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Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice.
Open accessAbstract
Altered autophagy contributes to the pathogenesis of Alzheimer's disease and other tauopathies, for which curative treatment options are still lacking. We have recently shown that trehalose reduces tau pathology in a tauopathy mouse model by stimulation of autophagy. Here, we studied the effect of the autophagy inducing drug rapamycin on the progression of tau pathology in P301S mutant tau transgenic mice. Rapamycin treatment resulted in a significant reduction in cortical tau tangles, less tau hyperphosphorylation, and lowered levels of insoluble tau in the forebrain. The favourable effect of rapamycin on tau pathology was paralleled by a qualitative reduction in astrogliosis. These effects were visible with early preventive or late treatment. We further noted an accumulation of the autophagy associated proteins p62 and LC3 in aged tangle bearing P301S mice that was lowered upon rapamycin treatment. Thus, rapamycin treatment defers the progression of tau pathology in a tauopathy animal model and autophagy stimulation may constitute a therapeutic approach for patients suffering from tauopathies.
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“Rapamycin treatment inhibits both tau hyperphosphorylation (Liu et al., 2013; Ozcelik et al., 2013; Tramutola et al., 2017) and the development of status epilepticus and chronic epilepsy in models of pharmacological seizure induction (Zeng et al., 2008; Huang et al., 2010), TLE (Drion et al., 2016), and PTE (Guo et al., 2013; Butler et al., 2015).”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Ozcelik et al., 2013
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
West, M. J., Slomianka, L., & Gundersen, H. J. G. (1991) · The Anatomical Record · doi:10.1002/ar.1092310411 · Cited by 2,994
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Self-citationRavikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,150
Self-citationThe roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
Boland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0800-08.2008 · Cited by 1,119
Alzheimer's disease: strategies for disease modification
Citron, M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd2896 · Cited by 1,075
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Xie, P.-L., Zheng, M.-Y., Han, R., Chen, W., & Mao, J.-H. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1366061 · Cited by 40
Spleen tyrosine kinase (SYK) blocks autophagic Tau degradation in vitro and in vivo
Schweig, J. E., Yao, H., Coppola, K., Jin, C., Crawford, F., MULLAN, M. J., & Paris, D. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008033 · Cited by 38
Krishnan, S., Shrestha, Y., Jayatunga, D. P. W., Rea, S. L., Martins, R. N., & Bharadwaj, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186739 · Cited by 38
Association Between Atg5-independent Alternative Autophagy and Neurodegenerative Diseases
Honda, S., Arakawa, S., Yamaguchi, H., Torii, S., Sakurai, H. T., Tsujioka, M., Murohashi, M., & Shimizu, S. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.016 · Cited by 36
van Weering, J. R. T., & Scheper, W. (2019) · CNS Drugs · doi:10.1007/s40263-019-00643-1 · Cited by 38
Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms
Hwang, K., Vaknalli, R. N., Addo-Osafo, K., Vicente, M., & Vossel, K. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.903973 · Cited by 35
Lithium and the Interplay Between Telomeres and Mitochondria in Bipolar Disorder
Lundberg, M., Millischer, V., Backlund, L., Martinsson, L., Stenvinkel, P., Sellgren, C. M., Lavebratt, C., & Schalling, M. (2020) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.586083 · Cited by 38
FDA-Approved Kinase Inhibitors in Preclinical and Clinical Trials for Neurological Disorders
Lui, A., Vanleuven, J., Perekopskiy, D., Liu, D., Xu, D., Alzayat, O., Elgokhy, T., Do, T., Gann, M., Martin, R. M., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15121546 · Cited by 36
Gratuze, M., Julien, J., Morin, F., Marette, A., & Planel, E. (2017) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.08.001 · Cited by 34
Alzheimer’s disease: phenotypic approaches using disease models and the targeting of tau protein
Lauretti, E., & Praticò, D. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1737012 · Cited by 34
Das, S., Murumulla, L., Ghosh, P., & Challa, S. (2025) · BioMetals · doi:10.1007/s10534-025-00665-x · Cited by 30
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Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 32
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Young, Z. T., Mok, S., & Gestwicki, J. E. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024612 · Cited by 31
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Bi, D., Xiao, S., Lin, Z., Yao, L., Fang, W., Wu, Y. L., Xu, H. Y., Lu, J., & Xu, X. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c00394 · Cited by 28
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Lai, S. S. M., Ng, K. Y., Koh, R. Y., Chok, K. C., & Chye, S. M. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00737-0 · Cited by 31
Rahman, M. A., Rahman, M. H., Mamun-Or-Rashid, A. N. M., Hwang, H., Chung, S., Kim, B., & Rhim, H. (2022) · Biomedicines · doi:10.3390/biomedicines10051027 · Cited by 31
Ryan, K. C., Ashkavand, Z., Sarasija, S., Laboy, J. T., Samarakoon, R., & Norman, K. R. (2021) · Aging Cell · doi:10.1111/acel.13472 · Cited by 27
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de Thé, F.-X. B., Lassus, B., Schaler, A. W., Fowler, S. L., Goulbourne, C. N., Jeggo, R., la Cour, C. M., Millan, M. J., & Duff, K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01280-w · Cited by 28
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Cardoso, S., Seiça, R. M. F., & Moreira, P. I. (2016) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2016.1205488 · Cited by 27
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Wharton, W., Zhao, L., Steenland, K., Goldstein, F. C., Schneider, J. A., Barnes, L. L., Gearing, M., & Yaşar, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190011 · Cited by 28
Lu, J., Maezawa, I., Weerasekara, S., Erenler, R., Nguyen, T. D. T., Nguyen, J. T., Swisher, L. Z., Li, J., Jin, L., Ranjan, A., et al. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.05.085 · Cited by 26
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Salama, M., El-Desouky, S., Alsayed, A., El‐Hussiny, M., Magdy, K., Fekry, E., Shabka, O., El‐Khodery, S., Youssef, M. A., Sobh, M. A. K., et al. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9974-3 · Cited by 8
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Anglada‐Huguet, M., Rodrigues, S., Hochgräfe, K., Mandelkow�, E., & Mandelkow, E. (2021) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12170 · Cited by 7
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Wang, M., Zhang, B., Guo, R., Wang, H., Wu, D., Peng, X., Guo, H., Duan, J., Yang, W., Ren, P., et al. (2026) · Ultrasonics · doi:10.1016/j.ultras.2026.108075 · Cited by 3
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Ryan, K. C., Ashkavand, Z., Sarasija, S., Laboy, J. T., Samarakoon, R., & Norman, K. R. (2020) · Research Square · doi:10.21203/rs.3.rs-120594/v1 · Cited by 2
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Fernandes, H. R., Gomes, G. F., de Oliveira, A. C. P., & Campos, S. (2023) · Science of Computer Programming · doi:10.1016/j.scico.2023.103028 · Cited by 1
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Metadata
- Authors
- Ozcelik, S., Fraser, G., Castets, P., Schaeffer, V., Skachokova, Z., Breu, K., Clavaguera, F., Sinnreich, M., Kappos, L., Goedert, M., Tolnay, M., & Winkler, D. T.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University Hospital of Basel (CH)
- Corresponding author
- Winkler, David Theo
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-05-07
- Volume
- 8
- Issue
- 5
- Pages
- e62459
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3646815
- OpenAlex
- W1989723790
- Cited by
- 226
- References
- 38
- Citations by year
- 2026: 7 · 2025: 16 · 2024: 9 · 2023: 15 · 2022: 27 · 2021: 26 · 2020: 31 · 2019: 17 · 2018: 17 · 2017: 17 · 2016: 18 · 2015: 17 · 2014: 7 · 2013: 2
- FWCI
- 10.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- National Science Foundation
- University of Pennsylvania
- Velux Stiftung
- Parkinson's UK (K-1012)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (135214, 123812, 310030)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- rapamycin, tau pathology, P301S tau transgenic mice, tauopathy, Alzheimer's disease, autophagy, tau hyperphosphorylation, tau tangles, astrocyte activation, p62, LC3, trehalose, neuroprotection
- MeSH terms
- Animals, Astrocytes, Humans, Mice, Transgenic, Phosphorylation, Solubility, Time Factors, tau Proteins, Disease Progression, Sirolimus, Tauopathies, Mice
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