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On the role of Hsp27 in regulating apoptosis
Abstract
Heat shock proteins (Hsps) comprise several different families of proteins that are induced in response to a wide variety of physiological and environmental insults. One such protein which is highly induced during the stress response is a 27-kDa protein, termed Hsp27 whose expression is seen to correlate with increased survival in response to cytotoxic stimuli. It has been shown to prevent cell death by a wide variety of agents that cause apoptosis. Hsp27 is a molecular chaperone with an ability to interact with a large number of proteins. Recent evidence has shown that Hsp27 regulates apoptosis through an ability to interact with key components of the apoptotic signalling pathway, in particular, those involved in caspase activation and apoptosis. This article will review recent advances in the field and will address some of the potential mechanisms by which Hsp27 functions as an anti-apoptotic molecule.
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“Finally, there were three genes that overlapped between the microglial and astrocyte factors that were not a part of consensus mouse gene lists (UBC, DDIT4 and HSPB1), but which unsurprisingly are also part of cellular stress and damage response machinery52–55.”
From Dissection of artifactual and confounding glial signatures by single-cell sequencing of mouse and human brain (2022) · cites this paper as [52]
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Metadata
- Authors
- Concannon, C. G., Gorman, A. M., & Samali, A.
- Affiliations
- Ollscoil na Gaillimhe – University of Galway (IE)
- ORCID
- Gorman, A. M.
- Venue
- Apoptosis
- Published
- 2003-01
- Volume
- 8
- Issue
- 1
- Pages
- 61-70
- ISSN
- 1360-8185 (ISSN-L)
- 1573-675X
- OpenAlex
- W2144228610
- Cited by
- 513
- References
- 109
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 5 · 2023: 21 · 2022: 11 · 2021: 18 · 2020: 24 · 2019: 19 · 2018: 10 · 2017: 13 · 2016: 13 · 2015: 16 · 2014: 28 · 2013: 26 · 2012: 31
- FWCI
- 11.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- APOPTOSIS (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- Higher Education Authority
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Oncology › Clusterin in disease pathology
- Keywords
- HSP27, heat shock proteins, anti-apoptotic proteins, caspase activation, molecular chaperones, cell survival
- MeSH terms
- Animals, Cytoskeleton, Enzyme Activation, Heat-Shock Proteins, Humans, Models, Biological, Neoplasm Proteins, Neoplasms, Oxidation-Reduction, Protein Binding, Signal Transduction, Apoptosis, Reactive Oxygen Species, Molecular Chaperones, Caspases, HSP27 Heat-Shock Proteins, Caspase Inhibitors
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