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首页> 外文期刊>Molecular reproduction and development >Differential expression of glycoside residues in the mammalian zonapellucida
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Differential expression of glycoside residues in the mammalian zonapellucida

机译：哺乳动物透明带中糖苷残基的差异表达

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The mammalian zona pellucida is an extracellular matrix surrounding the oocyte, and is com posed of three major glycoproteins, ZP1, ZP2, and ZP3. Previous studies have suggested that the sperm receptor activity of the zona pellucida resides in specific oligosaccharide chains on the ZP3 glycoprotein. However, the nature of the terminal monosaccharide(s) on these glycosidic chains to which sperm bind is a matter of active debate. Evidence has been presented to support a role for at least three distinct monosaccharides in sperm binding, alpha-galactose, L-fucose on Lewis X structures, and beta-N-acetylglucosamine. Previous studies have shown that beta-N-acetylglucosamine is uniformly distributed throughout the zona matrix. In this study, we have investigated the expression and distribution of alpha-galactose and fucose moieties during the maturation of the zona pellucida in mouse, rat, and hamster. Interestingly, alpha-galactose residues are expressed only during later stages of zona secretion and, consequently, are confined to the inner portions of the mature zona pellucida in mouse and rat. In hamster, alpha-galactose residues are only detectable in the zona pellucida of ovulated eggs, and are not found in ovarian oocytes. Fucosyl residues linked to Lewis X glycosides are not detectable at any stage of zona maturation in these three species, whereas fucose linked to N-linked core oligosaccharides are present throughout the zona. These studies indicate a previously unappreciated heterogeneity in the composition of zona glycosides. The specific localization of alpha-galactose residues to the inner portions of the zona matrix suggest a role in the later stages of sperm penetration through the zona. Finally, due to their absence from the zona surface, alpha-galactose and Lewis X fucosyl residues are not likely to be mediators of primary sperm binding. Mel. Reprod. Dev. 57:296-308, 2000.
机译：哺乳动物透明带是卵母细胞周围的细胞外基质，由三种主要糖蛋白ZP1，ZP2和ZP3组成。先前的研究表明，透明带的精子受体活性位于ZP3糖蛋白上的特定寡糖链中。然而，精子结合在这些糖苷链上的末端单糖的性质是一个有争议的问题。已有证据支持至少三种不同的单糖在精子结合中的作用，α-半乳糖，路易斯X结构上的L-岩藻糖和β-N-乙酰氨基葡萄糖。先前的研究表明，β-N-乙酰氨基葡糖均匀分布在整个透明带基质中。在这项研究中，我们研究了透明带在小鼠，大鼠和仓鼠中成熟过程中α-半乳糖和岩藻糖部分的表达和分布。有趣的是，仅在透明带分泌的后期才表达α-半乳糖残基，因此，α-半乳糖残基仅在小鼠和大鼠中局限于成熟透明带的内部。在仓鼠中，仅在排卵卵的透明带中可检测到α-半乳糖残基，而在卵巢卵母细胞中未发现。在这三个物种的透明带成熟的任何阶段都无法检测到与Lewis X糖苷连接的岩藻糖基残基，而与N连接的核心寡糖连接的岩藻糖则遍布整个透明带。这些研究表明，在透明带糖苷的组成中以前没有意识到的异质性。 α-半乳糖残基在透明带基质内部的特定定位表明在精子穿过透明带渗透的后期阶段中起作用。最后，由于它们在透明带表面的缺失，α-半乳糖和Lewis X岩藻糖基残基不太可能成为主要精子结合的介质。梅尔责备。开发人员57：296-308，2000。

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