Cited by 306Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

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Boutajangout, Allal, Ingadottir, Johanna, Davies, Peter, Sigurdsson, Einar M.·2011·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2011.07337.xPMC PMC3366469

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Abstract

J. Neurochem. (2011) 118, 658–667. Targeting hyperphosphorylated tau by immunotherapy is emerging as a promising approach to treat tauopathies such as Alzheimer’s disease and frontotemporal dementia. We have previously reported that active tau immunization clears tau aggregates from the brain and attenuates or prevents functional impairments in two different tangle mouse models. Here, we assessed the efficacy of passive immunization with the PHF1 antibody, which targets a phospho‐epitope within one of our active immunogens. Homozygous female tangle mice (JNPL3, 2–3 months) were injected intraperitoneally once per week with PHF1 or pooled mouse IgG (250 μg/125 μL; n = 10 per group) for a total of 13 injections. Their behavior was assessed at 5–6 months of age and brain tissue was subsequently harvested for analyses of treatment efficacy. The treated mice performed better than controls on the traverse beam task (p < 0.03), and had 58% less tau pathology in the dentate gyrus of the hippocampus (p = 0.02). As assessed by western blots, the antibody therapy reduced the levels of insoluble pathological tau by 14–27% (PHF1, p < 0.05; PHF1/total tau, p < 0.0001) and 34–45% (CP13 or CP13/total tau, p < 0.05). Levels of soluble tau and sarkosyl soluble tau were unchanged, compared with controls, as well as total tau levels in all the fractions. Plasma levels of PHF1 correlated inversely with tau pathology in the brainstem (p < 0.01), with a strong trend in the motor cortex (p < 0.06) as well as with insoluble total tau levels (p < 0.02), indicating that higher dose of antibodies may have a greater therapeutic effect. Significant correlation was also observed between performance on the traverse beam task and PHF1 immunoreactivity in the dentate gyrus (p < 0.05) as well as with insoluble PHF1/total tau ratio on western blots (p < 0.04). These results show that passive immunization with tau antibodies can decrease tau pathology and functional impairments in the JNPL3 model. Future studies will determine the feasibility of this approach with other monoclonals and in different tangle models in which thorough cognitive assessment can be performed.

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Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,506
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431
Long-term effects of Aβ42 immunisation in Alzheimer's disease: follow-up of a randomised, placebo-controlled phase I trial
Holmes, C., Boche, D., Wilkinson, D., Yadegarfar, G., Hopkins, V., Bayer, A., Jones, R. W., Bullock, R., Love, S., Neal, J. W., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61075-2 · Cited by 1,416 · cited 1×
“However, recent findings from this trial indicate that plaque clearance did not halt or slow the progression of dementia, emphasizing the need for alternative targets (Holmes et al. 2008).”
Background
Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
Nicoll, J. A. R., Wilkinson, D., Holmes, C., Steart, P., Markham, H., & Weller, R. O. (2003) · Nature Medicine · doi:10.1038/nm840 · Cited by 1,397
Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
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
Self-citation
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Orgogozo, J.-M., Gilman, S., Dartigues, J.-F., Laurent, B., Puel, M., Kirby, L. C., Jouanny, P., Dubois, B., Eisner, L., Flitman, S., et al. (2003) · Neurology · doi:10.1212/01.wnl.0000073623.84147.a8 · Cited by 1,356
Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
Gilman, S., Koller, M., Black, R. S., Jenkins, L., Griffith, S. G., Fox, N. C., Eisner, L., Kirby, L., Rovira, M. B., Forette, F., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000159740.16984.3c · Cited by 1,329

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Additional file 4 of Conformation-selective tau monoclonal antibodies inhibit tau pathology in primary neurons and a mouse model of Alzheimer’s disease
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Additional file 1 of Conformation-selective tau monoclonal antibodies inhibit tau pathology in primary neurons and a mouse model of Alzheimer’s disease
Gibbons, G. S., Kim, S.-J., Wu, Q., Riddle, D. M., Leight, S. N., Changolkar, L. N., Xu, H., Meymand, E. S., O’Reilly, M., Zhang, B., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13192095
Additional file 3 of Conformation-selective tau monoclonal antibodies inhibit tau pathology in primary neurons and a mouse model of Alzheimer’s disease
Gibbons, G. S., Kim, S.-J., Wu, Q., Riddle, D. M., Leight, S. N., Changolkar, L. N., Xu, H., Meymand, E. S., O’Reilly, M., Zhang, B., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13192101
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Behl, C. (2026) · Springer eBooks · doi:10.1007/978-3-662-72210-7_14
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Pan, R., Congdon, E. E., Chukwu, J. E., Luo, C. C., Sigurdsson, E. M., & Kong, X. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.16.716390
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SynCAR platform for capturing neuronal synaptic proteopathic seeds
Sebastian, R. M., Kupp, R., Nanavati, D. M., Parfentev, I., Krzystek, T. J., Romanul, N., Yanamandra, K., Preiss, C. N., Manos, J. D., Wu, H.-Y., et al. (2026) · iScience · doi:10.1016/j.isci.2026.116362

Authors: Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M.
Affiliations: New York University (US)
University of Iceland (IS)
Albert Einstein College of Medicine (US)
Corresponding author: Sigurdsson, Einar M.
ORCID: Boutajangout, Allal
Davies, Peter
Sigurdsson, Einar M.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2011-07
Volume: 118
Issue: 4
Pages: 658-667
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2011.07337.x
PMC: PMC3366469
OpenAlex: W1538003756
Cited by: 306
References: 57
Citations by year: 2026: 6 · 2025: 11 · 2024: 13 · 2023: 10 · 2022: 14 · 2021: 15 · 2020: 22 · 2019: 19 · 2018: 23 · 2017: 25 · 2016: 27 · 2015: 30 · 2014: 35 · 2013: 33 · 2012: 17
FWCI: 20.06
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Alzheimer's Association (AG032611)
National Institutes of Health
National Institute on Aging (R01AG020197, AG032611, R37AG022102, AG022102, AG 020197, R01AG022102, R01AG032611)
National Institute of Mental Health (R37MH038623, MH38623, R01MH038623)
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: passive immunization, hyperphosphorylated tau, tau immunotherapy, tauopathy, Alzheimer's disease, frontotemporal dementia, tau aggregates, motor function, dentate gyrus, neurodegenerative disease treatment
MeSH terms: Animals, Antibodies, Antibodies, Monoclonal, Astrocytes, Brain, Brain Chemistry, Brain Stem, Data Interpretation, Statistical, Enzyme-Linked Immunosorbent Assay, Postural Balance, Female, Gliosis, Image Processing, Computer-Assisted, Immunization, Passive, Immunohistochemistry, Motor Activity, Motor Cortex, Phosphorylation, Blotting, Western, tau Proteins, Dentate Gyrus, Antibodies, Blocking, Neurodegenerative Diseases, Tauopathies, Mice

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Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

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