ArticleExperimental eye research2021
Cholesterol and cholesterol bilayer domains inhibit binding of alpha-crystallin to the membranes made of the major phospholipids of eye lens fiber cell plasma membranes.
Article in Experimental eye research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 20 citations in OpenAlex.
- The Mammalian Ocular Lens in Focus: Development, Anatomy, Physiology, Transparency, Biomechanics, and Age-related Challenges.Journal of visualized experiments : JoVE · 2026Review
- Special Issue "Cellular and Molecular Insights into Ocular Changes Associated with Systemic Disorders and Conditions".International journal of molecular sciences · 2026Article
- 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
- 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
- Mechanical Properties of Eye Lens Cortical and Nuclear Membranes and the Whole Lens.Investigative ophthalmology & visual science · 2025Article
- 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
- 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
- Tissue, cellular, and molecular level determinants for eye lens stiffness and elasticity.Frontiers in ophthalmology · 2024Review
- Interaction of βInternational journal of molecular sciences · 2023Article
- Binding of βInternational journal of molecular sciences · 2023Article
- Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.International journal of molecular sciences · 2022Article
- Membrane elasticity modulated by cholesterol in model of porcine eye lens-lipid membrane.Experimental eye research · 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
- Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation.Membranes · 2021Review
- Cholesterol and cholesterol bilayer domains inhibit binding of alpha-crystallin to the membranes made of the major phospholipids of eye lens fiber cell plasma membranes.Experimental eye research · 2021Article
- Role of Choline in Ocular Diseases.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The concentration of α-crystallin decreases in the eye lens cytoplasm, with a corresponding increase in membrane-bound α-crystallin during cataract formation. The eye lens's fiber cell plasma membrane consists of extremely high cholesterol (Chol) content, forming cholesterol bilayer domains (CBDs) within the membrane. The role of high Chol content in the lens membrane is unclear. Here, we applied the continuous-wave electron paramagnetic resonance spin-labeling method to probe the role of Chol and CBDs on α-crystallin binding to membranes made of four major phospholipids (PLs) of the eye lens, i.e., phosphatidylcholine (PC), sphingomyelin (SM), phosphatidylserine (PS), and phosphatidylethanolamine (PE). Small unilamellar vesicles (SUVs) of PC, SM*, and PS with 0, 23, 33, 50, and 60 mol% Chol and PE* with 0, 9, and 33 mol% Chol were prepared using the rapid solvent exchange method followed by probe-tip sonication. The 1 mol% CSL spin-labels used during SUVs preparation distribute uniformly within the Chol/PL membrane, enabling the investigation of Chol and CBDs' role on α-crystallin binding to the membrane. For PC, SM*, and PS membranes, the binding affinity (K
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