On the role of Hsp27 in regulating apoptosis

Concannon, C. G.; Gorman, A. M.; Samali, A.

doi:10.1023/a:1021601103096

Cited by 516Heat shock proteins researchCell death mechanisms and regulationClusterin in disease pathology

The DOI matches its Crossref record; 107 of the 109 references it cites were found in a registry or an index.

On the role of Hsp27 in regulating apoptosis

Concannon, C. G., Gorman, A. M., Samali, A.·2003·Apoptosis

DOI 10.1023/a:1021601103096

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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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Three genes overlapped between the microglial and astrocyte factors that were not part of consensus mouse gene lists (UBC, DDIT4 and HSPB1), and these are part of cellular stress and damage response machinery.
“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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Characterization of two novel human small heat shock proteins: protein kinase-related HspB8 and testis-specific HspB9
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Human αB-Crystallin
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Defined sequence segments of the small heat shock proteins HSP25 and αB‐crystallin inhibit actin polymerization
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A 27 kDa heat shock protein that has anomalous prognostic powers in early and advanced breast cancer
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Apoptosis-the story so far...
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Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease.
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Apoptosis of Ewing's sarcoma cells is accompanied by accumulation of ubiquitinated proteins.
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Enhancement of expression of stress proteins by agents that lower the levels of glutathione in cells
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HspB3, the most deviating of the six known human small heat shock proteins
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Heat shock proteins are differentially expressed in human gastrointestinal cancers
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The small heat shock protein HSP27 is not an independent prognostic marker in axillary lymph node-negative breast cancer patients.
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Immunohistochemical studies on Waf1p21, p16, pRb and p53 in human esophageal carcinomas and neighboring epithelia from a high-risk area in northern China
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Expression of the small heat shock genes during Drosophila development: comparison of the accumulation of hsp23 and hsp27 mRNAs and polypeptides
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Heat shock protein expression in human tumours grown in severe combined immunodeficient mice
Katoh, M., Koninkx, J. F. J. G., & Schumacher, U. (2000) · Cancer Letters · doi:10.1016/s0304-3835(00)00601-7 · Cited by 19

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Authors: Concannon, C. G., Gorman, A. M., & Samali, A.
Affiliations: Ollscoil na Gaillimhe – University of Galway (IE)
ORCID: Gorman, A. M.
Venue: Apoptosis
Publisher: Springer Science and Business Media LLC
Published: 2003-01
Volume: 8
Issue: 1
Pages: 61-70
ISSN: 1360-8185 (ISSN-L)
1573-675X
DOI: 10.1023/a:1021601103096
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: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
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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On the role of Hsp27 in regulating apoptosis

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