Tseng L, Gurpide E
Endocrinology. 1975 Oct;97(4):825-33. doi: 10.1210/endo-97-4-825.
Estradiol-17beta dehydrogenase activity in proliferative human endometrium (average of 1.5 nmole of estrone formed from estradiol/mg protein/h) was stimulated as much as as 6-fold during incubations of tissue slices in culture medium containing progesterone. Stimulation was already detectable at 7 h and the highest activity values were reached at 48-72 h of incubation in the presence of excess progesterone. Maximal stimulation was achieved with concentrations of the hormone of 0.25 mug/ml or higher. At concentrations approximately equal to midluteal plasma levels (20 ng/ml) more than 50% of the maximal response was observed. Norgestrel (17alpha-ethynyl-18-methyl-19-nortestosterone) was also effective in inducing enzymatic activity. The similarity of the effects obtained with progesterone (a possible substrate for estradiol dehydrogenase) and the synthetic progestin indicates that the stimulation of enzymatic activity was not due to substrate induction. Addition of estradiol to the culture medium had no influence on the activity of the enzyme. The induction of estradiol dehydrogenase by progesterone was inhibited by puromycin or actinomycin D. These observations indicate that progestational agents increase the rate of de novo synthesis of the enzyme. Stimulation of endometrial estradiol dehydrogenase was also observed after 2-3 day oral administration of medroxyprogesterone acetate to women in the follicular phase. In contrast, the enzymatic activity in endometrium obtained from women taking estrogens was found to be as low as in normal proliferative tissue. These in vitro and in vivo results point to progesterone as the agent responsible for the 10-fold increase in endometrial estradiol dehydrogenase activity observed during the luteal phase in menstruating women. Data obtained from superfusion studies of estrogen dynamics in endometrium indicate that changes in enzyme concentrations may play a physiologic role in the regulation of tissue levels of estradiol.
增殖期人子宫内膜中雌二醇 - 17β脱氢酶活性（平均每毫克蛋白质每小时由雌二醇形成1.5纳摩尔雌酮）在含有孕酮的培养基中孵育组织切片时，被刺激高达6倍。在7小时时即可检测到刺激作用，在存在过量孕酮的情况下孵育48 - 72小时时达到最高活性值。激素浓度为0.25微克/毫升或更高时可实现最大刺激。在浓度约等于黄体中期血浆水平（20纳克/毫升）时，观察到超过最大反应的50%。炔诺孕酮（17α - 乙炔基 - 18 - 甲基 - 19 - 去甲睾酮）在诱导酶活性方面也有效。孕酮（雌二醇脱氢酶的可能底物）和合成孕激素所获得的效应相似，表明酶活性的刺激并非由于底物诱导。向培养基中添加雌二醇对该酶的活性没有影响。孕酮对雌二醇脱氢酶的诱导被嘌呤霉素或放线菌素D抑制。这些观察结果表明，孕激素增加了该酶从头合成的速率。在卵泡期向妇女口服醋酸甲羟孕酮2 - 3天后，也观察到子宫内膜雌二醇脱氢酶受到刺激。相反，发现服用雌激素的妇女子宫内膜中的酶活性与正常增殖组织中的一样低。这些体外和体内结果表明，孕酮是导致月经周期黄体期妇女子宫内膜雌二醇脱氢酶活性增加10倍的因素。从子宫内膜雌激素动力学的灌流研究获得的数据表明，酶浓度的变化可能在调节组织中雌二醇水平方面发挥生理作用。
