Baulieu E E
INSERM U. 33, Laboratoire Hormones, Bicêtre, France.
Horm Res. 1987;28(2-4):181-95. doi: 10.1159/000180943.
Antisteroid hormones compete for hormone binding at the receptor level and prevent the hormonal response. A new concept is proposed for explaining the antiglucocorticosteroid activity of RU 486 in the chick oviduct system. It is based on the ability of the antisteroid to stabilize the hetero-oligomeric 8S-form of the glucocorticosteroid receptor, which involves the interaction of the 94,000-dalton receptor and the heat-shock protein MW 90,000 (hsp 90). It is proposed that hsp 90 caps the DNA-binding site of the receptor, and this prevents it from binding to the DNA of hormone regulatory elements and to increase transcription of regulated genes. This paper reviews other antiglucocorticosteroid and antiestrogen systems with reference to this hypothesis, and also describes a four-step analysis of the molecular mechanism of antisteroid hormone action at the receptor level.
抗类固醇激素在受体水平上竞争激素结合并阻止激素反应。本文提出了一个新的概念来解释RU 486在鸡输卵管系统中的抗糖皮质激素活性。这一概念基于抗类固醇稳定糖皮质激素受体异源寡聚体8S形式的能力，这种稳定涉及94,000道尔顿受体与分子量为90,000的热休克蛋白（hsp 90）的相互作用。有人提出，hsp 90覆盖了受体的DNA结合位点，从而阻止其与激素调节元件的DNA结合并增加受调控基因的转录。本文参照这一假说综述了其他抗糖皮质激素和抗雌激素系统，并描述了抗类固醇激素在受体水平作用分子机制的四步分析。
