Kester M H, van Dijk C H, Tibboel D, Hood A M, Rose N J, Meinl W, Pabel U, Glatt H, Falany C N, Coughtrie M W, Visser T J
Department of Internal Medicine III, Erasmus University Medical School, Rotterdam, The Netherlands.
J Clin Endocrinol Metab. 1999 Jul;84(7):2577-80. doi: 10.1210/jcem.84.7.5975.
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 approximately 3,3'-T2 > T3 approximately 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.
硫酸化是甲状腺激素失活的途径之一。人胎儿血液和羊水中的碘甲状腺原氨酸硫酸盐浓度非常高，这表明这些结合物在子宫内有重要的生成。人雌激素磺基转移酶（SULT1E1）在子宫等组织中表达。在此我们首次证明，SULT1E1催化激素原T4、活性激素T3以及代谢物反式T3和3,3'-二碘甲状腺原氨酸（3,3'-T2）的硫酸化，对反式T3的偏好约为3,3'-T2 > T3约> T4。因此，单一酶能够使两种如此不同的激素——女性性激素和甲状腺激素——硫酸化。需要考虑SULT1E1在胎儿甲状腺激素代谢中的潜在作用。
