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Regulation of epithelial barrier through cell‐cell adhesion‐induced remodeling of N‐glycans of the Na,K‐ATPase beta1 subunit

Recent studies suggested the role of N‐glycans linked to the Na,K‐ATPase β1 subunit in cell‐cell adhesion in epithelia. The aim of this study was to test whether the structure of N‐glycans affects intercellular adhesion. The complexity of N‐glycans of the Na,K‐ATPase β1 subunit gradually decreases upon the formation of a tight monolayer from dispersed MDCK cells. This correlates with a cell‐cell adhesion‐induced increase in expression of GnT‐III (stops N‐glycan branching) and a decrease in expression of GnTs IVC and V (promote N‐glycan branching) as detected by real‐time quantitative PCR. Increased N‐glycan branching due to partial silencing of the gene encoding GnT‐III results in a 2‐fold increase in the paracellular permeability of the MDCK cell monolayer. However, reducing N‐glycan branching by swainsonine tightens and stabilizes cell‐cell junctions as detected by a 3‐fold decrease in the paracellular permeability and a 2‐ to 3‐fold increase in the resistance of the adherens junction proteins to extraction by non‐ionic detergent. Mutagenic removal of N‐glycosylation sites from the Na,K‐ATPase β1‐subunit impairs cell‐cell adhesion and decreases the tightening and stabilizing effects of swainsonine on cell‐cell junctions. These results suggest epithelial cells can regulate tightness of intercellular junctions via remodeling of N‐glycans, including those linked to the Na,K‐ATPase β1‐subunit.