ArticleBiochimica et biophysica acta2014
Alpha-crystallin-mediated protection of lens cells against heat and oxidative stress-induced cell death.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.
- Common variants in SOX-2 and congenital cataract genes contribute to age-related nuclear cataract.Communications biology · 2020Pooled it
- Evaluation of protein profile in vitreous samples of patients with naive age-related macular degeneration using proteomic approaches.BMC geriatrics · 2025Article
- Aging of the human eye lens: Epigenetic landscape and therapeutic targets in age‑related cataracts (Review).International journal of molecular medicine · 2025Review
- The 3D Genome Structure of a Blcap-Linked Silencer Loop Regulates Terminal Differentiation During Lens Fiber Cell Denucleation.Investigative ophthalmology & visual science · 2025Article
- Quantitative spatial analysis of crystallin proteins in human lens epithelial cells.Scientific reports · 2025Article
- Engineered MEVs for photoreceptor-targeted delivery of USP25 to alleviate diabetic retinopathy.Journal of nanobiotechnology · 2025Article
- Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.Protein science : a publication of the Protein Society · 2025Article
- Article
- αB-Crystallin Peptide Fused with Elastin-like Polypeptide: Intracellular Activity in Retinal Pigment Epithelial Cells Challenged with Oxidative Stress.Antioxidants (Basel, Switzerland) · 2023Article
- Interplay between Nrf2 and αB-crystallin in the lens and heart of zebrafish under proteostatic stress.Frontiers in molecular biosciences · 2023Article
- Prognostic value and potential biological functions of ferroptosis-related gene signature in bladder cancer.Oncology letters · 2022Article
- Conformational Changes of α-Crystallin Proteins Induced by Heat Stress.International journal of molecular sciences · 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
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Therapeutic Potential of α-Crystallins in Retinal Neurodegenerative Diseases.Antioxidants (Basel, Switzerland) · 2021Review
- The engineered expression of secreted HSPB5-Fc in CHO cells exhibits cytoprotection in vitro.BMC biotechnology · 2021Article
- Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.Zoological research · 2021Article
- Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens.The protein journal · 2020Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In addition to their key role as structural lens proteins, α-crystallins also appear to confer protection against many eye diseases, including cataract, retinitis pigmentosa, and macular degeneration. Exogenous recombinant α-crystallin proteins were examined for their ability to prevent cell death induced by heat or oxidative stress in a human lens epithelial cell line (HLE-B3). Wild type αA- or αB-crystallin (WT-αA and WT-αB) and αA- or αB-crystallins, modified by the addition of a cell penetration peptide (CPP) designed to enhance the uptake of proteins into cells (gC-αB, TAT-αB, gC-αA), were produced by recombinant methods. In vitro chaperone-like assays were used to assay the ability of α-crystallins to protect client proteins from chemical or heat induced aggregation. In vivo viability assays were performed in HLE-B3 to determine whether pre-treatment with α-crystallins reduced death after exposure to oxidative or heat stress. Most of the five recombinant α-crystallin proteins tested conferred some in vitro protection from protein aggregation, with the greatest effect seen with WT-αB and gC-αB. All α-crystallins displayed significant protection to oxidative stress induced cell death, while only the αB-crystallins reduced cell death induced by thermal stress. Our findings indicate that the addition of the gC tag enhanced the protective effect of αB-crystallin against oxidative but not thermally-induced cell death. In conclusion, modifications that increase the uptake of α-crystallin proteins into cells, without destroying their chaperone-like activity and anti-apoptotic functions, create the potential to use these proteins therapeutically.
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Registered trials
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