Bunyagidj C, McLachlan J A
Developmental Endocrinology and Pharmacology Section, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.
J Steroid Biochem. 1988 Nov;31(5):795-801. doi: 10.1016/0022-4731(88)90288-9.
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.
研究了小鼠肝脏和子宫中雌激素2/4-羟化酶（ESH）和儿茶酚-O-甲基转移酶（COMT）的活性。虽然2-羟基雌二醇（2-OHE2）是肝脏中的主要产物，但子宫中产生的2-羟基雌二醇和4-羟基雌二醇量相等。在两个组织中，2-羟基雌二醇都是COMT的首选底物，但该酶活性水平在小鼠子宫中要低得多（少17倍）。因此，在失活相对较少的情况下优先产生4-羟基雌二醇（4-OHE2），为子宫组织局部形成化学活性更高的雌激素形式提供了一种机制。
