Lamb D J, Steinberger A, Sanborn B M
Endocr Res Commun. 1981;8(4):263-72. doi: 10.3109/07435808109045745.
The nuclear accumulation of 3H-androgen had been correlated with the effects of this steroid on nuclear RNA polymerase activity in the Sertoli cell under identical experimental conditions. The synthetic androgen methyltrienolone (R1881) was chosen to avoid ambiguities caused by metabolism of the radioligand. Nuclear accumulation of specifically bound 3H-R1881 was apparent after 5 min and preceded RNA polymerase II activation. RNA polymerase II activity was significantly increased by 10 min after administration of R1881, and the response was maximal at 15 min. Although nuclear binding of 3H-R1881 continued to increase over this interval, the enzyme activity declined to basal levels by 20 min. Saturation of nuclear binding sites required concentrations of R1881 that were approximately one order of magnitude higher than those required for maximal polymerase II activation at 15 min. The results indicate that occupancy of only a small fraction of the specific nuclear binding sites by androgen is required to elicit maximal elevation of RNA polymerase II activity in cultured Sertoli cells.
在相同实验条件下,3H-雄激素的核内蓄积与该类固醇对支持细胞中核RNA聚合酶活性的影响相关。选择合成雄激素甲基三烯olone(R1881)以避免放射性配体代谢引起的歧义。特异性结合的3H-R1881在5分钟后出现核内蓄积,并先于RNA聚合酶II激活。给予R1881后10分钟,RNA聚合酶II活性显著增加,在15分钟时反应达到最大值。尽管在此期间3H-R1881的核结合持续增加,但酶活性在20分钟时降至基础水平。核结合位点的饱和所需的R1881浓度比15分钟时最大聚合酶II激活所需的浓度高约一个数量级。结果表明,雄激素仅占据一小部分特异性核结合位点即可在培养的支持细胞中引起RNA聚合酶II活性的最大升高。