Jordan V C, Dix C J, Prestwich G
Adv Exp Med Biol. 1979;117:133-55. doi: 10.1007/978-1-4757-6589-2_7.
Recent studies from this laboratory have demonstrated oestradiol-oestrogen receptors associated with the nuclear compartment of the rat uterine cell will initiate protein synthesis, as evidenced by a rise in progesterone receptor concentrations, and cell division whereas the anti-oestrogen - oestrogen receptor complex causes protein synthesis and cellular hypertrophy rather than hyperplasia. It is probable that this separation of biological activities resides in the intrinsic activity of the respective receptor complexes. We have demonstrated that caution should be exercised in the interpretation of low affinity ligand-hormone receptor interactions undertaken in vitro. Simple tests for ligand specificity for a binding protein are clearly insufficient evidence to characterise a hormone receptor complex using a conventional 15 hr technique of sucrose density gradient analysis. Oestrogens and anti-oestrogens do not seem to disrupt the subunit integrity of the cytoplasmic oestrogen receptor and it appears likely that the ligand plays a fundamental role in confering the correct biological properties to the hormone receptor complex.
该实验室最近的研究表明，与大鼠子宫细胞核区室相关的雌二醇 - 雌激素受体会启动蛋白质合成，这表现为孕酮受体浓度升高以及细胞分裂；而抗雌激素 - 雌激素受体复合物则会导致蛋白质合成和细胞肥大而非增生。很可能这种生物活性的差异存在于各自受体复合物的内在活性中。我们已经证明，在解释体外进行的低亲和力配体 - 激素受体相互作用时应谨慎。对于结合蛋白的配体特异性的简单测试显然不足以作为使用传统的15小时蔗糖密度梯度分析技术来表征激素受体复合物的证据。雌激素和抗雌激素似乎不会破坏细胞质雌激素受体的亚基完整性，而且配体似乎在赋予激素受体复合物正确的生物学特性方面起着基本作用。
