ArticleInvestigative ophthalmology & visual science2010
α- and β-crystallins modulate the head group order of human lens membranes during aging.
Article in Investigative ophthalmology & visual science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Lens aging and disease: Molecular mechanisms, functional consequences, and pharmacological implications.Progress in retinal and eye research · 2026Review
- Cholesterol and Q147E Deamidation Modulates αA-Crystallin Membrane Binding Elucidating Protective Role of Lens Membrane Composition Changes With Aging.Investigative ophthalmology & visual science · 2025Article
- Interaction of βInternational journal of molecular sciences · 2023Article
- Binding of βInternational journal of molecular sciences · 2023Article
- Native Ambient Mass Spectrometry of an Intact Membrane Protein Assembly and Soluble Protein Assemblies Directly from Lens Tissue.Angewandte Chemie (International ed. in English) · 2022Article
- Native Ambient Mass Spectrometry of an Intact Membrane Protein Assembly and Soluble Protein Assemblies Directly from Lens Tissue.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Alpha-Crystallin-Membrane Association Modulated by Phospholipid Acyl Chain Length and Degree of Unsaturation.Membranes · 2022Article
- 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 four major phospholipids of eye lens membranes.Experimental eye research · 2021Article
- Small molecules, both dietary and endogenous, influence the onset of lens cataracts.Experimental eye research · 2017Review
- Effect of Mild Heating on Human Lens Epithelial Cells: A Possible Model of Lens Aging.Scientific reports · 2016Article
- The etiology of human age-related cataract. Proteins don't last forever.Biochimica et biophysica acta · 2016Review
- αA-crystallin gene CpG islands hypermethylation in nuclear cataract after pars plana vitrectomy.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2015Article
- Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Carbon turnover in the water-soluble protein of the adult human lens.Molecular vision · 2013Article
- Article
- Degradation of an old human protein: age-dependent cleavage of γS-crystallin generates a peptide that binds to cell membranes.The Journal of biological chemistry · 2012Article
- Instability of the cellular lipidome with age.Age (Dordrecht, Netherlands) · 2012Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
purposeTo examine the physical properties of human lens cell membranes as a function of age.
methodsThe environment of the phospholipid head groups in fiber cell membranes from human lenses, aged 22 to 83 years, was assessed with Laurdan and two-photon confocal microscopy. The effect of mild thermal stress on head group order was studied with lens pairs in which one intact lens was incubated at 50 °C. Dihydrosphingomyelin vesicles were preloaded with Laurdan, α-, β-, or γ-crystallin was added, and surface fluidity was determined.
resultsThe membrane head group environment became more fluid with age as indicated by increased water penetration. Furthermore, these changes could be replicated simply by exposing intact human lenses to mild thermal stress; conditions which decreased the concentration of soluble α- and β-crystallins. Vesicle binding experiments showed that α- and β-, but not γ-, crystallins markedly affected head group order.
conclusionsThe physical properties of cell membranes in the lens nucleus change substantially with age, and α- and β-crystallins may modulate this effect. β-Crystallins may therefore play a role in lens cells, and cells of other tissues, apart from being simple structural proteins. Age-dependent loss of these crystallins may affect membrane integrity and contribute to the dysfunction of lenses in older people.
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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.