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The Journal of Clinical Endocrinology & Metabolism Vol. 84, No. 4 1357-1364
Copyright © 1999 by The Endocrine Society

Original Studies

Characterization of Human Iodothyronine Sulfotransferases1

Monique H. A. Kester, Ellen Kaptein, Thirza J. Roest, Caren H. van Dijk, Dick Tibboel, Walter Meinl, Hansruedi Glatt, Michael W. H. Coughtrie and Theo J. Visser

Department of Internal Medicine III, Erasmus University Medical School (M.H.A.K., E.K., T.J.R., C.H.v.D., T.J.V.), and the Department of Pediatric Surgery, Erasmus University Medical School and Sophia Children Hospital (M.H.A.K., D.T.), 3000 DR Rotterdam, The Netherlands; the Department of Toxicology, German Institute of Human Nutrition (W.M., H.G.) D-14558, Potsdam-Rehbrucke, Germany; and the Department of Molecular and Cellular Pathology, University of Dundee (M.W.H.C.), Dundee DD1 9S4, Scotland

Address all correspondence and requests for reprints to: Dr. Theo J. Visser, Department of Internal Medicine III, Erasmus University Medical School, Room Bd 234, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands. E-mail: visser{at}inw3.azr.nl

Sulfation is an important pathway of thyroid hormone metabolism that facilitates the degradation of the hormone by the type I iodothyronine deiodinase, but little is known about which human sulfotransferase isoenzymes are involved. We have investigated the sulfation of the prohormone T4, the active hormone T3, and the metabolites rT3 and 3,3'-diiodothyronine (3,3'-T2) by human liver and kidney cytosol as well as by recombinant human SULT1A1 and SULT1A3, previously known as phenol-preferring and monoamine-preferring phenol sulfotransferase, respectively. In all cases, the substrate preference was 3,3'-T2 >> rT3 > T3 > T4. The apparent Km values of 3,3'-T2 and T3 [at 50 µmol/L 3'-phosphoadenosine-5'-phosphosulfate (PAPS)] were 1.02 and 54.9 µmol/L for liver cytosol, 0.64 and 27.8 µmol/L for kidney cytosol, 0.14 and 29.1 µmol/L for SULT1A1, and 33 and 112 µmol/L for SULT1A3, respectively. The apparent Km of PAPS (at 0.1 µmol/L 3,3'-T2) was 6.0 µmol/L for liver cytosol, 9.0 µmol/L for kidney cytosol, 0.65 µmol/L for SULT1A1, and 2.7 µmol/L for SULT1A3. The sulfation of 3,3'-T2 was inhibited by the other iodothyronines in a concentration-dependent manner. The inhibition profiles of the 3,3'-T2 sulfotransferase activities of liver and kidney cytosol obtained by addition of 10 µmol/L of the various analogs were better correlated with the inhibition profile of SULT1A1 than with that of SULT1A3. These results indicate similar substrate specificities for iodothyronine sulfation by native human liver and kidney sulfotransferases and recombinant SULT1A1 and SULT1A3. Of the latter, SULT1A1 clearly shows the highest affinity for both iodothyronines and PAPS, but it remains to be established whether it is the prominent isoenzyme for sulfation of thyroid hormone in human liver and kidney.




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