H+ and HCO3- transporters in human salivary ducts. An immunohistochemical study.

The presence and cellular distribution of key H+ and HCO3- transport proteins was studied in human salivary ducts. Immunofluorescence and immunoperoxidase light microscopy was applied, using specific antibodies against the NHE1 and NHE3 isoforms of the Na+/H+ exchanger, against the 31 and 70 kDa subunits of the vacuolar H+-ATPase and against the electrogenic Na+-HCO3- cotransporter. The results show basolateral NHE1 and apical NHE3 in human submandibular, parotid and sublingual duct cells. Vacuolar H+-ATPase was found predominantly in the apical membrane of parotid, submandibular and sublingual duct cells, although it was absent in certain parotid striated duct cells. The Na+-HCO3- cotransporter was predominantly expressed in the apical membrane of parotid and sublingual striated ducts, and intracellularly distributed in the distal parts of the gland tree and in submandibular ducts. The results indicate that HCO3- transport properties of salivary ducts may vary not only between gland and species, but even in different duct segments of the same gland as well.