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Papers In Press, published online ahead of print March 16, 2003
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Molecular Endocrinology, Laval University, Quebec, PQ G1V 4G2
Corresponding Author: alain.belanger{at}crchul.ulaval.ca
Arachidonic and linoleic acids are metabolized, in several tissues, to hydroxylated metabolites which are important mediators of many physiological and pathophysiological processes. The conjugation of leukotriene B4 (LTB4), 5-hydroxyeicosatetraenoic acid (HETE), 12-HETE and 15-HETE, and 13- hydroxyoctadecadienoic acid (HODE) by the human UGT enzymes was investigated. All substrates tested were efficiently conjugated by human liver microsomes to polar derivatives containing the glucuronyl moiety as assessed by mass spectrometry. The screening analyses with stably expressed UGT enzymes in HK293 showed that glucuronidation of LTB4 was observed with UGT1A1, UGT1A3, UGT1A8 and UGT2B7 whereas UGT1A1, UGT1A3, UGT1A4 and UGT1A9 also conjugated most of the HETEs and 13-HODE. LA and AA metabolites also appear to be good substrates for the UGT2B subfamily members, especially for UGT2B4 and UGT2B7 that conjugate all HETE and 13-HODE. Interestingly, UGT2B10 and UGT2B11, which are considered as orphan enzymes since no conjugation activity was so far demonstrated with these enzymes, conjugated 12-HETE, 15-HETE and 13-HODE. In summary, our data showed that several members of UGT1A and UGT2B families are capable of converting LA and AA metabolites into glucuronide derivatives which is considered as an irreversible step to inactivation and elimination of endogenous substances from the body.
Revised on March 5, 2003
Accepted on March 10, 2003
Glucuronidation of Arachidonic and Linoleic Acid Metabolites by Human UDP-glucuronosyltransferases
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