Dean Jurrien
Laboratory of Cellular and Developmental Biology, NIDDK, Building 50, Room 3134, National Institutes of Health, 50 South Drive, Bethesda, Maryland 20892, USA.
Bioessays. 2004 Jan;26(1):29-38. doi: 10.1002/bies.10412.
The zona pellucida is an extracellular coat that surrounds mammalian eggs and early embryos. This insoluble matrix separates germ from somatic cells during folliculogenesis and plays critical roles during fertilization and early development. The mouse and human zona pellucida contain three glycoproteins (ZP1 or ZPB, ZP2, ZP3), the primary structures of which have been deduced by molecular cloning. Targeted mutagenesis of endogenous mouse genes and transgenesis with human homologues provide models to investigate the roles of individual zona components. Collectively, the genetic data indicate that no single mouse zona pellucida protein is obligatory for taxon-specific sperm binding and that two human proteins are not sufficient to support human sperm binding. An observed post-fertilization persistence of mouse sperm binding to "humanized" zona pellucida correlates with uncleaved ZP2. These observations are consistent with a model for sperm binding in which the supramolecular structure of the zona pellucida necessary for sperm binding is modulated by the cleavage status of ZP2.
透明带是一种围绕哺乳动物卵子和早期胚胎的细胞外被膜。这种不溶性基质在卵泡发生过程中将生殖细胞与体细胞分开,并在受精和早期发育过程中发挥关键作用。小鼠和人类的透明带含有三种糖蛋白(ZP1 或 ZPB、ZP2、ZP3),其一级结构已通过分子克隆推导得出。对内源性小鼠基因进行靶向诱变以及用人同源物进行转基因,为研究单个透明带成分的作用提供了模型。总体而言,遗传数据表明,没有单一的小鼠透明带蛋白对于物种特异性精子结合是必需的,并且两种人类蛋白不足以支持人类精子结合。观察到受精后小鼠精子与“人源化”透明带的持续结合与未切割的 ZP2 相关。这些观察结果与一种精子结合模型一致,在该模型中,精子结合所需的透明带超分子结构受 ZP2 的切割状态调节。