Catechol estrogen formation in mouse uterus.
Estrogen 2/4-hydroxylase (ESH) and catechol-O-methyltransferase (COMT) activities in mouse liver and uterus were studied. While 2-hydroxyestradiol (2-OHE2) was the predominant product in the liver, equal amounts of 2- and 4-hydroxyestradiol were produced in the uterus. Two-hydroxyestradiol was the preferred substrate for COMT in both tissues, but the level of this enzyme activity was much less in the mouse uterus (17-fold less). Thus, preferential production of 4-hydroxyestradiol (4-OHE2) in the presence of relatively less deactivation provides a mechanism for the local formation of a more chemically active form of estrogen by uterine tissue.
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Developmental Endocrinology and Pharmacology Section, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.
McLachlan
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JA
D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases; D002394:Catechol O-Methyltransferase / Q000378:metabolism; D019363:Cytochrome P-450 CYP1A1; D065633:Cytochrome P-450 CYP1B1; D004958:Estradiol / Q000031:analogs & derivatives / Q000096:biosynthesis; D002393:Estrogens, Catechol / Q000096:biosynthesis*; D005260:Female; D051379:Mice; D013250:Steroid Hydroxylases / Q000378:metabolism; D013997:Time Factors; D014599:Uterus / Q000201:enzymology / Q000378:metabolism*
D002393:Estrogens, Catechol; D004958:Estradiol; C001390:2-hydroxyestradiol; C014036:4-hydroxyestradiol; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C585498:Cyp1b1 protein, mouse; D019363:Cytochrome P-450 CYP1A1; D065633:Cytochrome P-450 CYP1B1; C020120:estrogen 2-hydroxylase; D002394:Catechol O-Methyltransferase