ArticleBiochimica et biophysica acta2014
Intact and N- or C-terminal end truncated AQP0 function as open water channels and cell-to-cell adhesion proteins: end truncation could be a prelude for adjusting the refractive index of the lens to prevent spherical aberration.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 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
- Verification of the gene and protein expression of the aquaglyceroporin AQP3 in the mammalian lens.Experimental eye research · 2024Article
- Aquaporin water channels: roles beyond renal water handling.Nature reviews. Nephrology · 2023Review
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 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
- A novel missense mutation in the gene encoding major intrinsic protein (MIP) in a Giant panda with unilateral cataract formation.BMC genomics · 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
- 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
- Molecular mechanism of Aquaporin 0-induced fiber cell to fiber cell adhesion in the eye lens.Biochemical and biophysical research communications · 2018Article
- Identification of a novel MIP frameshift mutation associated with congenital cataract in a Chinese family by whole-exome sequencing and functional analysis.Eye (London, England) · 2018Article
- The Role of Aquaporins in Ocular Lens Homeostasis.International journal of molecular sciences · 2017Review
- Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.Investigative ophthalmology & visual science · 2017Article
- β1-Integrin Deletion From the Lens Activates Cellular Stress Responses Leading to Apoptosis and Fibrosis.Investigative ophthalmology & visual science · 2017Article
- Applying bimolecular fluorescence complementation to screen and purify aquaporin protein:protein complexes.Protein science : a publication of the Protein Society · 2016Article
- MALDI Imaging Mass Spectrometry Spatially Maps Age-Related Deamidation and Truncation of Human Lens Aquaporin-0.Investigative ophthalmology & visual science · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundInvestigate the impact of natural N- or C-terminal post-translational truncations of lens mature fiber cell Aquaporin 0 (AQP0) on water permeability (Pw) and cell-to-cell adhesion (CTCA) functions.
methodsThe following deletions/truncations were created by site-directed mutagenesis (designations in parentheses): Amino acid residues (AA) 2-6 (AQP0-N-del-2-6), AA235-263 (AQP0-1-234), AA239-263 (AQP0-1-238), AA244-263 (AQP0-1-243), AA247-263 (AQP0-1-246), AA250-263 (AQP0-1-249) and AA260-263 (AQP0-1-259). Protein expression was studied using immunostaining, fluorescent tags and organelle-specific markers. Pw was tested by expressing the respective complementary ribonucleic acid (cRNA) in Xenopus oocytes and conducting osmotic swelling assay. CTCA was assessed by transfecting intact or mutant AQP0 into adhesion-deficient L-cells and performing cell aggregation and adhesion assays.
resultsAQP0-1-234 and AQP0-1-238 did not traffic to the plasma membrane. Trafficking of AQP0-N-del-2-6 and AQP0-1-243 was reduced causing decreased membrane Pw and CTCA. AQP0-1-246, AQP0-1-249 and AQP0-1-259 mutants trafficked properly and functioned normally. Pw and CTCA functions of the mutants were directly proportional to the respective amount of AQP0 expressed at the plasma membrane and remained comparable to those of intact AQP0 (AQP0-1-263).
conclusionsPost-translational truncation of N- or C-terminal end amino acids does not alter the basal water permeability of AQP0 or its adhesive functions. AQP0 may play a role in adjusting the refractive index to prevent spherical aberration in the constantly growing lens. GENERAL SIGNIFICANCE: Similar studies can be extended to other lens proteins which undergo post-translational truncations to find out how they assist the lens to maintain transparency and homeostasis for proper focusing of objects on to the retina.
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