Hazum E, Keinan D
Peptides. 1984 Jan-Feb;5(1):119-23. doi: 10.1016/0196-9781(84)90061-5.
Specific GnRH receptor proteins of purified rat Leydig cells and membrane preparations were identified using an 125I-labeled bioactive photoaffinity derivative of GnRH. Sodium dodecyl sulfate polyacrylamide gel electrophoresis resulted in the identification of two specific components with apparent molecular weights of 60,000 and 54,000 daltons. Fluorescent visualization of GnRH receptors in these cells, utilizing a bioactive rhodamine derivative of the hormone, indicated that the fluorescently labeled receptors were initially distributed uniformly on the cell surface and then formed clusters which subsequently internalized (at 37 degrees C) into endocytic vesicles. These processes were dependent on specific binding sites for the rhodamine-labeled peptide on Leydig cells. These findings indicate further characterization of the testicular GnRH receptors and may have important implications towards the understanding of the molecular events involved in the action of the hormone in the testis.
利用125I标记的促性腺激素释放激素（GnRH）生物活性光亲和衍生物，鉴定纯化的大鼠睾丸间质细胞和膜制剂中的特异性GnRH受体蛋白。十二烷基硫酸钠聚丙烯酰胺凝胶电泳鉴定出两种特异性成分，其表观分子量分别为60,000和54,000道尔顿。利用该激素的生物活性罗丹明衍生物对这些细胞中的GnRH受体进行荧光可视化分析，结果表明，荧光标记的受体最初均匀分布在细胞表面，随后形成簇，这些簇随后（在37℃）内化到内吞小泡中。这些过程依赖于罗丹明标记肽在睾丸间质细胞上的特异性结合位点。这些发现进一步表征了睾丸GnRH受体，可能对理解该激素在睾丸中作用所涉及的分子事件具有重要意义。
