Sulfation of Thyroid Hormone by Estrogen Sulfotransferase
Author(s) -
Monique H. A. Kester,
Caren H. van Dijk,
Dick Tibboel,
Alan M. Hood,
Natasha Rose,
Walter Meinl,
Ulrike Pabel,
Hansruedi Glatt,
Charles N. Falany,
Michael W.H. Coughtrie,
T.J. Visser
Publication year - 1999
Publication title -
the journal of clinical endocrinology and metabolism
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.206
H-Index - 353
eISSN - 1945-7197
pISSN - 0021-972X
DOI - 10.1210/jcem.84.7.5975
Subject(s) - sulfotransferase , sulfation , hormone , endocrinology , medicine , thyroid , estrogen , prohormone , in utero , fetus , biology , chemistry , biochemistry , pregnancy , genetics
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.
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