小鼠受精的分子基础

David J. Miller, Barry D. Shur
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引用次数: 15

摘要

最近对小鼠受精的研究发现了两个互补的配子受体,它们介导精子与卵子的结合。精子表面β1,4-半乳糖转移酶(GalTase)与卵膜(透明带)糖蛋白ZP3的特异性低聚糖结合。有证据表明,这些分子可能会刺激精子的顶体反应。顶体反应后,精子被认为通过结合另一种糖蛋白ZP2而附着在带上。顶体反应的精子释放水解酶,包括顶体酶和n -乙酰氨基葡萄糖酶,使其能够穿透透明带。穿透后的精子与卵膜结合并激活发育后,n -乙酰氨基葡萄糖酶从卵皮质颗粒中胞外分泌,作为多精带阻断的一部分,从ZP3低聚糖中整体去除精子GalTase结合位点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Molecular basis of fertilization in the mouse

Recent studies of mouse fertilization have identified two complementary gamete receptors that mediate sperm-egg binding. Sperm surface β1,4-galactosyltransferase (GalTase) binds to specific oligosaccharides of the egg coat (zona pellucida) glycoprotein ZP3. Evidence suggests that these same molecules may stimulate the acrosome reaction in sperm. After the acrosome reaction, it is thought that sperm remain adherent to the zona by binding another glycoprotein, ZP2. The acrosome-reacted sperm releases hydrolytic enzymes, including acrosin and N-acetylglucosaminidase, enabling it to penetrate the zona pellucida. After the penetrating sperm binds to the egg membrane and activates development, N-acetylglucosaminidase is exocytosed from egg cortical granules and, as part of the zona block to polyspermy, globally removes the sperm GalTase binding site from ZP3 oligosaccharides.

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