Saito S, Nakamura T, Titani K, Sugino H
Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
Biochem Biophys Res Commun. 1991 Apr 15;176(1):413-22. doi: 10.1016/0006-291x(91)90940-9.
We have developed an assay method for activin-binding protein, which exploits its high affinity for sulfated polysaccharides. We used this method to investigate the production of activin-binding protein by rat ovarian granulosa cells, in vitro. The production of activin-binding protein by granulosa cells was dependent on the cell density; the maximum was observed at 6 x 10(5) cells/ml. Follicle-stimulating hormone (FSH), but not luteinizing hormone (LH), enhanced production significantly. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and ligand blotting analyses of the activin-binding protein secreted by rat granulosa cells demonstrated it was the same protein molecule as that purified from rat ovaries. It is inferred from these results that the granulosa cell is a source of ovarian activin-binding protein and that its secretion is regulated by FSH.
我们开发了一种用于激活素结合蛋白的检测方法,该方法利用了其对硫酸化多糖的高亲和力。我们使用此方法在体外研究大鼠卵巢颗粒细胞产生激活素结合蛋白的情况。颗粒细胞产生激活素结合蛋白取决于细胞密度;在6×10⁵个细胞/毫升时观察到最大值。促卵泡激素(FSH)而非促黄体生成素(LH)能显著提高其产量。对大鼠颗粒细胞分泌的激活素结合蛋白进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)和配体印迹分析表明,它与从大鼠卵巢中纯化的蛋白分子相同。从这些结果可以推断,颗粒细胞是卵巢激活素结合蛋白的来源,并且其分泌受FSH调节。