Pousette A, Björk P, Carlström K
J Steroid Biochem. 1987 Jan;26(1):31-4. doi: 10.1016/0022-4731(87)90027-6.
An estramustine binding protein, in many aspects similar to the prostatic secretion protein (PSP), has partly been characterized in the submaxillary gland of the male rat. The [3H]estramustine-macromolecule complex is found in the void volume of a Sephadex G 200 column, indicating a Stokes radius larger than 52 A. The estramustine binding protein is bound to Concanavalin-A, indicating a glycoprotein structure. Like PSP, the macromolecule complex that is bound to Concanavalin-A inhibits the binding of the androgen-receptor complex to DNA-cellulose. The concentration of the protein is decreased following testectomy or estrogen treatment but can be restored to normal values following testosterone administration. These results strongly indicate that the estramustine binding macromolecule in the submaxillary gland belongs to the same group of proteins as PSP. We have earlier proposed a role for PSP as an intracellular regulator of androgen activity. Based on these new results it is tempting to speculate that androgen sensitive glycoproteins may act in the same way in all androgen sensitive tissues.
一种雌莫司汀结合蛋白，在许多方面与前列腺分泌蛋白（PSP）相似，已在雄性大鼠的颌下腺中得到部分表征。[3H]雌莫司汀 - 大分子复合物出现在葡聚糖G 200柱的空体积中，表明其斯托克斯半径大于52埃。雌莫司汀结合蛋白与伴刀豆球蛋白A结合，表明其具有糖蛋白结构。与PSP一样，与伴刀豆球蛋白A结合的大分子复合物会抑制雄激素受体复合物与DNA - 纤维素的结合。睾丸切除或雌激素处理后，该蛋白的浓度会降低，但睾酮给药后可恢复到正常值。这些结果有力地表明，颌下腺中的雌莫司汀结合大分子与PSP属于同一类蛋白质。我们之前曾提出PSP作为雄激素活性的细胞内调节剂的作用。基于这些新结果，很容易推测雄激素敏感糖蛋白可能在所有雄激素敏感组织中以相同方式起作用。
