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Updated: Jul 14, 2025

Functional Assessment of Intestinal Tight Junction Barrier and Ion Permeability in Native Tissue by Ussing Chamber Technique
Published on: May 26, 2021
Claudin-23 reshapes epithelial tight junction architecture to regulate barrier function.
Arturo Raya-Sandino1, Kristen M Lozada-Soto1, Nandhini Rajagopal2
1Department of Pathology, University of Michigan Medical School, Ann Arbor, MI, USA.
Claudin-23 (CLDN23) strengthens the intestinal epithelial barrier by forming complexes with CLDN3 and CLDN4. These protein interactions create unique tight junction pores, regulating permeability and barrier function.
Area of Science:
- Cell Biology
- Biophysics
- Gastroenterology
Background:
- Tight junction proteins, claudins, regulate epithelial barrier function.
- Heterogeneity in gastrointestinal barrier function is linked to differential claudin expression.
Purpose of the Study:
- Investigate the role of claudin-23 (CLDN23) in intestinal epithelial barrier function.
- Elucidate the mechanisms by which CLDN23 modulates paracellular permeability.
Main Methods:
- Utilized complementary experimental approaches to study CLDN23 function.
- Employed computational modeling to analyze claudin complex formation and pore architecture.
Main Results:
- CLDN23 is enriched in luminal intestinal epithelial cells, enhancing barrier integrity.
- CLDN23 associates with CLDN3 and CLDN4, influencing their localization and regulating ion/macromolecule permeability.
- Computational models revealed that CLDN23-CLDN3/CLDN4 complexes form unique pores with distinct charge and architecture.
Conclusions:
- CLDN23 strengthens the epithelial barrier by interacting with CLDN3 and CLDN4.
- Claudin complex formation is interaction-dependent, leading to diverse pore properties.
- A model is proposed where distinct claudin complexes modulate epithelial barrier function through altered tight junction structure.

