Tabibzadeh S, Kong Q F, Satyaswaroop P G, Babaknia A
Department of Pathology, University of South Florida, Tampa, USA.
Hum Reprod. 1996 Mar;11(3):633-40. doi: 10.1093/humrep/11.3.633.
Human endometrium is a steroid-sensitive tissue and there is evidence that supports the viewpoint that heat shock proteins (HSP) are implicated in the regulation of steroid function. Therefore, in this study we examined the expression of various members of the heat shock family of proteins in the steroid-responsive human endometrium. Western blot analysis revealed that the expression of HSP90 showed minimal changes throughout the menstrual cycle. When normalized to the amount of HSP90, the expression of HSP27, HSP60 and the constitutive form of heat shock protein 70 (HSC70) increased progressively during the late proliferative and early secretory phases, and diminished in the mid- to late secretory and menstrual phases. In contrast, the inducible form of heat shock protein 70 (HSP70) did not undergo these changes. The cellular and subcellular localizations of these proteins were examined in human endometria by immunohistochemical staining. With the exception of HSP70, which was found primarily in the epithelial cells, the immunoreactivity for other heat shock proteins was found in both the stroma and the epithelium. Immunoreactivity for HSP27 was found in the lymphoid aggregates within endometrial stroma, and both HSP27 and HSP90 were found in endothelial cells. The immunoreactive heat shock proteins were found in the nuclei and/or cytoplasm of cells. However, no consistent nuclear versus cytoplasmic staining emerged, and such localization was irrespective of the site, the cell type or the phase of the menstrual cycle. Our findings show that endometrium has a full complement of heat shock proteins. The menstrual cycle-dependent changes in the amounts of heat shock protein suggest regulation by steroid hormones.
人类子宫内膜是一种对类固醇敏感的组织,有证据支持热休克蛋白(HSP)参与类固醇功能调节的观点。因此,在本研究中,我们检测了类固醇反应性人类子宫内膜中热休克蛋白家族各成员的表达。蛋白质印迹分析显示,HSP90的表达在整个月经周期中变化极小。以HSP90的量进行标准化后,HSP27、HSP60和组成型热休克蛋白70(HSC70)的表达在增殖晚期和分泌早期逐渐增加,在分泌中期至晚期及月经期减少。相比之下,诱导型热休克蛋白70(HSP70)未发生这些变化。通过免疫组织化学染色在人类子宫内膜中检测了这些蛋白的细胞和亚细胞定位。除主要在上皮细胞中发现的HSP70外,其他热休克蛋白在基质和上皮中均有免疫反应性。在子宫内膜基质内的淋巴聚集物中发现了HSP27的免疫反应性,在内皮细胞中同时发现了HSP27和HSP90。免疫反应性热休克蛋白存在于细胞的细胞核和/或细胞质中。然而,未出现一致的细胞核与细胞质染色情况,且这种定位与部位、细胞类型或月经周期阶段无关。我们的研究结果表明,子宫内膜具有完整的热休克蛋白。热休克蛋白量的月经周期依赖性变化提示受类固醇激素调节。