Thompson C, Powell-Jones W, Lucier G W
Biochem J. 1981 Jan 15;194(1):1-8. doi: 10.1042/bj1940001.
Gel-filtration (Sephadex G-75) analysis of hepatic cytosol reveals both qualitative and quantitative sex differences in oestrogen-binding proteins. The elution profile of [(3)H]oestradiol-labelled cytosol shows four species of oestrogen-binding proteins (peaks I, II, IV and V) common to both sexes. The amount of [(3)H]oestradiol binding in peak I is equivalent in both males and females and corresponds quantitatively to the specific oestrogen receptor. The amount of binding in the remaining three peaks is greater in males than females. In addition, an oestrogen-binding protein (peak III) is present that is unique to male cytosol. Proteinase-inhibition studies demonstrate that the observed multiplicity of oestrogen-binding proteins is not an artefact of proteolytic breakdown. Sex differences in oestrogen-binding proteins are absent in immature male and female animals; the oestrogen-binding protein profile in immature rats resembles that of an adult female. Gonadectomy of adult animals does not affect the oestrogen-binding-protein profile. In contrast, neonatal (day 1) castration results in partial feminization of the characteristic oestrogen-binding protein profile seen in the adult male; the appearance of Peak III is suppressed and marked decreases in the amount of oestradiol binding occurs in the remaining peaks. Hypophysectomy of adult animals results in near abolishment of the observed sex differences; the male oestrogen-binding protein profile is partially feminized and the female profile is partially masculinized, as characterized by the appearance of [(3)H]oestradiol binding in the region of peak III and increased amounts of binding in peaks IV and V. The present studies demonstrate a multiplicity of oestrogen-binding proteins in liver cytosol and raise the possibility that the presence of some of these proteins may be imprinted at birth through the hypothalamic-pituitary axis, by a mechanism requiring neonatal androgen exposure.
对肝细胞溶胶进行凝胶过滤（葡聚糖凝胶G - 75）分析，结果显示雌激素结合蛋白在定性和定量方面均存在性别差异。[³H]雌二醇标记的细胞溶胶的洗脱图谱显示，雌雄两性共有四种雌激素结合蛋白（峰I、II、IV和V）。峰I中[³H]雌二醇的结合量在雄性和雌性中相当，并且在数量上与特异性雌激素受体相对应。其余三个峰中的结合量在雄性中比雌性中更大。此外，存在一种仅在雄性细胞溶胶中出现的雌激素结合蛋白（峰III）。蛋白酶抑制研究表明，观察到的雌激素结合蛋白的多样性并非蛋白水解分解的人为产物。未成熟的雄性和雌性动物不存在雌激素结合蛋白的性别差异；未成熟大鼠的雌激素结合蛋白图谱类似于成年雌性。成年动物去势并不影响雌激素结合蛋白图谱。相反，新生（第1天）阉割会导致成年雄性中特征性雌激素结合蛋白图谱部分雌性化；峰III的出现受到抑制，其余峰中雌二醇结合量显著减少。成年动物垂体切除导致观察到的性别差异几乎消失；雄性雌激素结合蛋白图谱部分雌性化，雌性图谱部分雄性化，其特征是在峰III区域出现[³H]雌二醇结合，并且峰IV和V中的结合量增加。本研究证明了肝细胞溶胶中存在多种雌激素结合蛋白，并提出了一种可能性，即这些蛋白中的一些可能在出生时通过下丘脑 - 垂体轴，通过一种需要新生期雄激素暴露的机制而被印记。
