ArticleJournal of cellular biochemistry2010
The role of the cysteine residue in the chaperone and anti-apoptotic functions of human Hsp27.
Article in Journal of cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Intermolecular disulfide bond formation promotes Hsp42 higher-order assembly and shapes client selection in yeast.bioRxiv : the preprint server for biology · 2026Article
- Review
- Homo-oxidized HSPB1 protects H9c2 cells against oxidative stress via activation of KEAP1/NRF2 signaling pathway.iScience · 2023Article
- Site-Specific Glycation of Human Heat Shock Protein (Hsp27) Enhances Its Chaperone Activity.ACS chemical biology · 2023Article
- The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27.International journal of molecular sciences · 2021Article
- Bmal1 Regulates the Redox Rhythm of HSPB1, and Homooxidized HSPB1 Attenuates the Oxidative Stress Injury of Cardiomyocytes.Oxidative medicine and cellular longevity · 2021Article
- Peeking from behind the veil of enigma: emerging insights on small heat shock protein structure and function.Cell stress & chaperones · 2020Review
- Local unfolding of the HSP27 monomer regulates chaperone activity.Nature communications · 2019Article
- Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation.Frontiers in immunology · 2016Review
- Heat shock protein-mediated protection against Cisplatin-induced hair cell death.Journal of the Association for Research in Otolaryngology : JARO · 2015Article
- Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.Cell stress & chaperones · 2014Article
- Pro-inflammatory cytokines downregulate Hsp27 and cause apoptosis of human retinal capillary endothelial cells.Biochimica et biophysica acta · 2014Article
- Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.Biochemistry · 2013Article
- Identification of potential protein targets of isothiocyanates by proteomics.Chemical research in toxicology · 2011Article
- Abnormal modulation of cell protective systems in response to ischemic/reperfusion injury is important in the development of mouse sickle cell hepatopathy.Haematologica · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The small heat shock protein Hsp27 is a molecular chaperone and an anti-apoptotic protein. Human Hsp27 has one cysteine residue at position 137. We investigated the role of this cysteine residue in the chaperone and anti-apoptotic functions of Hsp27 by mutating the cysteine residue to an alanine (Hsp27(C137A)) and comparing it to wild-type protein (Hsp27(WT)). Both proteins were multi-subunit oligomers, but subunits of Hsp27(WT) were disulfide-linked unlike those of Hsp27(C137A), which were monomeric. Hsp27(C137A) was indistinguishable from Hsp27(WT) with regard to its secondary structure, surface hydrophobicity, oligomeric size and chaperone function. S-thiolation and reductive methylation of the cysteine residue had no apparent effect on the chaperone function of Hsp27(WT). The anti-apoptotic function of Hsp27(C137A) and Hsp27(WT) was studied by overexpressing them in CHO cells. No difference in the caspase-3 or -9 activity was observed in staurosporine-treated cells. The rate of apoptosis between Hsp27(C137A) and Hsp27(WT) overexpressing cells was similar whether the cells were treated with staurosporine or etoposide. However, the mutant protein was less protective relative to the wild-type protein in preventing caspase-3 and caspase-9 activation and apoptosis induced by 1 mM H(2)O(2) in CHO and HeLa cells. These data demonstrate that in human Hsp27, disulfide formation by the lone cysteine does not affect its chaperone function and anti-apoptotic function against chemical toxicants. However, oxidation of the lone cysteine in Hsp27 might at least partially affect the anti-apoptotic function against oxidative stress.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.