ArticleExperimental eye research2013
The water permeability of lens aquaporin-0 depends on its lipid bilayer environment.
Article in Experimental eye research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 60 citations in OpenAlex.
- Analytical Ultracentrifugation in Different High-Density Media Allows to Assess Heterogeneity of mRNA-Lipid Nanoparticles.Small methods · 2026Article
- Endogenous Aquaporin-0 Lipid Binding in Ocular Lens Tissue via Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Physical Properties of Lens Membranes in Animals with Different Lifespans.Biomolecules · 2025Article
- Regulation of water flow in the ocular lens: new roles for aquaporins.The Journal of physiology · 2024Review
- Verification of the gene and protein expression of the aquaglyceroporin AQP3 in the mammalian lens.Experimental eye research · 2024Article
- Functional regulation of aquaporin dynamics by lipid bilayer composition.Nature communications · 2024Article
- Review
- Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023Article
- Identification and quantification of ionising radiation-induced oxysterol formation in membranes of lens fibre cells.Advances in redox research · 2023Article
- Proteoliposomes reconstituted with human aquaporin-1 reveal novel single-ion-channel properties.Biophysical reports · 2023Article
- Role of aquaporins in corneal healing post chemical injury.Experimental eye research · 2023Review
- Oxysterol Compounds in Mouse Mutant αA- and αB-Crystallin Lenses Can Improve the Optical Properties of the Lens.Investigative ophthalmology & visual science · 2022Article
- Aquaporin ion conductance properties defined by membrane environment, protein structure, and cell physiology.Biophysical reviews · 2022Review
- Signaling Mechanisms and Pharmacological Modulators Governing Diverse Aquaporin Functions in Human Health and Disease.International journal of molecular sciences · 2022Review
- Lens Aquaporins in Health and Disease: Location is Everything!Frontiers in physiology · 2022Review
- Membrane nanodomains and transport functions in plant.Plant physiology · 2021Review
- Spatially Resolved Proteomic Analysis of the Lens Extracellular Diffusion Barrier.Investigative ophthalmology & visual science · 2021Article
- Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation.Membranes · 2021Review
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Formation of cholesterol Bilayer Domains Precedes Formation of Cholesterol Crystals in Membranes Made of the Major Phospholipids of Human Eye Lens Fiber Cell Plasma Membranes.Current eye research · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Aquaporin-0 (AQP0), the primary water channel in lens fiber cells, is critical to lens development, organization, and function. In the avascular lens there is thought to be an internal microcirculation associated with fluid movement. Although AQP0 is known to be important in fluid fluxes across membranes, the water permeability of this channel has only been measured in Xenopus oocytes and in outer lens cortical membranes, but not in inner nuclear membranes, which have an increased cholesterol/phospholipid ratio. Here we measure the unit water permeability of AQP0 in different proteoliposomes with cholesterol/phospholipid ratios and external pHs similar to those found in the cortex and nucleus of the lens. Osmotic stress measurements were performed with proteoliposomes containing AQP0 and three different lipids mixtures: (1) phosphatidylcholine (PC) and phosphatidylglycerol (PG), (2) PC, PG, with 40 mol% cholesterol, and (3) sphingomyelin (SM), PG, with 40 mol% cholesterol. At pH 7.5 the unit permeabilities of AQP0 were 3.5 ± 0.5 × 10(-14) cm(3)/s (mean ± SEM), 1.1 ± 0.1 × 10(-14) cm(3)/s, and 0.50 ± 0.04 × 10(-14) cm(3)/s in PC:PG, PC:PG:cholesterol, and SM:PG:cholesterol, respectively. For lipid mixtures at pH 6.5, corresponding to conditions found in the lens nucleus, the AQP0 permeabilities were 1.5 ± 0.4 × 10(-14) cm(3)/s and 0.76 ± 0.03 × 10(-14) cm(3)/s in PC:PG:cholesterol and SM:PG:cholesterol, respectively. Thus, although AQP0 unit permeability can be modified by changes in pH, it is also sensitive to changes in bilayer lipid composition, and decreases with increasing cholesterol and SM content. These data imply that AQP0 water permeability is regulated by bilayer lipid composition, so that AQP0 permeability would be significantly less in the lens nucleus than in the lens cortex.
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