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Claudin-15 (CLDN15) is an integral membrane protein and a member of the claudin family, localized at tight junctions between epithelial cells[2][4]. It forms paracellular channels, polymerizing into tight junction strands to create cation- and water-selective pores that regulate the movement of sodium and water across epithelia, especially in the intestine and large intestine, contributing to epithelial permeability and the maintenance of tissue polarity[1][2][3][4]. Claudin-15 is highly expressed in the villi of the small intestine and crypts of the cecum and large intestine, where it plays a critical role in Na+-dependent nutrient absorption and maintains the energy efficiency of sodium transport. Genetic disruption of CLDN15 impairs paracellular sodium flux and absorption, highlighting its specificity for cation selectivity and its essential function in intestinal barrier physiology[3]. There are no well-established drugs targeting this molecule, and it is not generally considered a classical therapeutic target such as a receptor, enzyme, or transporter, though its dysfunction is implicated in disease states[2][3][4].
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