Carpino A, Romeo F, Rago V
Department of Cell Biology, Faculty of Pharmacy, University of Calabria, Italy.
J Anat. 2004 Mar;204(Pt 3):217-20. doi: 10.1111/j.0021-8782.2004.00272.x.
Abstract Cytochrome P450 aromatase is a terminal enzyme that catalyses the conversion of androgens into oestrogens. This study investigated the immunohistochemical localization of aromatase in human efferent ductules and proximal ductus epididymis using a mouse anti-human monoclonal P450arom IgG as primary antibody and a goat anti-mouse biotinylated IgG as secondary antibody. A strong immunoreaction was observed in the epithelial cell cytoplasm of both ductuli efferentes and proximal ductus epididymis, whereas the smooth muscle cells were immunonegative in the two regions. The results show, for the first time in humans, that epithelial cells of ductuli efferentes and proximal caput epididymis express aromatase, suggesting that locally produced oestrogens may have a role in epididymal function.
摘要 细胞色素P450芳香化酶是一种催化雄激素转化为雌激素的末端酶。本研究使用小鼠抗人单克隆P450arom IgG作为一抗,山羊抗小鼠生物素化IgG作为二抗,研究了芳香化酶在人输出小管和附睾近端导管中的免疫组织化学定位。在输出小管和附睾近端导管的上皮细胞质中均观察到强烈的免疫反应,而这两个区域的平滑肌细胞免疫阴性。结果首次在人类中表明,输出小管和附睾头近端的上皮细胞表达芳香化酶,提示局部产生的雌激素可能在附睾功能中起作用。