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

Theo Visser; Ellen Kaptein; Anthonie L. Gijzel; Wouter W. de Herder; Thomas Ebner; Brian Burchell

doi:10.1016/0014-5793(93)80151-J

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

Theo Visser, Ellen Kaptein, Anthonie L. Gijzel, Wouter W. de Herder, Thomas Ebner, Brian Burchell

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Abstract

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.

Original language	English
Pages (from-to)	358-360
Journal	FEBS Letters
Volume	324
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)80151-J
Publication status	Published - 21 Jun 1993

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FEBS Letters - June 21 1993 - Visser - Glucuronidation of thyroid hormone by human bilirubin and phenolFinal published version, 310 KB

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abstract = "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.",

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T1 - Glucuronidation of thyroid hormone by human bilirubin and phenol UDP-glucuronyltransferase isoenzymes

AU - Visser, Theo

AU - Kaptein, Ellen

AU - Gijzel, Anthonie L.

AU - de Herder, Wouter W.

AU - Ebner, Thomas

AU - Burchell, Brian

PY - 1993/6/21

Y1 - 1993/6/21

N2 - 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.

AB - 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.

U2 - 10.1016/0014-5793(93)80151-J

DO - 10.1016/0014-5793(93)80151-J

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EP - 360

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

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

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