Kuiper G G, Lemmen J G, Carlsson B, Corton J C, Safe S H, van der Saag P T, van der Burg B, Gustafsson J A
Center for Biotechnology and Department of Medical Nutrition, Karolinska Institute, Huddinge, Sweden.
Endocrinology. 1998 Oct;139(10):4252-63. doi: 10.1210/endo.139.10.6216.
The rat, mouse and human estrogen receptor (ER) exists as two subtypes, ER alpha and ER beta, which differ in the C-terminal ligand-binding domain and in the N-terminal transactivation domain. In this study, we investigated the estrogenic activity of environmental chemicals and phytoestrogens in competition binding assays with ER alpha or ER beta protein, and in a transient gene expression assay using cells in which an acute estrogenic response is created by cotransfecting cultures with recombinant human ER alpha or ER beta complementary DNA (cDNA) in the presence of an estrogen-dependent reporter plasmid. Saturation ligand-binding analysis of human ER alpha and ER beta protein revealed a single binding component for [3H]-17beta-estradiol (E2) with high affinity [dissociation constant (Kd) = 0.05 - 0.1 nM]. All environmental estrogenic chemicals [polychlorinated hydroxybiphenyls, dichlorodiphenyltrichloroethane (DDT) and derivatives, alkylphenols, bisphenol A, methoxychlor and chlordecone] compete with E2 for binding to both ER subtypes with a similar preference and degree. In most instances the relative binding affinities (RBA) are at least 1000-fold lower than that of E2. Some phytoestrogens such as coumestrol, genistein, apigenin, naringenin, and kaempferol compete stronger with E2 for binding to ER beta than to ER alpha. Estrogenic chemicals, as for instance nonylphenol, bisphenol A, o, p'-DDT and 2',4',6'-trichloro-4-biphenylol stimulate the transcriptional activity of ER alpha and ER beta at concentrations of 100-1000 nM. Phytoestrogens, including genistein, coumestrol and zearalenone stimulate the transcriptional activity of both ER subtypes at concentrations of 1-10 nM. The ranking of the estrogenic potency of phytoestrogens for both ER subtypes in the transactivation assay is different; that is, E2 >> zearalenone = coumestrol > genistein > daidzein > apigenin = phloretin > biochanin A = kaempferol = naringenin > formononetin = ipriflavone = quercetin = chrysin for ER alpha and E2 >> genistein = coumestrol > zearalenone > daidzein > biochanin A = apigenin = kaempferol = naringenin > phloretin = quercetin = ipriflavone = formononetin = chrysin for ER beta. Antiestrogenic activity of the phytoestrogens could not be detected, except for zearalenone which is a full agonist for ER alpha and a mixed agonist-antagonist for ER beta. In summary, while the estrogenic potency of industrial-derived estrogenic chemicals is very limited, the estrogenic potency of phytoestrogens is significant, especially for ER beta, and they may trigger many of the biological responses that are evoked by the physiological estrogens.
大鼠、小鼠和人类的雌激素受体(ER)存在两种亚型,即ERα和ERβ,它们在C端配体结合结构域和N端反式激活结构域存在差异。在本研究中,我们通过与ERα或ERβ蛋白的竞争结合试验,以及在瞬时基因表达试验中,使用通过在雌激素依赖性报告质粒存在的情况下用重组人ERα或ERβ互补DNA(cDNA)共转染培养物来产生急性雌激素反应的细胞,研究了环境化学物质和植物雌激素的雌激素活性。对人ERα和ERβ蛋白的饱和配体结合分析显示,[3H]-17β-雌二醇(E2)具有单一结合成分,亲和力高[解离常数(Kd)=0.05 - 0.1 nM]。所有环境雌激素化学物质[多氯羟基联苯、二氯二苯三氯乙烷(DDT)及其衍生物、烷基酚、双酚A、甲氧滴滴涕和十氯酮]与E2竞争结合两种ER亚型,具有相似的偏好和程度。在大多数情况下,相对结合亲和力(RBA)比E2至少低1000倍。一些植物雌激素,如香豆雌酚、染料木黄酮、芹菜素、柚皮素和山奈酚,与E2竞争结合ERβ比结合ERα更强。雌激素化学物质,如壬基酚、双酚A、o,p'-DDT和2',4',6'-三氯-4-联苯酚,在100 - 1000 nM浓度下刺激ERα和ERβ的转录活性。植物雌激素,包括染料木黄酮、香豆雌酚和玉米赤霉烯酮,在1 - 10 nM浓度下刺激两种ER亚型的转录活性。在反式激活试验中,两种ER亚型的植物雌激素雌激素效力排名不同;即,对于ERα,E2 >> 玉米赤霉烯酮 = 香豆雌酚 > 染料木黄酮 > 大豆苷元 > 芹菜素 = 根皮素 > 鹰嘴豆芽素A = 山奈酚 = 柚皮素 > 芒柄花素 = 依普黄酮 = 槲皮素 = 白杨素;对于ERβ,E2 >> 染料木黄酮 = 香豆雌酚 > 玉米赤霉烯酮 > 大豆苷元 > 鹰嘴豆芽素A = 芹菜素 = 山奈酚 = 柚皮素 > 根皮素 = 槲皮素 = 依普黄酮 = 芒柄花素 = 白杨素。除了玉米赤霉烯酮是ERα的完全激动剂和ERβ的混合激动剂 - 拮抗剂外,未检测到植物雌激素的抗雌激素活性。总之,虽然工业来源的雌激素化学物质的雌激素效力非常有限,但植物雌激素的雌激素效力显著,尤其是对ERβ,它们可能引发许多由生理性雌激素引起的生物学反应。