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Anion Selectivity by the Sodium Iodide Symporter

Institut de Recherche Interdisciplinaire en Biologie Humaine et Moléculaire (J.V.S., C.M., S.C., J.E.D.), Laboratory of Physiology (R.B.), University of Brussels, School of Medicine, and Department of Nuclear Medicine (A.S.), Erasmus Hospital, B 1070 Brussels, Belgium; and Laboratory of Biochemistry and Genetics (J.W.), National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830

Address all correspondence and requests for reprints to: J. Van Sande, Institut de Recherche Interdisciplinaire en Biologie Humaine et Moléculaire, University of Brussels, School of Medicine, Campus Erasme, Building C, Route de Lennik 808, B 1070 Brussels, Belgium. E-mail: jvsande{at}ulb.ac.be.

The iodide transporter of the thyroid (NIS) has been cloned by the group of Carrasco. The NIS-mediated transport was studied by electrophysiological methods in NIS-expressing Xenopus oocytes. Using this method, the anion selectivity of NIS was different from that previously reported for thyroid cells, whereas perchlorate and perrhenate were found not transported. In this study we compared the properties of human NIS, stably transfected in COS-7 cells to those of the transport in a thyroid cell line, the FRTL5 cells, by measuring the transport directly. We measured the uptake of ¹²⁵I^-, ¹⁸⁶ReO₄^-, and ^99mTcO₄^- and studied the effect on it of known competing anions, i.e. ClO₄^-, SCN^-, ClO₃^-, ReO₄^-, and Br^-. We conclude that the properties of the NIS transporter account by themselves for the properties of the thyroid iodide transporter as described previously in thyroid slices. The order of affinity was: ClO₄^- > ReO₄^- > I^- SCN^- > ClO₃^- > Br^-. NIS is also inhibited by dysidenin (as in dog thyroid).

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