Wieland S J, Fox T O
Steroids. 1981 May;37(5):527-28. doi: 10.1016/s0039-128x(81)90359-7.
Since approximately 1% of 3-ketosteroid reductase (which metabolizes dihydrotestosterone (17 beta-hydroxyl-5 alpha-androstan-3-one] to 5 alpha-androstane-3 alpha, 17 beta-diol or 5 alpha-androstane-3 beta, 17 beta-diol) from mouse kidney cytosol adheres to DNA under conditions that allow virtually complete androgen receptor binding, these two DNA-binding activities were compared in cytosol extracts of mouse kidney and hypothalamus-preoptic area. This DNA-binding fractions of 3-ketosteroid reductase was distinguished from androgen receptor in several ways: (1) its pattern of elution from DNA-cellulose with steps of increasing NaCl concentration differed from that for receptors from wild-type kidney; (2) it was influenced differently by the mutation Tfm, both in level and in DNA-cellulose elution pattern; (3) in mouse kidney cytosol it was relatively stable at moderate (25 degrees C) temperatures which rapidly inactivated ligand-free androgen receptors in the same cytosols; (4) the DNA-binding was not proportional to androgen receptor levels between two wild-type tissues, the hypothalamus-preoptic area and kidney. By these criteria, a simple relationship of androgen receptors and a DNA-binding fraction of 3-ketosteroid reductase activity is unlikely.
由于在能使雄激素受体几乎完全结合的条件下，来自小鼠肾胞质溶胶的约1%的3-酮类固醇还原酶（将二氢睾酮（17β-羟基-5α-雄甾烷-3-酮）代谢为5α-雄甾烷-3α，17β-二醇或5α-雄甾烷-3β，17β-二醇）会黏附于DNA，因此在小鼠肾和下丘脑-视前区的胞质溶胶提取物中对这两种DNA结合活性进行了比较。3-酮类固醇还原酶的这种DNA结合部分在几个方面与雄激素受体有所不同：（1）其从DNA纤维素上用逐步增加的NaCl浓度洗脱的模式与野生型肾受体的洗脱模式不同；（2）它受Tfm突变的影响在水平和DNA纤维素洗脱模式上均有所不同；（3）在小鼠肾胞质溶胶中，它在中等温度（25℃）下相对稳定，而相同胞质溶胶中无配体的雄激素受体则会迅速失活；（4）在两个野生型组织即下丘脑-视前区和肾之间，DNA结合与雄激素受体水平不成正比。根据这些标准，雄激素受体与3-酮类固醇还原酶活性的一个DNA结合部分之间不太可能存在简单的关系。
