Infantile human labial glands: Distribution of aquaporins and claudins in the context of paracellular and transcellular pathways

Abstract

Human labial glands consist of saliva-secreting cells which are formed by serous and predominantly mucous glandular cells. The following excretory duct system converts the isotonic saliva into a hypotonic fluid. Liquids are transported across the membrane of epithelial cells by paracellular or transcellular mode of action. We studied aquaporins (AQP) and tight junction proteins in the endpieces and duct system of human labial glands of 3–5-month-old infants for the first time. AQP1, AQP3, and AQP5 represent the transcellular transport; tight junction proteins like claudin-1, − 3, − 4, and − 7 regulate the permeability of the paracellular pathway.Specimens of 28 infants were included in this study and analyzed histologically. AQP1 was present in myoepithelial cells and in endothelial cells of small blood vessels. AQP3 showed basolateral plasmamembrane localization in glandular endpieces. AQP5 was localized at the apical cytomembrane in serous and mucous glandular cells and at the lateral membrane in serous cells. Ducts remained unstained with the antibody to AQP1, AQP3, and AQP5. Claudin-1, − 3, − 4, and − 7 were expressed mainly in the lateral plasmamembrane of serous glandular cells. In the ducts, claudin-1, − 4, and − 7 were detected at the basal cell layer, claudin-7 also at the lateral cytomembrane. Our findings provide new insights into the localization of epithelial barrier components necessary for regulating saliva-modification in infantile labial glands.