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RENAL TRANSPORT OF ORGANIC COMPOUNDS MEDIATED BY MOUSE ORGANIC ANION TRANSPORTER 3 (MOAT3): FURTHER SUBSTRATE SPECIFICITY OF MOAT3

Department of Clinical Pharmacy, School of Pharmaceutical Sciences, Showa University, Tokyo, Japan (Y.K., A.T., N.K., M.O., T.Y.); and Department of Physiology and Biophysics, the University of Texas Medical Branch at Galveston, Galveston, Texas (N.O.)

Organic anion transporter 3 [Oat3(Slc22a8)] plays an important role in the renal handling of organic compounds. The substrate specificity of rat Oat3 and human Oat3 has been elucidated; information on mouse Oat3 (mOat3) is less defined. The aim of this study was to extend the substrate selectivity of mOat3. When expressed in Xenopus laevis oocytes, mOat3 mediated the uptake of p-aminohippuric acid and estron sulfate (ES). In addition to these substrates, we found that several organic compounds such as prostaglandin E₂, prostaglandin F₂, allopurinol, 6-mercaptopurine (6-MP), 5-fluorouracil (5-FU), and L-carnitine are substrates of mOat3, compounds identified for the first time. The apparent K_m values for the uptake of mOat3 that mediated the transport of 6-MP, 5-FU, and L-carnitine were 4.01 ± 0.7 µM, 53.9 ± 8.9 nM, and 61.9 ± 1.1 nM, respectively. Northern blot analysis revealed that gene coding for mOat3 is predominant in the kidney and, to a lesser extent, in the brain and the eye. Our findings thus provide further insights into the role of Oat3 in renal drug transport.

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