ArticleInvestigative ophthalmology & visual science2017
Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.
Article in Investigative ophthalmology & visual science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 25 citations in OpenAlex.
- CatExperimental eye research · 2026Article
- Effect of hydrogen peroxide on lens transparency, intracellular pH, gap junction coupling, hydrostatic pressure and membrane water permeability.Experimental eye research · 2024Article
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- GPX1 knockout, not catalase knockout, causes accelerated abnormal optical aberrations and cataract in the aging lens.Molecular vision · 2022Article
- Loss of fiber cell communication may contribute to the development of cataracts of many different etiologies.Frontiers in physiology · 2022Review
- Beyond the Channels: Adhesion Functions of Aquaporin 0 and Connexin 50 in Lens Development.Frontiers in cell and developmental biology · 2022Review
- Deletion of beaded filament proteins or the C-terminal end of Aquaporin 0 causes analogous abnormal distortion aberrations in mouse lens.Experimental eye research · 2021Article
- Eph-ephrin Signaling Affects Eye Lens Fiber Cell Intracellular Voltage and Membrane Conductance.Frontiers in physiology · 2021Article
- Lens aquaporins function as peroxiporins to facilitate membrane transport of hydrogen peroxide.Biochemical and biophysical research communications · 2020Article
- Positively charged amino acid residues in the extracellular loops A and C of lens aquaporin 0 interact with the negative charges in the plasma membrane to facilitate cell-to-cell adhesion.Experimental eye research · 2019Article
- C-Terminal End of Aquaporin 0 Regulates Lens Gap Junction Channel Function.Investigative ophthalmology & visual science · 2019Article
- The Connexin50D47A Mutant Causes Cataracts by Calcium Precipitation.Investigative ophthalmology & visual science · 2019Article
- A predominant form of C-terminally end-cleaved AQP0 functions as an open water channel and an adhesion protein in AQP0Biochemical and biophysical research communications · 2019Article
- Deletion of Seventeen Amino Acids at the C-Terminal End of Aquaporin 0 Causes Distortion Aberration and Cataract in the Lenses of AQP0ΔC/ΔC Mice.Investigative ophthalmology & visual science · 2019Article
- Proteome-transcriptome analysis and proteome remodeling in mouse lens epithelium and fibers.Experimental eye research · 2019Article
- Molecular mechanism of Aquaporin 0-induced fiber cell to fiber cell adhesion in the eye lens.Biochemical and biophysical research communications · 2018Article
- Aquaporin 5 promotes corneal wound healing.Experimental eye research · 2018Article
- Congenital cataract: a guide to genetic and clinical management.Therapeutic advances in rare diseaseReview
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Purpose: The objective of this study was to understand the molecular and physiologic mechanisms behind the lens cataract differences in Aquaporin 0-knockout-Heterozygous (AQP0-Htz) mice developed in C57 and FVB (lacks beaded filaments [BFs]) strains. Methods: Lens transparency was studied using dark field light microscopy. Water permeability (Pf) was measured in fiber cell membrane vesicles. Western blotting/immunostaining was performed to verify expression of BF proteins and connexins. Microelectrode-based intact lens intracellular impedance was measured to determine gap junction (GJ) coupling resistance. Lens intracellular hydrostatic pressure (HP) was determined using a microelectrode/manometer system. Results: Lens opacity and spherical aberration were more distinct in AQP0-Htz lenses from FVB than C57 strains. In either background, compared to wild type (WT), AQP0-Htz lenses showed decreased Pf (approximately 50%), which was restored by transgenic expression of AQP1 (TgAQP1/AQP0-Htz), but the opacities and differences between FVB and C57 persisted. Western blotting revealed no change in connexin expression levels. However, in C57 AQP0-Htz and TgAQP1/AQP0-Htz lenses, GJ coupling resistance decreased approximately 2.8-fold and the HP gradient decreased approximately 1.9-fold. Increased Pf in TgAQP1/AQP0-Htz did not alter GJ coupling resistance or HP. Conclusions: In C57 AQP0-Htz lenses, GJ coupling resistance decreased. HP reduction was smaller than the coupling resistance reduction, a reflection of an increase in fluid circulation, which is one reason for the less severe cataract in C57 than FVB. Overall, our results suggest that AQP0 modulates GJs in the presence of BF proteins to maintain lens transparency and homeostasis.
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Registered trials
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