Regulation of sulfated glycoprotein-1 and cathepsin D expression in adult rat epididymis.
Regulation of sulfated glycoprotein-1 and cathepsin D expression in adult rat epididymis.
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DOI：
10.1002/j.1939-4640.2003.tb02690.x
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发表时间：
2003-05
影响因子：
--
通讯作者：
L. Hermo;S. Andonian
中科院分区：
文献类型：
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作者：
L. Hermo;S. Andonian
内吞作用，即蛋白质从附睾管腔内化并最终在溶酶体中降解，是附睾上皮细胞维持有利于精子成熟的适当管腔环境的主要功能之一。本研究采用光镜免疫细胞化学方法，研究了用Bouin固定液和石蜡包埋的成年大鼠附睾中2种溶酶体酶，硫酸糖蛋白-1 （SGP-1）和组织蛋白酶D的调控作用。在睾丸素(T)补充或不补充睾丸素(T)、传出管结扎（EDL）或垂体切除术(H)后，主要细胞的溶酶体与抗sgp -1抗体反应强烈，窄细胞、透明细胞和基底细胞也是如此，其染色模式与对照动物相似。这些实验过程也对所有细胞类型的组织蛋白酶D表达没有影响，除了附睾体和附睾尾的透明细胞，这些细胞在睾丸切除术和垂体切除术后变得强烈反应，而不像对照动物的完全无反应状态。在O+T动物和EDL动物中，透明细胞保持无反应。这些数据综合起来表明SGP-1的表达不受睾丸或垂体因子的控制，组织蛋白酶D在主细胞、窄细胞和基底细胞中的表达也是如此。然而，睾酮或其代谢物对组织蛋白酶D表达的特异性抑制似乎发生在附睾体和尾的透明细胞中。此外，除了小的、典型的溶酶体外，主细胞还显示出核上和核下的大球形结构，这些结构对抗sgp -1和抗组织蛋白酶D抗体都有免疫反应，表明它们是溶酶体。在电子显微镜下，这些结构呈现出电子透光，并且在电子密集的颗粒状背景中包含膜状轮廓。这些图像表明，各种实验程序对主要细胞中几种其他溶酶体酶的表达产生不利影响，导致溶酶体表型类似于在各种溶酶体贮积病中观察到的表型。
Endocytosis, whereby proteins are internalized from the epididymal lumen to be eventually degraded in lysosomes, is one of the major functions of the epididymal epithelial cells in maintaining a proper luminal milieu conducive for sperm maturation. In the present study, using light microscope immunocytochemical methods, we examined the regulation of 2 lysosomal enzymes, sulfated glycoprotein-1 (SGP-1) and cathepsin D, in adult rat epididymides fixed in Bouin fixative and embedded in paraffin. After orchidectomy (O) with or without testosterone (T) supplementation, efferent duct ligation (EDL), or hypophysectomy (H), lysosomes of principal cells were intensely reactive with the anti-SGP-1 antibody, as were narrow, clear, and basal cells, with staining patterns similar to that of control animals. These experimental procedures also had no effect on cathepsin D expression in all cell types, except for clear cells of the corpus and cauda epididymidis, which after orchiedectomy and hypophysectomy, became intensely reactive, unlike their completely unreactive state in control animals. In O+T animals, as well as in EDL animals, clear cells remained unreactive. These data taken together suggest that expression of SGP-1 is not under the control of testicular or pituitary factors, as is also the case for cathepsin D expression by principal, narrow, and basal cells. However, specific inhibition of cathepsin D expression by testosterone or one of its metabolites appears to occur in clear cells of the corpus and cauda epididymidis. Furthermore, in addition to small, typical lysosomes, principal cells also revealed large supranuclear and infranuclear spherical structures that were immunoreactive with both anti-SGP-1 and anti-cathepsin D antibodies, suggesting their lysosomal nature. With electron microscopy, these structures appeared electron-lucent and contained membranous profiles embedded in an electron-dense, granular background. Such images suggest that the various experimental procedures adversely affect the expression of several other lysosomal enzymes in principal cells, leading to a lysosomal phenotype similar to that observed in various lysosomal storage diseases.