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Am J Physiol Gastrointest Liver Physiol 282: G573-G579, 2002. First published November 14, 2001; doi:10.1152/ajpgi.00338.2001
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Vol. 282, Issue 3, G573-G579, March 2002

SPECIAL COMMUNICATIONS
Identification of an apical Clminus /HCO3minus exchanger in the small intestine

Zhaohui Wang1, Snezana Petrovic1,2, Elizabeth Mann1,2, and Manoocher Soleimani1,2

1 Department of Medicine, University of Cincinnati, Cincinnati 45267 - 0585; and 2 Veterans Affairs Medical Center at Cincinnati, Ohio 45220

HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> secretion is the most important defense mechanism against acid injury in the duodenum. However, the identity of the transporter(s) mediating apical HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> secretion in the duodenum remains unknown. A family of anion exchangers, which include downregulated in adenoma (DRA or SLC26A3), pendrin (PDS or SLC26A4), and the putative anion transporter (PAT1 or SLC26A6) has recently been identified. DRA and pendrin mediate Cl-/base exchange; however, the functional identity and distribution of PAT1 (SLC26A6) is not known. In these studies, we investigated the functional identity, tissue distribution, and membrane localization of PAT1. Expression studies in Xenopus oocytes demonstrated that PAT1 functions in Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchange mode. Tissue distribution studies indicated that the expression of PAT1 is highly abundant in the small intestine but is low in the colon, a pattern opposite that of DRA. PAT1 was also abundantly detected in stomach and heart. Immunoblot analysis studies identified PAT1 as a ~90 kDa protein in the duodenum. Immunohistochemical studies localized PAT1 to the brush border membranes of the villus cells of the duodenum. We propose that PAT1 is an apical Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger in the small intestine.

duodenum; bicarbonate secretion; apical Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchange; putative anion transporter; downregulated in adenoma; chloride/formate exchanger


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