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Glucuronidation of thyroid hormone by human bilirubin and phenol UDP‐glucuronyltransferase isoenzymes
Author(s) -
Visser Theo J.,
Kaptein Ellen,
Gijzel Anthonie L.,
de Herder Wouter W.,
Ebner Thomas,
Burchell Brian
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80151-j
Subject(s) - glucuronidation , bilirubin , chemistry , glucuronosyltransferase , hormone , biochemistry , thyroid , medicine , endocrinology , microsome , enzyme , biology
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.