Singer S S, Giera D, Johnson J, Sylvester S
Endocrinology. 1976 Apr;98(4):963-74. doi: 10.1210/endo-98-4-963.
Liver cytosols from female rats contained 6-8 times as much cortisol sulfotransferase activity as those from males. The reaction product, with both sexes, appeared to be cortisol-21 sulfate. Liver cytosols from male and female rats showed different substrate preferences when tested with cortisol, estradiol-17beta, testosterone, and dehydroepiandrosterone, suggesting that they contained different steroid sulfotransferases. Fractionation of cytosols from female rats on DEAE Sephadex A-50 columns resolved 3 steroid sulfotransferases, or families of steroid sulfotransferases (STI, STII, and STIII). These enzymes exhibited different substrate preferences. STI and STIII had the greatest preferences for cortisol, although none of the enzymes was restricted to the glucocorticoid. Fractionation of cytosols from males resolved 2 sulfotransferases which eluted at salt concentrations identical to STII and STIII from females. Study of the development of cortisol sulfotransferase activity with age showed little enzyme activity in rats of either sex at 2 days after birth. Enzyme activity developed in parallel in both sexes until 30 days after birth. Then the sulfotransferase activity began to rise in females and to drop in males. By day 50-55 both sexes attained adult enzyme levels. STII was the major enzyme in all immature animals. STIII was also present, but STI was absent. In male rats STIII activity began to rise by day 30. Soon after, STII activity began to drop. By day 55 adult male patterns developed. STI was the major enzyme in females by day 30. In ensuing days all 3 enzyme levels rose, until by day 50 adult enzyme patterns and levels were attained. The data suggest that the ovaries stimulated production of all 3 sulfotransferases and that the testes suppressed production of STII (and perhaps STI). Preliminary studies with gonadectomized rats supported the suppressive role of the testes, but suggested that the ovaries were not the only factor controlling sulfotransferase production in female rats.
雌性大鼠肝脏胞质溶胶中皮质醇硫酸转移酶的活性是雄性大鼠的6 - 8倍。无论雌雄，反应产物似乎都是皮质醇 - 21 - 硫酸盐。当用皮质醇、雌二醇 - 17β、睾酮和脱氢表雄酮进行测试时，雄性和雌性大鼠的肝脏胞质溶胶表现出不同的底物偏好，这表明它们含有不同的类固醇硫酸转移酶。在DEAE - 葡聚糖A - 50柱上对雌性大鼠的胞质溶胶进行分级分离，分离出3种类固醇硫酸转移酶，或类固醇硫酸转移酶家族（STI、STII和STIII）。这些酶表现出不同的底物偏好。STI和STIII对皮质醇的偏好最大，尽管没有一种酶只作用于糖皮质激素。对雄性大鼠胞质溶胶的分级分离得到2种硫酸转移酶，它们在与雌性大鼠的STII和STIII相同的盐浓度下洗脱。对皮质醇硫酸转移酶活性随年龄发展的研究表明，出生后2天的雌雄大鼠中酶活性都很低。在出生后30天之前，雌雄两性的酶活性平行发展。然后，硫酸转移酶活性在雌性中开始上升，在雄性中开始下降。到50 - 55天时，雌雄两性都达到了成年酶水平。STII是所有未成熟动物中的主要酶。STIII也存在，但STI不存在。在雄性大鼠中，STIII活性在30天时开始上升。不久之后，STII活性开始下降。到55天时，成年雄性模式形成。到30天时，STI是雌性中的主要酶。在随后的几天里，所有3种酶的水平都上升了，直到50天时达到成年酶模式和水平。数据表明，卵巢刺激了所有3种硫酸转移酶的产生，而睾丸抑制了STII（可能还有STI）的产生。对去势大鼠的初步研究支持了睾丸的抑制作用，但表明卵巢不是控制雌性大鼠硫酸转移酶产生的唯一因素。
