ArticleThe Journal of biological chemistry2013
Chaperone peptides of α-crystallin inhibit epithelial cell apoptosis, protein insolubilization, and opacification in experimental cataracts.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 1 of them a synthesis that pooled it.
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Who cites it
57 citing papers in PubMed, 1 synthesis or guideline pooled it, 83 citations in OpenAlex.
- Alcohol intake and the risk of age-related cataracts: a meta-analysis of prospective cohort studies.PloS one · 2014Pooled it
- Review
- Glycation at the Crossroads of Disease Pathogenesis: Mechanistic Insights and Therapeutic Frontiers.Diseases (Basel, Switzerland) · 2026Review
- 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
- Pharmacological Strategies for Cataract Management: From Molecular Targets to Clinical Translation.International journal of molecular sciences · 2025Review
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- Article
- Research progress on antioxidants and protein aggregation inhibitors in cataract prevention and therapy (Review).Molecular medicine reports · 2025Review
- Thiol-Mediated Enhancement of NACS chemical biology · 2024Article
- Mechanisms contributing to inhibition of retinal ganglion cell death by cell permeable peptain-1 under glaucomatous stress.Cell death discovery · 2024Article
- Peptain-1 blocks ischemia/reperfusion-induced retinal capillary degeneration in mice.Frontiers in cellular neuroscience · 2024Article
- Peptains block retinal ganglion cell death in animal models of ocular hypertension: implications for neuroprotection in glaucoma.Cell death & disease · 2022Article
- Role of ATP-Small Heat Shock Protein Interaction in Human Diseases.Frontiers in molecular biosciences · 2022Review
- αA and αB peptides from human cataractous lenses show antichaperone activity and enhance aggregation of lens proteins.Molecular vision · 2022Article
- Therapeutic Potential of α-Crystallins in Retinal Neurodegenerative Diseases.Antioxidants (Basel, Switzerland) · 2021Review
- HspB4/αA-Crystallin Modulates Neuroinflammation in the Retina via the Stress-Specific Inflammatory Pathways.Journal of clinical medicine · 2021Article
- Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.Zoological research · 2021Article
- Transcriptional analysis of cleft palate in TGFβ3 mutant mice.Scientific reports · 2020Article
- Transporter-Mediated Mitochondrial GSH Depletion Leading to Mitochondrial Dysfunction and Rescue with αB Crystallin Peptide in RPE Cells.Antioxidants (Basel, Switzerland) · 2020Article
- Development of a brain-permeable peptide nanofiber that prevents aggregation of Alzheimer pathogenic proteins.PloS one · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
α-Crystallin is a member of the small heat-shock protein (sHSP) family and consists of two subunits, αA and αB. Both αA- and αB-crystallin act as chaperones and anti-apoptotic proteins. Previous studies have identified the peptide (70)KFVIFLDVKHFSPEDLTVK(88) in αA-crystallin and the peptide (73)DRFSVNLDVKHFSPEELKVK(92) in αB-crystallin as mini-chaperones. In the human lens, lysine 70 (Lys(70)) of αA and Lys(92) of αB (in the mini-chaperone sequences) are acetylated. In this study, we investigated the cellular effects of the unmodified and acetyl mini-chaperones. The αA- and αB-crystallin peptides inhibited stress-induced aggregation of four client proteins, and the αA-acetyl peptide was more effective than the native peptide against three of the client proteins. Both the acetyl and native crystallin peptides inhibited stress-induced apoptosis in two mammalian cell types, and this property was directly related to the inhibition of cytochrome c release from mitochondria and the activity of caspase-3 and -9. In organ-cultured rat lenses, the peptides inhibited calcimycin-induced epithelial cell apoptosis. Intraperitoneal injection of the peptides inhibited cataract development in selenite-treated rats, which was accompanied by inhibition of oxidative stress, protein insolubilization, and caspase activity in the lens. These inhibitory effects were more pronounced for acetyl peptides than native peptides. A scrambled αA-crystallin peptide produced no such effects. The results suggest that the α-crystallin chaperone peptides could be used as therapeutic agents to treat cataracts and diseases in which protein aggregation and apoptosis are contributing factors.
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Registered trials
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