...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The FEBS journal >Analysis of the stability of the spermadhesin PSP-I/PSP-II heterodimer - Effects of Zn2+ and acidic pH
【24h】

Analysis of the stability of the spermadhesin PSP-I/PSP-II heterodimer - Effects of Zn2+ and acidic pH

机译：精豆粘蛋白PSP-I / PSP-II异二聚体的稳定性分析-Zn2 +和酸性pH的影响

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Spermadhesins are a family of 12-16 kDa proteins with a single CUB domain. PSP-I and PSP-II, the most abundant boar spermadhesins, are present in seminal plasma as a noncovalent heterodimer. Dimerization markedly affects the binding ability of the subunits. Notably, heparin and mannose 6-phosphate binding abilities of PSP-II are abolished, indicating that the corresponding binding sites may be located at ( or near) the dimer interface. Pursuing the hypothesis that cryptic binding sites in PSP-I/PSP-II may be exposed in specific physiological environments, we examined the influence of Zn2+ and acidic pH on the heterodimer stability. According to near-UV CD spectra, the core native fold is preserved in the presence of physiological concentrations of Zn2+, a cation unusually abundant in boar seminal plasma. However, the thermostability of the heterodimer decreases significantly, as observed by CD and differential scanning calorimetry. The effect is Zn2+-specific and is reversed by EDTA. Destabilization is also observed at acidic pH. Gel filtration analysis using radioiodinated PSP-I/PSP-II reveals that dissociation of the heterodimer at low (nanomolar) protein concentrations is promoted by both Zn2+ and acidic pH. Although the integrity of the heterodimer in seminal plasma seems to be guaranteed by its high concentration, dissociation may be facilitated in the female genital tract because of dilution of the protein in the intraluminal fluids of the cervix and the uterus, and the acidic fluid of the uterotubal junction. Such a mechanism may be relevant in the regulation of uterine immune reactions.
机译：精豆粘附素是具有单个CUB结构域的12-16 kDa蛋白家族。 PSP-I和PSP-II是最丰富的公猪精粘附素，以非共价异二聚体的形式存在于精浆中。二聚化显着影响亚基的结合能力。值得注意的是，PSP-II的肝素和甘露糖6-磷酸结合能力被取消，表明相应的结合位点可能位于二聚体界面处（或附近）。根据PSP-I / PSP-II中隐含结合位点可能在特定生理环境中暴露的假设，我们研究了Zn2 +和酸性pH对异二聚体稳定性的影响。根据近紫外CD光谱，在生理浓度的Zn2 +（一种在公猪精浆中异常丰富的阳离子）的存在下，保留了核心天然折叠。然而，如通过CD和差示扫描量热法所观察到的，异二聚体的热稳定性显着降低。该效应是Zn2 +特异的，并且被EDTA逆转。在酸性pH下也观察到不稳定。使用放射性碘化的PSP-I / PSP-II进行的凝胶过滤分析表明，Zn2 +和酸性pH均可促进低（纳摩尔）蛋白质浓度下异二聚体的解离。尽管异二聚体在精浆中的完整性似乎可以通过其高浓度来保证，但由于该蛋白在子宫颈和子宫的腔内液中以及该蛋白的酸性液中的稀释，可能有助于女性生殖道的解离。子宫管交界处。这种机制可能与子宫免疫反应的调节有关。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号