Halting of Caspase Activity Protects Tau from MC1-Conformational Change and Aggregation Article Swipe
Emma Mead
,
Dimitra Kestoras
,
Yolanda Gibson
,
Lucy Hamilton
,
Ross Goodson
,
Sophie Jones
,
Sarah Eversden
,
Peter Davies
,
Michael J. O’Neill
,
Michael Hutton
,
Philip Szekeres
,
Joanna Wolak
·
YOU?
·
· 2016
· Open Access
·
· DOI: https://doi.org/10.3233/jad-150960
YOU?
·
· 2016
· Open Access
·
· DOI: https://doi.org/10.3233/jad-150960
Intracellular neurofibrillary tangles (NFTs) are the hallmark of Alzheimer’s disease and other tauopathies in which tau, a microtubule-associated protein, loses its ability to stabilize microtubules. Several post-translational modifications including phosphorylation and truncation increase tau’s propensity to aggregate thus forming NFTs; however, the mechanisms underlying tau conformational change and aggregation still remain to be defined. Caspase activation and subsequent proteolytic cleavage of tau is thought to be a potential trigger of this disease-related pathological conformation. The aim of this work was to investigate the link between caspase activation and a disease-related conformational change of tau in a neuroblastoma cell-based model of spontaneous tau aggregation. We demonstrated that caspase induction initiates proteolytic cleavage of tau and generation of conformationally altered and aggregated tau recognized by the MC1 conformational antibody. Most importantly, these events were shown to be attenuated with caspase inhibitors. This implies that therapeutics aimed at inhibiting caspase-mediated tau cleavage may prove beneficial in slowing cleavage and aggregation, thus potentially halting tau pathology and disease progression.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.3233/jad-150960
- https://content.iospress.com:443/download/journal-of-alzheimers-disease/jad150960?id=journal-of-alzheimers-disease%2Fjad150960
- OA Status
- hybrid
- Cited By
- 32
- References
- 45
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2511854837
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W2511854837Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.3233/jad-150960Digital Object Identifier
- Title
-
Halting of Caspase Activity Protects Tau from MC1-Conformational Change and AggregationWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2016Year of publication
- Publication date
-
2016-09-02Full publication date if available
- Authors
-
Emma Mead, Dimitra Kestoras, Yolanda Gibson, Lucy Hamilton, Ross Goodson, Sophie Jones, Sarah Eversden, Peter Davies, Michael J. O’Neill, Michael Hutton, Philip Szekeres, Joanna WolakList of authors in order
- Landing page
-
https://doi.org/10.3233/jad-150960Publisher landing page
- PDF URL
-
https://content.iospress.com:443/download/journal-of-alzheimers-disease/jad150960?id=journal-of-alzheimers-disease%2Fjad150960Direct link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
hybridOpen access status per OpenAlex
- OA URL
-
https://content.iospress.com:443/download/journal-of-alzheimers-disease/jad150960?id=journal-of-alzheimers-disease%2Fjad150960Direct OA link when available
- Concepts
-
Tau protein, Conformational change, Cleavage (geology), Chemistry, Cell biology, Intracellular, Microtubule, Caspase, Caspase 3, Biophysics, Programmed cell death, Biochemistry, Apoptosis, Biology, Alzheimer's disease, Disease, Medicine, Pathology, Fracture (geology), PaleontologyTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
32Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 1, 2023: 2, 2022: 2, 2021: 2, 2020: 16Per-year citation counts (last 5 years)
- References (count)
-
45Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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