Visser T J
Department of Internal Medicine III, Erasmus University Medical School, Rotterdam, The Netherlands.
Chem Biol Interact. 1994 Jun;92(1-3):293-303. doi: 10.1016/0009-2797(94)90071-x.
The type I iodothyronine deiodinase (ID-I) in liver and kidney converts the prohormone thyroxine (T4) by outer ring deiodination (ORD) to bioactive 3,3',5-triiodothyronine (T3) or by inner ring deiodination (IRD) to inactive 3,3',5-triiodothronine (rT3), while it also catalyzes the IRD of T3 and the ORD of rT3, with the latter as the preferred substrate. Sulfation of the phenolic hydroxyl group blocks the ORD of T4, while it strongly stimulates the IRD of both T4 and T3, indicating that sulfation is an important step in the irreversible inactivation of thyroid hormone. This review summarizes recent studies concerning this interaction between sulfation and deiodination of iodothyronines, the characterization of iodothyronine sulfotransferase activities, the measurement of iodothyronine sulfates in humans and animals, and the possible physiological importance of iodothyronine sulfation.
肝脏和肾脏中的I型碘甲状腺原氨酸脱碘酶（ID-I）通过外环脱碘（ORD）将前体激素甲状腺素（T4）转化为生物活性的3,3',5-三碘甲状腺原氨酸（T3），或通过内环脱碘（IRD）将其转化为无活性的3,3',5-三碘甲状腺原氨酸（rT3），同时它也催化T3的IRD和rT3的ORD，其中rT3是更优先的底物。酚羟基的硫酸化会阻断T4的ORD，而它会强烈刺激T4和T3的IRD，这表明硫酸化是甲状腺激素不可逆失活的一个重要步骤。这篇综述总结了关于碘甲状腺原氨酸硫酸化与脱碘之间这种相互作用、碘甲状腺原氨酸硫酸转移酶活性的特征、人和动物体内碘甲状腺原氨酸硫酸盐的测量以及碘甲状腺原氨酸硫酸化可能的生理重要性的近期研究。
