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1 Department of Medicine, University of Cincinnati, Cincinnati, OH, USA; Research Services, Veterans Affairs Medical Center, Cincinnati, OH, USA
2 Research Services, Veterans Affairs Medical Center, Cincinnati, OH, USA
3 Department of Medicine, University of Cincinnati, Cincinnati, OH, USA
* To whom correspondence should be addressed. E-mail: manoocher.soleimani{at}uc.edu.
SLC26A6 (PAT1) is located on the apical membrane of mouse kidney proximal tubule and mediates Cl-/HCO3- exchange in in vitro expression systems. We hypothesized that PAT1 along with a Cl-/HCO3- exchange are present in apical membranes of rat kidney proximal tubules. Northern hybridizations indicated the exclusive expression of SLC26A6 (PAT1) in rat kidney cortex and immunocytochemical staining localized PAT1 on the apical membrane of proximal tubules, with complete prevention of he labeling with the preadsorbed serum. To examine the functional presence of apical Cl-/HCO3- exchanger, proximal tubules were isolated, microperfused, loaded with the pH sensitive dye BCPCF-AM and examined by digital ratiometric imaging. The pH of the perfusate and bath was kept at 7.4. Buffering capacity was measured and transport rates were calculated as equivalent base flux (EBF). The results demonstrated that in the presence of basolateral DIDS (to inhibit NBC1) and apical EIPA (to inhibit NHE3) the magnitude of cell acidification in response to addition of luminal Cl- was ~5.0 fold higher in the presence than in the absence of CO2/HCO3-. The Cl-dependent base transport was inhibited by ~61% in the presence of 0.5 mM luminal DIDS. The presence of physiologic concentrations of oxalate in the lumen (200 µM) did not affect the Cl-/HCO3- exchange activity. These results are consistent with the presence of SLC26A6 (PAT1) and Cl-/HCO3- exchanger activity in the apical membrane of rat kidney proximal tubule. We propose that SLC26A6 is likely responsible for the apical Cl-/HCO3- (and Cl-/OH-) exchanger activities in kidney proximal tubule.
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