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Articles in PresS, published online ahead of print November 14, 2001
Am J Physiol Gastrointest Liver Physiol, 10.1152/ajpgi.00338.2001
Submitted on August 1, 2001
Accepted on November 9, 2001
1 Medicine, University of Cincinnati, Cincinnati, OH, USA
2 Medicine, University of Cincinnati, Cincinnati, OH, USA; Veterans Affairs Medical Center, Cincinnati, OH, USA
* To whom correspondence should be addressed. E-mail: manoocher.soleimani{at}uc.edu.
HCO3- secretion is the most important defense mechanism against acid injury in the duodenum. However, the identity of the transporter(s) mediating apical HCO3- secretion in the duodenum remains unknown. A family of anion exchangers which include Down-Regulated in Adenoma (DRA or SLC26A3), Pendrin (PDS or SLC26A4), and the Putative Anion Transporter (PAT1 or SLC26A6 or CFEX) 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-/HCO3- exchange mode. The 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 to that of DRA. PAT1 was also abundantly detected in stomach and heart. Immunoblot analysis studies identified PAT1 as a ~90 kD 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-/HCO3- exchanger in the small intestine.
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