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Articles in PresS, published online ahead of print March 6, 2002
Am J Physiol Gastrointest Liver Physiol, 10.1152/ajpgi.00421.2001
Submitted on October 31, 2001
Accepted on February 22, 2002
1 The Water and Salt Research Center, University of Aarhus, Aarhus, Denmark; Department of Oral Biology, Semmelweis University of Budapest, Budapest, Hungary
2 The Water and Salt Research Center, University of Aarhus, Aarhus, Denmark
3 Department of Biochemistry, University of Aarhus, Aarhus, Denmark
4 Department of Oral Biology, Semmelweis University of Budapest, Budapest, Hungary
5 Division of Nephrology, University of California, Los Angeles, CA, USA
6 School of Biological Sciences, University of Manchester, Manchester, United Kingdom
* To whom correspondence should be addressed. E-mail: sn{at}ana.au.dk.
Patterns of salivary HCO3- secretion vary widely between species and between individual glands. In particular, virtually nothing is known about the molecular identity of the HCO3- transporters involved in human salivary secretion. We have therefore examined the distribution of several known members of the Na+-HCO3- cotransporter (NBC) family in the parotid and submandibular glands. Using a combination of RT-PCR and immunoblotting analyses, the electroneutral cotransporters NBC3 and NBCn1 mRNA and protein expression were detected in both human and rat tissues. Immunohistochemistry demonstrated that NBC3 was present at the apical membranes of acinar and duct cells in both human and rat parotid and submandibular glands. NBCn1 was strongly expressed at the basolateral membrane of striated duct cells but not in the acinar cells in the human salivary glands, whereas little or no NBCn1 labeling was observed in the rat salivary glands. The presence of NBCn1 at the basolateral membrane of human striated duct cells suggests that it may contribute to ductal HCO3- secretion. In contrast, the expression of NBC3 at the apical membranes of acinar and duct cells in both human and rat salivary glands, indicates a possible role of this isoform in HCO3- salvage under resting conditions.
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