ArticleActa physiologica (Oxford, England)2017
Claudin-2-mediated cation and water transport share a common pore.
Article in Acta physiologica (Oxford, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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61 citing papers in PubMed, 114 citations in OpenAlex.
- Inflammation-Induced Claudin-2 Up-Regulation Limits Pancreatitis Development by Enhancing Pancreatic Ductal Transport.Gastroenterology · 2026Article
- Mechanism of Fluid Reabsorption in Kidney Proximal Tubule: Interplay Between Lateral NaActa physiologica (Oxford, England) · 2026Article
- Gut Microbiota as a Mediator of Dietary Salt Effects on Blood Pressure.International journal of molecular sciences · 2026Review
- Molecular dynamics analyses of CLDN15 pore size and charge selectivity.The Journal of general physiology · 2026Article
- Review
- Exploring claudin proteins: from sequence motifs to their impact on tight junction-mediated signaling pathways.Amino acids · 2025Review
- Claudin Proteins: Their Potential Role in Obesity and Adipose Tissue Signaling, Physiology and Disease.Nutrients · 2025Review
- Prebiotics as modulators of colonic calcium and magnesium uptake.Acta physiologica (Oxford, England) · 2025Review
- Inter-claudin antagonism of paracellular pore function: mechanism and beyond.Tissue barriers · 2025Review
- Paracellular Transport and Renal Tubule Calcium Handling: Emerging Roles in Kidney Stone Disease.Journal of the American Society of Nephrology : JASN · 2024Review
- Liver abscess induced by intestinal hypervirulentiScience · 2024Article
- Biophysics of claudin proteins in tight junction architecture: Three decades of progress.Biophysical journal · 2024Review
- Article
- Transporters, Ion Channels, and Junctional Proteins in Choroid Plexus Epithelial Cells.Biomedicines · 2024Review
- Review
- Quercetin Improves Barrier Properties in Porcine Small Intestine but Not in Peyer's Patches.International journal of molecular sciences · 2024Article
- Prednisolone Targets Claudins in Mouse Brain Blood Vessels.International journal of molecular sciences · 2023Article
- Chronic Ouabain Targets Pore-Forming Claudin-2 and Ameliorates Radiation-Induced Damage to the Rat Intestinal Tissue Barrier.International journal of molecular sciences · 2023Article
- Article
- Critical Signaling Transduction Pathways and Intestinal Barrier: Implications for Pathophysiology and Therapeutics.Pharmaceuticals (Basel, Switzerland) · 2023Review
1 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
aimClaudin-2 is a tight junction protein typically located in 'leaky' epithelia exhibiting large paracellular permeabilities like small intestine and proximal kidney tubule. Former studies revealed that claudin-2 forms paracellular channels for small cations like sodium and potassium and also paracellular channels for water. This study analyses whether the diffusive transport of sodium and water occurs through a common pore of the claudin-2 channel.
methodsWild-type claudin-2 and different claudin-2 mutants were expressed in MDCK I kidney tubule cells using an inducible system. Ion and water permeability and the effect of blocking reagents on both were investigated on different clones of the mutants.
resultsNeutralization of a negatively charged cation interaction site in the pore with the mutation, D65N, decreased both sodium permeability and water permeability. Claudin-2 mutants (I66C and S68C) with substitution of the pore-lining amino acids with cysteine were used to test the effect of steric blocking of the claudin-2 pore by thiol-reactive reagents. Addition of thiol-reactive reagents to these mutants simultaneously decreased conductance and water permeability. Remarkably, all experimental perturbations caused parallel changes in ion conductance and water permeability, disproving different or independent passage pathways.
conclusionOur results indicate that claudin-2-mediated cation and water transport are frictionally coupled and share a common pore. This pore is lined and determined in permeability by amino acid residues of the first extracellular loop of claudin-2.
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