Glucuronidation of thyroid hormone by human bilirubin and phenol UDP‐glucuronyltransferase isoenzymes

FEBS Letters

de Herder, Wouter W.²  Visser, Theo J.²  Kaptein, Ellen²  Burchell, Brian¹  Gijzel, Anthonie L.²  Ebner, Thomas¹ 

[1]Department of Biochemical Medicine, University of Dundee, Dundee, Scotland, UK

[2]Department of Internal Medicine III, Erasmus University Medical School, Rotterdam, The Netherlands

关键词: Thyroid hormone;    Iodothyronine;    Glucuronidation;    Bilirubin;    Phenol;    UDP-glucuronyltransferase;    Human liver;   

DOI  :  10.1016/0014-5793(93)80151-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The glucuronidation of thyroid hormone by UDP-glucuronyltransferases (UGTs) stably transfected in Chinese hamster V79 lung fibroblasts was investigated. Human bilirubin UGT (HP3) and phenol UGT (HP4) both catalysed the glucuronidation of T4 and rT3, whereas glucuronidation of T3 was not significant. rT3 was the preferred substrate for both isoenzymes, glucuronidation rates being 1.6- and 6.4-times higher than conjugation of T4 by HP3 and HP4 clones, respectively. This is the first identification of thyroid hormone as potential alternative endogenous substrate for bilirubin UGT.

【 授权许可】

Unknown