Mosselman S, Polman J, Dijkema R
N.V. Organon, Department of Biotechnology and Biochemistry, The Netherlands.
FEBS Lett. 1996 Aug 19;392(1):49-53. doi: 10.1016/0014-5793(96)00782-x.
A novel estrogen receptor (hereinafter referred to as ER beta) was cloned using degenerate PCR primers. A comparison of the amino acid sequence of ER beta with the "classical' ER (ER alpha) shows a high degree of conservation of the DNA-binding domain (96%), and of the ligand-binding domain (58%). In contrast, the A/B domain, the hinge region and the F-domain are not conserved. Northern blot analysis revealed that ER beta is expressed in human thymus, spleen, ovary and testis. Transient transfections of an ER beta expression construct together with an ERE-based reporter construct in CHO cells clearly demonstrated transactivation of ER beta by 17 beta-estradiol. In addition, the ER alpha antagonist ICI-164384 is a potent antagonist for ER beta as well. Interestingly, the level of transactivation by 17 beta-estradiol is higher for ER alpha than for ER beta, which may reflect suboptimal conditions for ER beta at the level of the ligand, responsive element or cellular context.
利用简并PCR引物克隆出一种新型雌激素受体（以下简称ERβ）。将ERβ的氨基酸序列与“经典”雌激素受体（ERα）进行比较，结果显示DNA结合结构域（96%）和配体结合结构域（58%）具有高度保守性。相比之下，A/B结构域、铰链区和F结构域并不保守。Northern印迹分析表明，ERβ在人类胸腺、脾脏、卵巢和睾丸中表达。在CHO细胞中，将ERβ表达构建体与基于雌激素反应元件（ERE）的报告基因构建体一起进行瞬时转染，结果清楚地证明了17β-雌二醇对ERβ的反式激活作用。此外，ERα拮抗剂ICI-164384对ERβ也是一种有效的拮抗剂。有趣的是，17β-雌二醇对ERα的反式激活水平高于对ERβ的反式激活水平，这可能反映了在配体、反应元件或细胞环境水平上，ERβ的条件并不理想。
