ArticleThe Biochemical journal2015
Identification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activities.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Anti-aggregation Properties of the Mini-Peptides Derived from Alpha Crystallin Domain of the Small Heat Shock Protein, Tpv HSP 14.3.Molecular biotechnology · 2025Article
- Using a stable protein scaffold to display peptides that bind to alpha-synuclein fibrils.Protein science : a publication of the Protein Society · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- The role of RGC degeneration in the pathogenesis of glaucoma.International journal of biological sciences · 2025Review
- Unveiling MiR-3085-3p as a modulator of cartilage degeneration in facet joint osteoarthritis: A novel therapeutic target.Journal of orthopaedic translation · 2025Article
- Peptains block retinal ganglion cell death in animal models of ocular hypertension: implications for neuroprotection in glaucoma.Cell death & disease · 2022Article
- The protective role of HSP27 in ocular diseases.Molecular biology reports · 2022Review
- Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance.Plant, cell & environment · 2021Article
- HSP20 Exerts a Protective Effect on Preeclampsia by Regulating Function of Trophoblast Cells Via Akt Pathways.Reproductive sciences (Thousand Oaks, Calif.) · 2019Article
- Chaperone-like activity of the N-terminal region of a human small heat shock protein and chaperone-functionalized nanoparticles.Proteins · 2019Article
- A monoclonal antibody targeted to the functional peptide of αB-crystallin inhibits the chaperone and anti-apoptotic activities.Journal of immunological methods · 2019Article
- Systemically administered peptain-1 inhibits retinal ganglion cell death in animal models: implications for neuroprotection in glaucoma.Cell death discovery · 2019Article
- Heterologous expression of Oenococcus oeni sHSP20 confers temperature stress tolerance in Escherichia coli.Cell stress & chaperones · 2018Article
- An αB-Crystallin Peptide Rescues Compartmentalization and Trafficking Response to Cu Overload of ATP7B-H1069Q, the Most Frequent Cause of Wilson Disease in the Caucasian Population.International journal of molecular sciences · 2018Article
- Extracellular small heat shock proteins: exosomal biogenesis and function.Cell stress & chaperones · 2018Review
- BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.Journal of molecular biology · 2017Article
- Lens transcriptome profile during cataract development in Mip-null mice.Biochemical and biophysical research communications · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies have identified peptides in the 'crystallin-domain' of the small heat-shock protein (sHSP) α-crystallin with chaperone and anti-apoptotic activities. We found that peptides in heat-shock protein Hsp20 (G71HFSVLLDVKHFSPEEIAVK91) and Hsp27 (D93RWRVSLDVNHFAPDELTVK113) with sequence homology to α-crystallin also have robust chaperone and anti-apoptotic activities. Both peptides inhibited hyperthermic and chemically induced aggregation of client proteins. The scrambled peptides of Hsp20 and Hsp27 showed no such effects. The chaperone activities of the peptides were better than those from αA- and αB-crystallin. HeLa cells took up the FITC-conjugated Hsp20 peptide and, when the cells were thermally stressed, the peptide was translocated from the cytoplasm to the nucleus. The two peptides inhibited apoptosis in HeLa cells by blocking cytochrome c release from the mitochondria and caspase-3 activation. We found that scrambling the last four amino acids in the two peptides (KAIV in Hsp20 and KTLV in Hsp27) made them unable to enter cells and ineffective against stress-induced apoptosis. Intraperitoneal injection of the peptides prevented sodium-selenite-induced cataract formation in rats by inhibiting protein aggregation and oxidative stress. Our study has identified peptides from Hsp20 and Hsp27 that may have therapeutic benefit in diseases where protein aggregation and apoptosis are contributing factors.
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