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Articles in PresS, published online ahead of print July 17, 2002
Am J Physiol Gastrointest Liver Physiol, 10.1152/ajpgi.00137.2002
Submitted on April 9, 2002
Accepted on July 12, 2002
1 Department of Medicine, Veterans Affairs Medical Center, Cincinnati, OH, USA; Department of Medicine, University of Cincinnati, Cincinnati, OH, USA
2 Department of Medicine, University of Cincinnati, Cincinnati, OH, USA
3 Department of Medicine, University of Tubingen, Tubingen, Germany
4 Department of Molecular and Cell Biology, University of California, Berkley, CA, USA
5 Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati, Cincinnati, OH, USA
* To whom correspondence should be addressed. E-mail: manoocher.soleimani{at}uc.edu.
The apical Cl-/HCO3- exchanger PAT1 (SLC26A6) is expressed on apical membranes of villus cells in the duodenum but its location in the stomach remains unknown. Here we examined the cell distribution and membrane location of PAT1 in mouse stomach. Immunofluorescence labeling studies with anti-PAT1 antibodies and D. biflorus agglutinin indicated the exclusive expression of PAT1 in gastric parietal cells. Double immunocytochemical staining revealed co-localization of PAT1 with the gastric H-K-ATPase, consistent with expression in tubulovesicles and/or the secretory canaliculus. Radiolabeled 36Cl flux studies demonstrated the functional presence of Cl-/HCO3- exchange in purified tubulovesicles of parietal cells. The expression of PAT1 was significantly decreased in parietal cells of gastric H-K-ATPase null mice, which exhibit a sharp reduction in tubulovesicle membranes. These data indicate that the Cl-/HCO3- exchanger PAT1 is localized on tubulovesicular membranes, and are consistent with the hypothesis that it functions in the maintenance of intravesicular ion concentrations in the resting state and dehydration of vesicles derived from the secretory membranes following the transition from the stimulated to the resting state.
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