Lian G, Enders G C
Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City 66160-7400.
J Androl. 1994 Jan-Feb;15(1):52-60.
While entactin has been recently reported in the mouse seminiferous tubule lamina propria at the light microscope level, the purpose of this paper was twofold: 1) to determine the ultrastructural localization of entactin with the two basal laminae that form the lamina propria of the mouse, and 2) to determine if immunoreactive entactin changes following hypophysectomy. The localization of entactin was demonstrated by three different means: 1) immunofluorescent localization in semi-thin cryosections of the testis, 2) immunoperoxidase staining in a preparation of isolated lamina propria, and 3) immuno-gold staining in ultra-thin sections of testis. These techniques all demonstrated that immunoreactive entactin is present in both the inner and outer basal laminae of the mouse seminiferous tubules and is co-localized with laminin. These results are consistent with previous work that demonstrated entactin is synthesized and secreted by both Sertoli and peritubular myoid cells. Because both Sertoli cells and peritubular myoid cells are androgen-responsive cells, we wanted to determine if hypophysectomy alters the testicular distribution of entactin. Changes in immunoreactive entactin and laminin in the basal laminae were observed in semi-thin cryosections of the testes from hypophysectomized mice up to 6 weeks after surgery. The results demonstrated that during this time period, while most of the spermatogenic cells degenerated, the intensity of immunoreactive entactin and laminin remained nearly unchanged, as the seminiferous tubule basal laminae took on an increasingly wavy appearance. This suggests that the relative concentration of entactin and laminin in the basal lamina is stable, and not dependent on the presence of normal spermatogenesis and pituitary hormones.
虽然最近在光镜水平上已报道巢蛋白存在于小鼠生精小管固有层中，但本文有两个目的：1）确定巢蛋白在构成小鼠固有层的两个基底层中的超微结构定位，2）确定垂体切除术后免疫反应性巢蛋白是否发生变化。通过三种不同方法证明了巢蛋白的定位：1）在睾丸半薄冰冻切片中的免疫荧光定位，2）在分离的固有层制剂中的免疫过氧化物酶染色，3）在睾丸超薄切片中的免疫金染色。这些技术均表明，免疫反应性巢蛋白存在于小鼠生精小管的内、外基底层中，并与层粘连蛋白共定位。这些结果与先前的研究一致，先前研究表明巢蛋白由支持细胞和睾丸肌样细胞合成并分泌。由于支持细胞和睾丸肌样细胞均为雄激素反应性细胞，我们想确定垂体切除是否会改变巢蛋白在睾丸中的分布。在垂体切除术后长达6周的小鼠睾丸半薄冰冻切片中，观察到基底层中免疫反应性巢蛋白和层粘连蛋白的变化。结果表明，在此时间段内，虽然大多数生精细胞退化，但免疫反应性巢蛋白和层粘连蛋白的强度几乎保持不变，而生精小管基底层呈现出越来越明显的波浪状外观。这表明基底层中巢蛋白和层粘连蛋白的相对浓度是稳定的，不依赖于正常生精过程和垂体激素的存在。
