ArticleIUBMB life2010
Importance of eye lens α-crystallin heteropolymer with 3:1 αA to αB ratio: stability, aggregation, and modifications.
Article in IUBMB life, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Age-Related Lens Membrane Composition and N101D Deamidation Modulate αA-Crystallin Membrane Interactions Relevant to Cataract.Investigative ophthalmology & visual science · 2026Article
- Heat shock protein-mediated remodeling of the bone immune microenvironment: mechanisms and precision therapeutic strategies for osteoporosis.Journal of translational medicine · 2026Review
- Temperature and cholesterol regulate the association of native bovine lens alpha-crystallin with in vitro reconstituted membranes made of synthetically prepared lipids and cholesterol.Experimental eye research · 2026Article
- Lipid and Cholesterol Peroxidation Leads to α-Crystallin Membrane Aggregation and Cataract Formation.Investigative ophthalmology & visual science · 2025Article
- Cholesterol and Q147E Deamidation Modulates αA-Crystallin Membrane Binding Elucidating Protective Role of Lens Membrane Composition Changes With Aging.Investigative ophthalmology & visual science · 2025Article
- The α-crystallin Chaperones Undergo a Quasi-ordered Co-aggregation Process in Response to Saturating Client Interaction.Journal of molecular biology · 2024Article
- Cholesterol Content Regulates the Interaction of αA-, αB-, and α-Crystallin with the Model of Human Lens-Lipid Membranes.International journal of molecular sciences · 2024Article
- Expression of αA-crystallin (CRYAA)Aging · 2023Article
- Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.International journal of molecular sciences · 2022Article
- Alpha-Crystallin Association with the Model of Human and Animal Eye Lens-Lipid Membranes is Modulated by Surface Hydrophobicity of Membranes.Current eye research · 2022Article
- Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation.Membranes · 2021Review
- Interaction of Alpha-Crystallin with Phospholipid Membranes.Current eye research · 2021Article
- Interaction of alpha-crystallin with four major phospholipids of eye lens membranes.Experimental eye research · 2021Article
- The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020Review
- Differences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses.Experimental eye research · 2018Article
- RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.Biochemical and biophysical research communications · 2017Article
- Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.Journal of proteome research · 2017Article
- Comparison of modification sites in glycated crystallin in vitro and in vivo.Analytical and bioanalytical chemistry · 2015Article
- Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners.PloS one · 2015Article
- Aggregation and fibrillation of eye lens crystallins by homocysteinylation; implication in the eye pathological disorders.The protein journal · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Chaperone-like activity (CLA) of α-crystallin is essential not only for the maintenance of eye lens transparency but also in the biology of other tissues. Eye lens α-crystallin is a heteropolymer composed of two homologous subunits, αA and αB, and in most vertebrates they are present in a ratio of 3:1. The structural and functional significance of this specific ratio of α-crystallin subunits is of considerable interest in understanding its role in the eye lens transparency. Previously, we have shown that although at physiologically relevant conditions αB-crystallin has greater CLA, under stress conditions such as elevated temperatures α-crystallin heteropolymer with 3:1 αA to αB ratio displayed higher CLA (Srinivas et al., Biochem. J., 2008, 414, 453 - 460). Herein, we provide a rationale for the existence of α-crystallin heteropolymer with 3:1 αA to αB ratio in terms of structural stability, aggregation pattern, and susceptibility to posttranslational modifications that could explain the importance of the heteropolymer of α-crystallin in the eye lens. We demonstrate that αA-crystallin is not only more stable but also imparts stability to the heteropolymer by preventing the aggregation of αB-crystallin at higher temperatures by using differential scanning calorimetry, size-exclusion chromatography, and denaturant-induced unfolding methods. Further, the physiological significance of heteropolymer with higher proportion of αA subunit is substantiated by using a heteropolymer with mutant (F71L) αA-crystallin and the susceptibility of 3:1 heteropolymer to glycation-induced modifications. Thus, the existence of 3:1 heteropolymer might be vital for the eye lens transparency under diverse conditions to prevent cataract.
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Registered trials
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.