Fournet-Dulguerov N, MacLusky N J, Leranth C Z, Todd R, Mendelson C R, Simpson E R, Naftolin F
Department of Obstetrics and Gynecology, Yale University School of Medicine, New Haven, Connecticut 06510.
J Clin Endocrinol Metab. 1987 Oct;65(4):757-64. doi: 10.1210/jcem-65-4-757.
Immunohistochemistry employing immunoglobulin G fractions raised against aromatase cytochrome P-450 and antiserum against 17 beta-estradiol dehydrogenase was used to localize these two steroid-converting enzymes in the human placenta. Immunostaining for both enzymes was found exclusively in the syncytiotrophoblast, while the underlying cytotrophoblast and the villus core did not stain. Ultrastructural examination of aromatase cytochrome P-450- and 17 beta-estradiol dehydrogenase-labeled sections disclosed immunoreactive product in the membranes of the endoplasmic reticulum; the nucleus, mitochondria, Golgi apparatus, and secretory granules were free of staining. These findings suggest that the syncytiotrophoblast is actively involved in the synthesis and metabolism of estrogens and in their role in placental endocrine function.
利用针对芳香化酶细胞色素P-450产生的免疫球蛋白G片段和抗17β-雌二醇脱氢酶抗血清进行免疫组织化学，以在人胎盘中定位这两种类固醇转化酶。发现这两种酶的免疫染色仅存在于合体滋养层中，而其下方的细胞滋养层和绒毛核心未染色。对芳香化酶细胞色素P-450和17β-雌二醇脱氢酶标记切片的超微结构检查显示，免疫反应产物存在于内质网的膜中；细胞核、线粒体、高尔基体和分泌颗粒均无染色。这些发现表明，合体滋养层积极参与雌激素的合成和代谢及其在胎盘内分泌功能中的作用。
