble protein extracts established that the filaments had a straight or twisted structure of variable length and were approximately 15 nm wide. Immunoelcecton microscopy showed that the tau filaments were phosphorylated at the TG3, AT100, AT8, and AD199 epitopes in vivo. In cortex, brain stem, and spinal cord, neurofibrillary tangles were also identified by thioflavin-S fluorescent microscopy and Gallyas silver stains. Together, our results show that expression of the P301L mutation in mice causes neuronal lesions that are similar to those seen in human tauopathies.
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“transgenic mice expressing human mutated tau showed NFT formation and neuronal loss, implying a causal relationship between tau over-expression and neurodegeneration (8 -11).”
From CREB-activity and nmnat2 transcription are down-regulated prior to neurodegeneration, while NMNAT2 over-expression is neuroprotective, in a mouse model of human tauopathy (2012) · cites this paper as [8]
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“Genetic studies show that the development of neurodegenerative tauopathies is associated with missense mutations in the microtubule-associated tau protein (MAPT) [26].”
From Diffusion tensor imaging reveals whole-brain microstructural changes in the P301L mouse model of tauopathy. (2020) · cites this paper as [26]
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“Both mouse models are known to demonstrate a proinflammatory phenotype (17, 18).”
From The Transcriptional Landscape of Microglial Genes in Aging and Neurodegenerative Disease (2019) · cites this paper as [17]
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Lewis, J., McGowan, E., Rockwood, J., Melrose, H., Nacharaju, P., Van Slegtenhorst, M., Gwinn-Hardy, K., Murphy, M. P., Baker, M., Yu, X., et al. (2000) · Nature Genetics · doi:10.1038/78078 · Cited by 1,371
Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122
Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease.
Delacourte, A., David, J. P., Sergeant, N., Buée, L., Wattez, A., Vermersch, P., Ghozali, F., Fallet-Bianco, C., Pasquier, F., Lebert, F., et al. (1999) · Neurology · doi:10.1212/wnl.52.6.1158 · Cited by 828
Structural characterization of the core of the paired helical filament of Alzheimer disease.
Wischik, C. M., Novák, M., Edwards, P. C., Klug, A., Tichelaar, W., & Crowther, R. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4884 · Cited by 609
Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M. K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)81127-7 · Cited by 564
Götz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441
Self-citationSpittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M. H., Sciot, R., Lommel, A. V., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 390
Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
Probst, A., Götz, J., Wiederhold, K., Tolnay, M., Mistl, C., Jaton, A., Hong, M., Ishihara, T., Lee, V., Trojanowski, J., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010051148 · Cited by 362
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- Gallyas, 1971, Acta Morphol. Acad. Sci. Hung., 19, 1
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Gorzek, R. C., Joly‐Amado, A., Hurst-Calle, N., Gabrielson, G. L., Miller, M., Osting, S., Nash, K. R., & Bürger, C. (2025) · Cells · doi:10.3390/cells14161238 · Cited by 2
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Lövestam, S., Shimozawa, A., Tarutani, A., Ohtani, R., Masuda‐Suzukake, M., Hasegawa, K., Robinson, A., Saito, Y., Murayama, S., Yoshida, M., et al. (2026) · Nature · doi:10.1038/s41586-026-11061-x · Cited by 4
A novel tauopathy model mimicking molecular and spatial aspects of human tau pathology
Yanai, R., Mitani, T. T., Susaki, E. A., Minamihisamatsu, T., Shimojo, M., Saito, Y., Mizuma, H., Nitta, N., Kaneda, D., Hashizume, Y., et al. (2024) · Brain Communications · doi:10.1093/braincomms/fcae326 · Cited by 2
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Janus, C., & Welzl, H. (2016) · Springer eBooks · doi:10.1007/978-1-4939-3777-6_6 · Cited by 2
Köhler, C. N., Fuhr, V., & Dinekov, M. (2017) · Brain Research · doi:10.1016/j.brainres.2017.08.029 · Cited by 2
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Lewis, J. M., & Hutton, M. L. (2005) · Humana Press eBooks · doi:10.1385/1-59259-834-x:065 · Cited by 2
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Mitra, S., Pandey, S., Gill, A., Roy, A., Dutta, S., Kumar, A., Ali, M., & Chawla, G. (2025) · Academia Biology · doi:10.20935/acadbiol7909 · Cited by 2
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Rudy, C. C. (2014) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.620 · Cited by 1
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.16.464454 · Cited by 1
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Rossi, D. P. (2013) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · Cited by 1
Yassine, N. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique)
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Ashe, K. H. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch11
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Brion, J. (2008) · Handbook of clinical neurology · doi:10.1016/s0072-9752(07)01241-9
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Duan, X., & Y., G. (2002) · Hong Kong journal of psychiatry
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Goedert, M., & Spillantini, M. G. (2007) · Blue books of neurology · doi:10.1016/s1877-184x(09)70055-3
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Duff, K., Krishnamurthy, P., Planel, E., & Hutton, M. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_13
Korenova, M., & Stožická, Z. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9378-2
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Lei, H.-Y., Pi, G.-L., He, T., Xiong, R., Lv, J.-R., Liu, J.-L., Wu, D.-Q., Li, M.-Z., Shi, K., Li, S.-H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25378030
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Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555693
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555714
Schweighauser, M., Murzin, A. G., Macdonald, J. A., Lavenir, I., Crowther, R. A., Scheres, S. H. W., & Goedert, M. (2023) · Figshare · doi:10.6084/m9.figshare.24257490
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555717
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555687
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555690
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555702
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555681
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555672
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555708
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555675
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555678
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555699
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555723
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555705
Kim, D. W., Tu, K. J., Wei, A., Lau, A., Gonzalez-Gil, A., Cao, T., Braunstein, K. E., Ling, J. P., Troncoso, J. C., Wong, P. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26555711
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Metadata
- Authors
- Götz, J., Chen, F., Barmettler, R., & Nitsch, R. M.
- Affiliations
- University of Zurich (CH)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 276
- Issue
- 1
- Pages
- 529-534
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2035156043
- Cited by
- 495
- References
- 26
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 29 · 2023: 13 · 2022: 20 · 2021: 18 · 2020: 16 · 2019: 17 · 2018: 9 · 2017: 16 · 2016: 10 · 2015: 11 · 2014: 15 · 2013: 22 · 2012: 18
- FWCI
- 18.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- transgenic mice, tau hyperphosphorylation, neurofibrillary tangles, tauopathy, neuronal apoptosis, astrocyte activation
- MeSH terms
- Animals, Brain, Gliosis, Humans, Immunohistochemistry, Mice, Transgenic, Actin Cytoskeleton, Microscopy, Electron, Microscopy, Fluorescence, Mutation, Organ Specificity, Phosphorylation, Protein Conformation, Immunoblotting, Gene Expression, Neurofibrillary Tangles, tau Proteins, Apoptosis, Amino Acid Substitution, Protein Isoforms, In Situ Nick-End Labeling, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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