Tau‐66: evidence for a novel tau conformation in Alzheimer's disease
Abstract
We have characterized a novel monoclonal antibody, Tau‐66, raised against recombinant human tau. Immunohistochemistry using Tau‐66 reveals a somatic‐neuronal stain in the superior temporal gyrus (STG) that is more intense in Alzheimer's disease (AD) brain than in normal brain. In hippocampus, Tau‐66 yields a pattern similar to STG, except that neurofibrillary lesions are preferentially stained if present. In mild AD cases, Tau‐66 stains plaques lacking obvious dystrophic neurites (termed herein ‘diffuse reticulated plaques’) in STG and the hippocampus. Enzyme‐linked immunosorbent assay (ELISA) analysis reveals that Tau‐66 is specific for tau, as there is no cross‐reactivity with MAP2, tubulin, Aβ 1−40, or Aβ 1−42, although Tau‐66 fails to react with tau or any other polypeptide on western blots. The epitope of Tau‐66, as assessed by ELISA testing of tau deletion mutants, appears discontinuous, requiring residues 155–244 and 305–314. Tau‐66 reactivity exhibits buffer and temperature sensitivity in an ELISA format and is readily abolished by SDS treatment. Taken together these lines of evidence indicate that the Tau‐66 epitope is conformation‐dependent, perhaps involving a close interaction of the proline‐rich and the third microtubule‐binding regions. This is the first indication that tau can undergo this novel folding event and that this conformation of tau is involved in AD pathology.
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Accumulation of tau in astrocytes alters astrocytic function, induces neuronal degeneration and promotes cell death through serial degenerative events such as BBB collapse and expression of low-molecular-weight heat shock proteins.
“Accumulation of tau in astrocytes alters astrocytic function, induces neuronal degeneration and promotes cell death through a serial degenerative events, such as boosting blood-brain barrier (BBB) collapse, and inducing expression of heat shock proteins with low molecular weight [228, 434, 436, 437].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [436]
Tau inclusions have been reported in microglia despite a lack of tau expression, providing evidence that pathological tau may transfer between cells in the brain.
“Tau inclusions have also been reported in microglia [80–82] despite a lack of tau expression, providing further evidence that pathological tau may also be transferring between cells in the brain.”
From Glial contributions to neurodegeneration in tauopathies (2017) · cites this paper as [81]
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Self-citation
- Authors
- Ghoshal, N., García‐Sierra, F., Fu, Y., Beckett, L. A., Mufson, E. J., Kuret, J., Berry, R. W., & Binder, L. I.
- Affiliations
- Northwestern University (US)
- Rush University Medical Center (US)
- The Ohio State University (US)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2001-06
- Volume
- 77
- Issue
- 5
- Pages
- 1372-1385
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1894083234
- Cited by
- 97
- References
- 55
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 1 · 2023: 4 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 3 · 2018: 5 · 2017: 2 · 2016: 7 · 2015: 4 · 2013: 2 · 2012: 5
- FWCI
- 2.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Northwestern University
- National Institutes of Health (1r03ag014499-01)
- National Institute on Aging (AG14499, AG09465, AG 10668, R01AG010668)
- 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 protein, tau conformation, Alzheimer's disease, superior temporal gyrus, hippocampus, conformational epitopes, proline-rich region
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Antibodies, Monoclonal, Antibody Specificity, Epitopes, Enzyme-Linked Immunosorbent Assay, Female, Humans, Hybridomas, Immunohistochemistry, Male, Middle Aged, Protein Conformation, Blotting, Western, Neurofibrillary Tangles, tau Proteins, Microscopy, Confocal, Fluorescent Antibody Technique, Indirect
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