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首页> 外文期刊>Human Reproduction >Native human zona pellucida glycoproteins: purification and binding properties.
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Native human zona pellucida glycoproteins: purification and binding properties.

机译：天然人透明带糖蛋白：纯化和结合特性。

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BACKGROUND: Fertilization starts with the binding of the spermatozoa to the zona pellucida (ZP) of the oocyte. Such binding is a carbohydrate-mediated event and consists of a series of tightly regulated events. Molecular interactions between spermatozoon and ZP in human are not well characterized due to limited availability of oocytes for research. Our current technology cannot generate recombinant human ZP (hZP) glycoproteins with native glycosylation. METHODS AND RESULTS: In this study, hZP glycoproteins, hZP2 (approximately 120 kDa), hZP3 (approximately 58 kDa) and hZP4 (approximately 65 kDa) were purified from ZP (purity 88%) by immunoaffinity columns. The binding sites of the purified native hZP3 and hZP4 were localized to the acrosome region of the capacitated human spermatozoa, and were lost after acrosome reaction. Purified human hZP2 bound to this region only in acrosome-reacted spermatozoa. Differential binding of the three glycoproteins to the post-acrosomal region and the midpiece of the spermatozoa was observed. In addition, hZP3, but not hZP2 and hZP4, induced hyperactivation. The stimulatory activity was dependent partly on N-linked glycosylation of hZP3. CONCLUSIONS: This manuscript describes the biological activities of purified hZP glycoproteins from the native source for the first time.
机译：背景：受精始于精子与卵母细胞透明带（Zona pellucida，ZP）的结合。这种结合是碳水化合物介导的事件，由一系列严格调控的事件组成。由于研究用卵母细胞的有限性，人类精子与ZP之间的分子相互作用尚不能很好地表征。我们当前的技术无法生成具有天然糖基化作用的重组人ZP（hZP）糖蛋白。方法和结果：在这项研究中，通过免疫亲和柱从ZP（纯度> 88％）中纯化了hZP糖蛋白，hZP2（约120kDa），hZP3（约58kDa）和hZP4（约65kDa）。纯化的天然hZP3和hZP4的结合位点定位于获能的人精子的顶体区域，并在顶体反应后丢失。纯化的人hZP2仅在顶体反应的精子中结合到该区域。观察到三种糖蛋白与精子后区域和中段的差异结合。此外，hZP3而非hZP2和hZP4诱导​​了过度激活。刺激活性部分取决于hZP3的N-联糖基化。结论：该手稿首次描述了从天然来源纯化的hZP糖蛋白的生物学活性。

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