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cotransporters in murine duodenum
1 Department of Physiology and Pharmacology, Institute of Medical Biology, University of Southern Denmark-Odense University, Winsloewparken 21, DK-5000 Odense C; 2 Department of Physiology, University of Aarhus Ole Worms Alle 160, and 3 Department of Cell Biology, Institute of Anatomy, University of Aarhus University Park 233/234, DK-8000 Aarhus C, Denmark
Inward Na+-HCO
cotransport has previously been demonstrated in acidified duodenal
epithelial cells, but the identity and localization of the mRNAs and
proteins involved have not been determined. The molecular expression
and localization of Na+-HCO
cotransporters (NBCs) were studied by RT-PCR, sequence analysis, and
immunohistochemistry. By fluorescence spectroscopy, the intracellular
pH (pHi) was recorded in suspensions of isolated murine
duodenal epithelial cells loaded with
2',7'-bis(2-carboxyethyl)-5(6)-carboxyfluorescein. Proximal duodenal epithelial cells expressed mRNA encoding two electrogenic NBC1 isoforms and the electroneutral NBCn1. Both NBC1 and
NBCn1 were localized to the basolateral membrane of proximal duodenal
villus cells, whereas the crypt cells did not label with the anti-NBC
antibodies. DIDS or removal of extracellular Cl
increased
pHi, whereas an acidification was observed on removal of
Na+ or both Na+ and Cl. The
effects of inhibitors and ionic dependence of acid/base transporters
were consistent with both inward and outward
Na+-HCO cotransport. Hence, we propose
that NBCs are involved in both basolateral electroneutral
HCO transport as well as basolateral electrogenic
HCO transport in proximal duodenal villus cells.
intracellular pH; ion transport; fluorescence spectroscopy; sodium-bicarbonate cotransporter proteins
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