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Am J Physiol Gastrointest Liver Physiol 283: G1207-G1216, 2002. First published July 17, 2002; doi:10.1152/ajpgi.00137.2002
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Vol. 283, Issue 5, G1207-G1216, November 2002

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Colocalization of the apical Clminus /HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger PAT1 and gastric H-K-ATPase in stomach parietal cells

Snezana Petrovic1,5, Zhaohui Wang1, Liyun Ma1, Ursula Seidler4, John G. Forte3, Gary E. Shull2, and Manoocher Soleimani1,5

Departments of 1 Medicine and 2 Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, Ohio 45267-0585; 3 Department of Molecular and Cell Biology, University of California, Berkley, California 94720; 4 University of Tubingen, 72076 Tubingen, Germany; and 5 Veterans Affairs Medical Center at Cincinnati, Cincinnati, Ohio 45220

The apical Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger called the putative anion transporter (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 Dolichos biflorus agglutinin indicated the exclusive expression of PAT1 in gastric parietal cells. Double immunocytochemical staining revealed colocalization 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-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> 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-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger PAT1 is localized on tubulovesicular membranes, and they 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.

Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchange; putative anion transporter; acid secretion; bicarbonate transport; SLC26A6


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