Fukuoka H, Jimbo T
Dept. of Perinato-Gynecology, Kagawa Medical School, Japan.
Nihon Naibunpi Gakkai Zasshi. 1988 Aug 20;64(8):698-706. doi: 10.1507/endocrine1927.64.8_698.
RU 34886 (RU 486) has been proved to fully antagonize the actions of glucocorticoid and progestin at the receptor level. The binding characteristics of RU 486 with the thymic glucocorticoid receptor (GR) and the uterine progestin receptor (PR) were investigated in order to elucidate the mechanism of these antagonistic actions. The ability of RU 486 was studied to promote the "activation" and the "nuclear translocation" of GR and RP. Under heat activation, RU 486 dissociated faster from the activated GR than the non activated, and the binding complex of RU 486 and GR showed lower affinity for DNA-cellulose than the glucocorticoid agonist-GR complex. Nearly undetectable amounts of RU 486 were recovered in the nucleus. Conversely, the RU 486-PR complex showed no difference of dissociation rate between the activated and the non activated condition. Its affinity for DNA-cellulose was the same as that of the activated progestin agonist-PR complex. A large amount of this compound was demonstrated in the nucleus.
RU 34886（RU 486）已被证明在受体水平上能完全拮抗糖皮质激素和孕激素的作用。为阐明这些拮抗作用的机制，研究了RU 486与胸腺糖皮质激素受体（GR）和子宫孕激素受体（PR）的结合特性。研究了RU 486促进GR和PR“激活”及“核转位”的能力。在热激活条件下，RU 486从活化的GR上解离的速度比未活化的GR更快，且RU 486与GR的结合复合物对DNA纤维素的亲和力低于糖皮质激素激动剂 - GR复合物。在细胞核中几乎检测不到RU 486。相反，RU 486 - PR复合物在活化和未活化条件下的解离速率没有差异。其对DNA纤维素的亲和力与活化的孕激素激动剂 - PR复合物相同。在细胞核中发现了大量这种化合物。
