ArticleBiochemistry2002
alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts.
Article in Biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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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
51 citing papers in PubMed, 104 citations in OpenAlex.
- Lens aging and disease: Molecular mechanisms, functional consequences, and pharmacological implications.Progress in retinal and eye research · 2026Review
- Preventing Age-Related Nuclear Cataract Development - Is Cholesterol the Key?Investigative ophthalmology & visual science · 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
- Cholesterol and Q147E Deamidation Modulates αA-Crystallin Membrane Binding Elucidating Protective Role of Lens Membrane Composition Changes With Aging.Investigative ophthalmology & visual science · 2025Article
- Identification of Age- and Cataract-Related Changes in High-Density Lens Protein Aggregates.Investigative ophthalmology & visual science · 2025Article
- Mechanical Properties of Eye Lens Cortical and Nuclear Membranes and the Whole Lens.Investigative ophthalmology & visual science · 2025Article
- Supra-biological performance of immobilized enzymes enabled by chaperone-like specific non-covalent interactions.Nature communications · 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
- Association of Alpha-Crystallin with Human Cortical and Nuclear Lens Lipid Membrane Increases with the Grade of Cortical and Nuclear Cataract.International journal of molecular sciences · 2024Article
- Interaction of βInternational journal of molecular sciences · 2023Article
- Binding of βInternational journal of molecular sciences · 2023Article
- Butein Inhibits the Glycation of α-Crystallin: An Approach in Prevention of Retinopathy.Journal of fluorescence · 2023Article
- Article
- 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
- An AFM Approach Applied in a Study of α-Crystallin Membrane Association: New Insights into Lens Hardening and Presbyopia Development.Membranes · 2022Article
- Alpha-Crystallin-Membrane Association Modulated by Phospholipid Acyl Chain Length and Degree of Unsaturation.Membranes · 2022Article
- Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.Frontiers in molecular biosciences · 2022Article
- Differentially expressed gene profiles and associated ceRNA network in ATG7-Deficient lens epithelial cells under oxidative stress.Frontiers in genetics · 2022Article
- The interaction of heat shock proteins with cellular membranes: a historical perspective.Cell stress & chaperones · 2021Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
alpha-Crystallin, the major protein component of the vertebrate lens, is thought to play a critical role in the maintenance of transparency through its ability to inhibit stress-induced protein aggregation. However, during aging and cataract formation the amount of membrane-bound alpha-crystallin increases significantly while high molecular weight complexes (HMWCs) comprised of alpha-crystallin and other lens crystallins accumulate. These and other recent data suggest a possible link between cataract formation, the formation of high molecular weight alpha-crystallin aggregates, and the progressive increase in membrane association of alpha-crystallin. To better understand these processes, we characterized the chaperone-like activity (CLA) and subunit exchange of membrane bound alpha-crystallin. In addition, we measured the membrane binding properties of in vitro constituted HMWCs to understand the mechanism by which increased alpha-crystallin is bound to the membrane of old and cataractous lens cells in vivo. Membrane-associated alpha-crystallin complexes have measurably reduced CLA compared to complexes in solution; however, membrane binding does not alter the time required for alpha-crystallin complexes to reach subunit exchange equilibrium. In addition, HMWCs prepared in vitro have a profoundly increased membrane binding capacity as compared to native alpha-crystallin. These results are consistent with a model in which increased membrane binding of alpha-crystallin is an integral step in the pathogenesis of many forms of cataracts.
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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.