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Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases
Abstract
Tau proteins aggregate into different neuronal inclusions in several neurodegenerative disorders. In Alzheimer's disease (AD), hyperphosphorylated Tau from paired helical filaments (PHF) of neurofibrillary tangles, named PHF‐Tau, have an electrophoretic profile with four main bands (Tau 55, 64, 69, 74 kDa). In Pick's disease, phosphorylated Tau from Pick bodies are made of two major components (Tau 55, 64 kDa) and a minor 69 kDa. Here we show, using specific antibodies against translated exon 2, 3 or 10 of Tau isoforms, that the set of Tau isoforms engaged in the most insoluble part of PHF in AD is made of Tau isoforms with exon 10 while they are lacking in phosphorylated Tau from Pick's disease. Our results suggest that specific sets of Tau isoforms distinguish between typical neuronal inclusions.
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“For example, increased 3R:4R ratios have been observed in Pick’s disease [108], while decreased 3R:4R ratios are found in progressive supranuclear palsy (PSP) and corticobasal degeneration [109–111].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [108]
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“Imbalanced 3R:4R tau ratios resulting from altered MAPT pre-mRNA splicing have been observed in various tauopathies.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [108]
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Vingtdeux, V., Buée, L., & Sergeant, N. (2011) · InTech eBooks · doi:10.5772/20567 · Cited by 1
Self-citationArrant, A. E., & Roberson, E. D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801942-9.00006-9 · Cited by 3
Pathogenesis of neurodegenerative diseases via templated recruitment
Guo, J. (2013) · ScholarlyCommons (University of Pennsylvania) · Cited by 1
Furukawa, Y. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00019-5 · Cited by 1
Sergeant, N., & Buée, L. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_4 · Cited by 1
Self-citationDelacourte, A., Sergeant, N., & Buée, L. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-336-3_20 · Cited by 1
Self-citation
Metadata
- Authors
- Sergeant, N., David, J.-P., Lefranc, D., Vermersch, P., Wattez, A., & Delacourte, A.
- Affiliations
- Inserm (FR)
- Corresponding author
- Delacourte, A
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-08-04
- Volume
- 412
- Issue
- 3
- Pages
- 578-582
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2017064090
- Cited by
- 117
- References
- 33
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 5 · 2016: 3 · 2015: 6 · 2014: 3 · 2013: 6 · 2012: 4
- FWCI
- 5.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Sanofi
- 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
- tau protein, tau isoforms, phosphorylated tau, Alzheimer's disease, Pick's disease, paired helical filaments, Pick bodies, neurofibrillary tangles, neuronal inclusions, exon 10
- MeSH terms
- Alzheimer Disease, Dementia, Humans, Isomerism, Molecular Weight, Phosphorylation, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Neurofibrillary Tangles, tau Proteins
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