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Physiol. Rev. 84: 987-1049, 2004; doi:10.1152/physrev.00040.2003
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Molecular and Cellular Physiology of Renal Organic Cation and Anion Transport

Stephen H. Wright and William H. Dantzler

Department of Physiology, College of Medicine, University of Arizona, Tucson, Arizona

Organic cations and anions (OCs and OAs, respectively) constitute an extraordinarily diverse array of compounds of physiological, pharmacological, and toxicological importance. Renal secretion of these compounds, which occurs principally along the proximal portion of the nephron, plays a critical role in regulating their plasma concentrations and in clearing the body of potentially toxic xenobiotics agents. The transepithelial transport involves separate entry and exit steps at the basolateral and luminal aspects of renal tubular cells. It is increasingly apparent that basolateral and luminal OC and OA transport reflects the concerted activity of a suite of separate transport processes arranged in parallel in each pole of proximal tubule cells. The cloning of multiple members of several distinct transport families, the subsequent characterization of their activity, and their subcellular localization within distinct regions of the kidney now allows the development of models describing the molecular basis of the renal secretion of OCs and OAs. This review examines recent work on this issue, with particular emphasis on attempts to integrate information concerning the activity of cloned transporters in heterologous expression systems to that observed in studies of physiologically intact renal systems.

1 We have elected to identify all transport proteins using capital letters (e.g., OCT1, OAT2, MRP3) and distinguish particular orthologs, when appropriate, by preceding the acronym with one or two lowercase letters indicative of the species (h, human; r, rat; m, mouse; p, pig; rb, rabbit; fl, flounder; ce, C. elegans; dr, Drosophila).

2 Determined using the NetNGlyc 1.0 Server (http://www.cbs.dtu.dk/services/NetNGlyc/).

3 Unless otherwise indicated, residue numbers reflect the human sequence for the protein under discussion. Consensus phosphorylation sites were predicted using PhosphoBase v.2.0 (http://www.cbs.dtu.dk/databases/PhosphoBase/).

Address for reprint requests and other correspondence: S. H. Wright, Dept. of Physiology, College of Medicine, Univ. of Arizona, Tucson, AZ 85724 (E-mail: shwright{at}u.arizona.edu).




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