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REVIEW

The Solute Carrier 26 Family of Proteins in Epithelial Ion Transport

Michael R. Dorwart, Nikolay Shcheynikov, Dongki Yang and Shmuel Muallem

Department of Physiology, University of Texas Southwestern, Medical Center at Dallas, Dallas, Texas, shmuel.muallem{at}utsouthwestern.edu

Transepithelial Cl^– and HCO₃^– transport is critically important for the function of all epithelia and, when altered or ablated, leads to a number of diseases, including cystic fibrosis, congenital chloride diarrhea, deafness, and hypotension (78, 111, 119, 126). HCO₃^– is the biological buffer that maintains acid-base balance, thereby preventing metabolic and respiratory acidosis (48). HCO₃^– also buffers the pH of the mucosal layers that line all epithelia, protecting them from injury (2). Being a chaotropic ion, HCO₃^– is essential for solubilization of ions and macromolecules such as mucins and digestive enzymes in secreted fluids. Most epithelia have a Cl^–/HCO₃ exchange activity in the luminal membrane. The molecular nature of this activity remained a mystery for many years until the discovery of SLC26A3 and the realization that it is a member of a new family of Cl^– and HCO₃^– transporters, the SLC26 family (73, 78). This review will highlight structural features, the functional diversity, and several regulatory aspects of the SLC26 transporters.