ArticleMolecular vision2002
Factors influencing alpha-crystallin association with phospholipid vesicles.
Article in Molecular vision, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 23 citations in OpenAlex.
- 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
- 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
- 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
- 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
- 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
- Large-scale binding of α-crystallin to cell membranes of aged normal human lenses: a phenomenon that can be induced by mild thermal stress.Investigative ophthalmology & visual science · 2010Article
- Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens.Biochemistry · 2009Article
- Isolation and characterization of betaA3-crystallin associated proteinase from alpha-crystallin fraction of human lenses.Molecular vision · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
purposeLens lipids undergo a number of changes with age, including an overall increase in phospholipid acyl chain saturation and a decrease in length. In addition, the amount of membrane bound alpha-crystallin increases dramatically with age and with the onset of cataract. The aim of this study was to determine if a link exists between age and cataract associated changes in lens lipids and the changes in alpha-crystallin membrane association.
methodsProtein-free lipid vesicles composed of a wide variety of synthetic and lens-derived lipid vesicles were formed by sonication. These vesicles were used with fluorescent native and recombinant alpha-crystallin conjugates in vesicle binding assays. Vesicles were collected by centrifugation and bound alpha-crystallin was quantified with fluorescence intensity measurements.
resultsalpha-Crystallin complexes showed remarkably similar binding profiles for all lipid vesicles tested, regardless of lipid origin, phospholipid head group, acyl chain length or saturation, and inclusion of cholesterol. In addition, recombinant alpha-crystallin complexes bind to these vesicles in a manner that is essentially indistinguishable from that of native human and bovine alpha-crystallins. Unlike alpha-crystallin binding to lens membranes containing intrinsic proteins, binding of alpha-crystallin to protein-free vesicles was very high capacity and unsaturable.
conclusionsWe conclude from these data that the binding of alpha-crystallin to lens membranes is not lipid-specific. Furthermore, protein post-translational changes, such as phosphorylation, do not appear to alter alpha-crystallin binding to these vesicles. Given the linearity of the binding curves, we propose that the only limiting factor for normal alpha-crystallin membrane binding is available surface area on the bilayer. Finally, the present data suggests that increased in vivo membrane association of alpha-crystallin is not a result of lipid changes, but more likely a result of non-lipid factors such as the accumulation of high molecular weight forms of alpha-crystallin.
Indexed as
Identifiers
11951084PMC2902965W1472944105What OpenQuestion holds
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.