Sulfation of Thyroid Hormone by Estrogen Sulfotransferase

Author:

Kester M. H. A.12,van Dijk C. H.1,Tibboel D.2,Hood A. M.3,Rose N. J. M.3,Meinl W.4,Pabel U.4,Glatt H.4,Falany C. N.5,Coughtrie M. W. H.3,Visser T. J.1

Affiliation:

1. Department of Internal Medicine III (M.H.A.K., C.H.v.D., T.J.V.) 3015 GD Rotterdam, The Netherlands

2. Department of Pediatric Surgery (M.H.A.K., D.T.), Erasmus University Medical School, 3015 GD Rotterdam, The Netherlands

3. Department of Molecular and Cellular Pathology, University of Dundee (A.M.H., N.J.M.R., M.W.H.C.), Dundee, Scotland

4. Department of Toxicology, German Institute of Human Nutrition (W.M., U.P., H.G.), Potsdam-Rehbrücke, Germany

5. Department of Pharmacology and Toxicology, University of Alabama (C.N.F.), Birmingham, Alabama

Abstract

Sulfation is one of the pathways by which thyroid hormone is inactivated. Iodothyronine sulfate concentrations are very high in human fetal blood and amniotic fluid, suggesting important production of these conjugates in utero. Human estrogen sulfotransferase (SULT1E1) is expressed among other tissues in the uterus. Here we demonstrate for the first time that SULT1E1 catalyzes the facile sulfation of the prohormone T4, the active hormone T3 and the metabolites rT3 and 3,3′-diiodothyronine (3,3′-T2) with preference for rT3 ≈ 3,3′-T2 > T3 ≈ T4. Thus, a single enzyme is capable of sulfating two such different hormones as the female sex hormone and thyroid hormone. The potential role of SULT1E1 in fetal thyroid hormone metabolism needs to be considered.

Publisher

The Endocrine Society

Subject

Biochemistry (medical),Clinical Biochemistry,Endocrinology,Biochemistry,Endocrinology, Diabetes and Metabolism

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