Liehr J G, Ricci M J, Jefcoate C R, Hannigan E V, Hokanson J A, Zhu B T
Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston 77555-1031, USA.
Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9220-4. doi: 10.1073/pnas.92.20.9220.
Estradiol is converted to catechol estrogens via 2- and 4-hydroxylation by cytochrome P450 enzymes. 4-Hydroxyestradiol elicits biological activities distinct from estradiol, most notably an oxidant stress response induced by free radicals generated by metabolic redox cycling reactions. In this study, we have examined 2- and 4-hydroxylation of estradiol by microsomes of human uterine myometrium and of associated myomata. In all eight cases studied, estradiol 4-hydroxylation by myoma has been substantially elevated relative to surrounding myometrial tissue (minimum, 2-fold; mean, 5-fold). Estradiol 2-hydroxylation in myomata occurs at much lower rates than 4-hydroxylation (ratio of 4-hydroxyestradiol/2-hydroxyestradiol, 7.9 +/- 1.4) and does not significantly differ from rates in surrounding myometrial tissue. Rates of myometrial 2-hydroxylation of estradiol were also not significantly different from values in patients without myomata. We have used various inhibitors to establish that 4-hydroxylation is catalyzed by a completely different cytochrome P450 than 2-hydroxylation. In myoma, alpha-naphthoflavone and a set of ethynyl polycyclic hydrocarbon inhibitors (5 microM) each inhibited 4-hydroxylation more efficiently (up to 90%) than 2-hydroxylation (up to 40%), indicating > 10-fold differences in Ki (<0.5 microM vs. > 5 microM). These activities were clearly distinguished from the selective 2-hydroxylation of estradiol in placenta by aromatase reported previously (low Km, inhibition by Fadrozole hydrochloride or ICI D1033). 4-Hydroxylation was also selectively inhibited relative to 2-hydroxylation by antibodies raised against cytochrome P450 IB1 (rat) (53 vs. 17%). These data indicate that specific 4-hydroxylation of estradiol in human uterine tissues is catalyzed by a form(s) of cytochrome P450 related to P450 IB1, which contribute(s) little to 2-hydroxylation. This enzyme(s) is therefore a marker for uterine myomata and may play a role in the etiology of the tumor.
雌二醇通过细胞色素P450酶的2-和4-羟基化作用转化为儿茶酚雌激素。4-羟基雌二醇引发的生物活性不同于雌二醇,最显著的是由代谢氧化还原循环反应产生的自由基诱导的氧化应激反应。在本研究中,我们检测了人子宫肌层及其相关肌瘤微粒体对雌二醇的2-和4-羟基化作用。在所研究的所有8例病例中,肌瘤对雌二醇的4-羟基化作用相对于周围肌层组织显著升高(最低为2倍;平均为5倍)。肌瘤中雌二醇的2-羟基化发生率远低于4-羟基化(4-羟基雌二醇/2-羟基雌二醇的比率为7.9±1.4),且与周围肌层组织的发生率无显著差异。子宫肌层对雌二醇的2-羟基化率与无肌瘤患者的值也无显著差异。我们使用了各种抑制剂来确定4-羟基化是由一种与2-羟基化完全不同的细胞色素P450催化的。在肌瘤中,α-萘黄酮和一组乙炔基多环烃抑制剂(5 microM)对4-羟基化的抑制作用(高达90%)比对2-羟基化的抑制作用(高达40%)更有效,表明其抑制常数(Ki)相差10倍以上(<0.5 microM对>5 microM)。这些活性与先前报道的胎盘芳香化酶对雌二醇的选择性2-羟基化作用(低Km,受盐酸法倔唑或ICI D1033抑制)明显不同。相对于2-羟基化,针对细胞色素P450 IB1(大鼠)产生的抗体对4-羟基化也有选择性抑制作用(53%对17%)。这些数据表明,人子宫组织中雌二醇的特异性4-羟基化是由一种与P450 IB1相关的细胞色素P450形式催化的,该形式对2-羟基化作用贡献很小。因此,这种酶是子宫肌瘤的一个标志物,可能在肿瘤的病因学中起作用。