ArticleExperimental eye research2019
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.
Article in Experimental eye research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- In Silico Modelling of the AQP0 T138R Mutation and its' links to Potential Mechanisms of Cataractogenesis.Research square · 2025Article
- A Conserved N-Terminal Di-Arginine Motif Stabilizes Plant DGAT1 and Modulates Lipid Droplet Organization.International journal of molecular sciences · 2025Article
- Structural assessment of OsNIP2;1 highlighted critical residues defining solute specificity and functionality of NIP class aquaporins.Journal of advanced research · 2024Article
- NovelInternational journal of ophthalmology · 2024Article
- Lens Aquaporins in Health and Disease: Location is Everything!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
- Development of a potent embryonic chick lens model for studying congenital cataracts in vivo.Communications biology · 2021Article
- Degradation of connexin 50 protein causes waterclefts in human lens.Open medicine (Warsaw, Poland) · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
This investigation was undertaken to find out whether the positive charges in the Extracellular Loops A (ELA) and C (ELC) of Aquaporin 0 (AQP0) are involved in lens fiber cell-to-cell adhesion (CTCA), and the possible mechanism of CTCA. AQP0 ELA or ELC was substituted with the corresponding AQP1 loop via Polymerase Chain Reaction. Positively charged arginine (R) and histidine (H) of mouse AQP0 ELA and ELC were substituted individually with glutamine (Q) to create R33Q, H40Q, R113Q and H122Q by mutagenesis. cRNA expression, immunostaining, Förster Resonance Energy Transfer (FRET) studies and protein analyses showed localization of all mutants except AQP0-AQP1ELC chimera (AQP0 ELC substituted with AQP1 ELC) at the plasma membrane. Osmotic Swelling Assay revealed comparable water permeability (P
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Registered trials
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