Differential Incorporation of Tau Isoforms in Alzheimer's Disease

Espinoza, Marisol; de Silva, Rohan; Dickson, Dennis W.; Davies, Peter

doi:10.3233/jad-2008-14101

Cited by 119Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Differential Incorporation of Tau Isoforms in Alzheimer's Disease

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Espinoza, Marisol, de Silva, Rohan, Dickson, Dennis W., Davies, Peter·2008·Journal of Alzheimer's Disease

DOI 10.3233/jad-2008-14101PMC PMC2882247

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Abstract

There are 6 different isoforms of tau expressed in the adult human brain, and little information is available on the cellular distribution of the isoforms. Tau inclusions are found in neurons and occasionally glia in a variety of diseases. Previous studies conducted on brain homogenates suggested that tau isoforms might be differentially incorporated into inclusions. To further elucidate the complex issue of tau isoform composition in Alzheimer's disease (AD) and other neurodegenerative diseases, monoclonal antibodies that differentiate between tau containing residues encoded by exon 10 (4R tau) and tau lacking exon 10 residues (3R tau) were used in single and double labeling immunohistochemistry as well as biochemical analyses of tau isolated from AD and other neurodegenerative diseases. Immunohistochemical analysis of the hippocampus in 34 AD cases performed with these antibodies showed both 3R and 4R tau isoforms in tangles. While biochemical studies showed that both isoforms were present in insoluble tau aggregates in AD hippocampus and cortex, not all tangles appear to be labeled with the 3R and 4R tau specific monoclonal antibodies. Similar studies in progressive supranuclear palsy and Pick's disease confirmed that these diseases were characterized by incorporation of specific isoforms in fibrillar lesions, but lesions in neither disease were exclusively composed of 3R tau or 4R tau isoforms.

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AD is the most prevalent of tauopathies and is considered a secondary tauopathy because tau aggregation is regarded as a response to other pathological proteins or events (Aβ), but it is not driven by tau mutations.
“AD is the most prevalent of tauopathies and is considered a secondary tauopathy because tau aggregation is regarded as a response to other pathological proteins or events (Aβ), but it is not driven by tau mutations (19, 65).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [19]
The Introduction (page unavailable) explicitly lists AD among the primary tauopathies, contrary to the claim that this paper considers it a secondary tauopathy. The Discussion (page unavailable) says there are no known tau-gene mutations in sporadic AD, but it does not establish that tau aggregation is a response to Aβ or that AD is the most prevalent tauopathy. (LLM, conf=0.88)
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In AD, tau tangles contain a mixture of 3R- and 4R-tau isoforms to adopt an AD-characteristic topology.
“In AD, tau tangles contain a mixture of 3R- and 4R-tau isoforms to adopt an AD-characteristic topology (18, 19).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [19]
The Abstract reports both 3R- and 4R-tau in AD tangles, and the Discussion says the isoforms often co-localize, although their proportions vary among cases. Neither passage establishes that the mixture causes tangles to adopt an AD-characteristic topology. (LLM, conf=0.88)
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Authors: Espinoza, M., de Silva, R., Dickson, D. W., & Davies, P.
Affiliations: Albert Einstein College of Medicine (US)
Reta Lila Weston Institute of Neurological Studies, University College London, 1 Wakefield Street, WC1N 1PJ London, UK
Mayo Clinic in Florida (US)
Corresponding author: Davies, Peter
ORCID: Dickson, Dennis W.
Davies, Peter
Venue: Journal of Alzheimer's Disease
Publisher: SAGE Publications
Published: 2008-05-09
Volume: 14
Issue: 1
Pages: 1-16
ISSN: 1387-2877 (ISSN-L)
1875-8908
DOI: 10.3233/jad-2008-14101
PMC: PMC2882247
OpenAlex: W162803433
Cited by: 119
References: 42
Citations by year: 2026: 3 · 2025: 3 · 2024: 8 · 2023: 2 · 2022: 5 · 2021: 16 · 2020: 17 · 2019: 9 · 2018: 10 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 5 · 2013: 3 · 2012: 8
FWCI: 2.72
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Journal of Alzheimer s Disease (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: National Institute of Mental Health (MH38623, R01MH038623)
National Institute of Neurological Disorders and Stroke (T32NS007098, NS 07098)
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: tau isoforms, Alzheimer's disease
MeSH terms: Aged, Aged, 80 and over, Alzheimer Disease, Female, Frontal Lobe, Hippocampus, Humans, Immunoenzyme Techniques, Male, Microscopy, Fluorescence, Middle Aged, Supranuclear Palsy, Progressive, Temporal Lobe, Neurofibrillary Tangles, tau Proteins, Protein Isoforms, Pick Disease of the Brain

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Differential Incorporation of Tau Isoforms in Alzheimer's Disease

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