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analysis of claudin-15 tight junction paracellular architecture by molecular dynamics simulations
Data show that alterations in myosin light chain kinase activity, claudin-15 and claudin-2 expression are associated with gluten-induced symptomatology and intestinal permeability changes in diarrhea-predominant irritable bowel syndrome (IBS-D).
structure of claudin-15 at a resolution of 2.4 angstroms; structure reveals a characteristic beta-sheet fold comprising 2 extracellular segments, which is anchored to a transmembrane four-helix bundle by a consensus motif; findings provide insight into molecular basis of ion homeostasis across tight junctions
Claudin-15 knockout leads to Na(+) deficiency and glucose malabsorption in the mouse adult small intestine.
Claudin-15-based formation of tight junctions to organize the microenvironment including ion conductance is important for normal-sized morphogenesis of the small intestine.
This gene encodes a member of the claudin family. Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets, and also play critical roles in maintaining cell polarity and signal transductions. Alternatively spliced transcript variants encoding the same protein have been found for this gene.
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