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Am J Physiol Renal Physiol (April 18, 2007). doi:10.1152/ajprenal.00102.2007
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Submitted on February 27, 2007
Accepted on April 8, 2007

Molecular Identification and Functional Characterization of Rabbit MATE1 and MATE2-K

Xiaohong Zhang1, Nathan J. Cherrington2, and Stephen H. Wright1*

1 Physiology, University of Arizona, Tucson, Arizona, United States
2 Pharmacology and Toxicology, University of Arizona, Tucson, Arizona, United States

* To whom correspondence should be addressed. E-mail: shwright{at}u.arizona.edu.

An electroneutral organic cation-proton exchanger in the apical membrane of proximal tubules mediates the final step of renal organic cation (OC) excretion. Two members of the Multidrug And Toxin Extrusion family, MATE1 and MATE2-K, were recently identified in human and rodent kidney and proposed to be the molecular basis of renal OC/H+ exchange. To take advantage of the comparative value of the large database on the kinetic and selectivity characteristics of OC/H+ exchange that exists for rabbit kidney, we cloned rbMATE1 and rbMATE2-K. The rabbit homologs have 75% (MATE1) and 74% (MATE2-K) amino acid identity to their human counterparts (and 51% identity with each other). rbMATE1 and rbMATE2-K exhibited H+ gradient dependent uptake and efflux of tetraethylammonium (TEA) when expressed in CHO cells. Both transporters displayed similar affinities for selected compounds (IC50s within 2-fold for TEA, 1-methyl-4-phenylpyridinium (MPP), and quinidine); and very different affinities for others (IC50s differing by 8 to 80-fold for choline and cimetidine, respectively). These results indicate that rbMATE1 and rbMATE2-K are multispecific OC/H+ exchangers with similar, but distinct, functional characteristics. Overall, the selectivity of MATE1 and MATE2-K correlated closely with that observed in rabbit renal brush border membrane vesicles.




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