The apical lamina of the sea urchin embryo: major glycoproteins associated with the hyaline layer.
The apical lamina of the sea urchin embryo: major glycoproteins associated with the hyaline layer.
复制标题
海胆胚胎的顶层：与透明层相关的主要糖蛋白。
DOI：
10.1016/0012-1606(82)90305-0
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发表时间：
1982
影响因子：
2.7
通讯作者：
Vacquier,VD
中科院分区：
文献类型：
--
作者：
Hall,HG;Vacquier,VD
海胆囊胚周围的透明层 (HL) 似乎溶解在 1Mglycine 中。然而，经过这种处理后，卵裂球的表面上仍然存在一层材料，这里称为顶层（AL），在胚胎逐渐解离时，它会像粘性回旋袋一样脱落。分离的透明层（称为 HL-AL 复合物）通过尿素-SDS-聚丙烯酰胺凝胶电泳进行分析。 HL-AL 复合物的主要蛋白质、透明蛋白、条带或沉淀在浓缩胶中。另外两种主要蛋白质均为 PAS 强阳性，其迁移表观分子量分别为 175K 和 145K 道尔顿。与完整胚胎一样，甘氨酸洗涤从分离的 HL-AL 复合物中去除透明蛋白，留下主要由 175K 和 145K 道尔顿蛋白组成的未溶解的 AL。胚胎自身位于卵黄周的皮质颗粒过氧化物酶对 HL-AL 复合物的蛋白质进行大量放射性碘化，进一步验证了它们的顶端细胞外位置。与透明蛋白不同，AL 蛋白不会与钙离子发生沉淀。与整个 HL-AL 复合物相比，AL 含有更高比例的碳水化合物。没有唾液酸与 HL-AL 复合物相关，但 AL 含有一些硫酸盐。与已发表的基于超微结构染色的报告相反，本研究中没有发现 HL-AL 复合物中存在胶原蛋白或重要糖胺聚糖的生化证据。与囊胚中的 AL 蛋白相比，1 小时胚胎中的 AL 蛋白没有观察到发育差异。然而，有证据表明玻璃蛋白存在异质性和发育差异。讨论了透明蛋白和 AL 蛋白可能组织成胚胎周围不同层的情况。考虑了 AL 蛋白在形态发生和细胞粘附中的影响，并且对 HL 和玻璃蛋白的假设作用提出了严格质疑。
The hyaline layer (HL) surrounding the sea urchin blastula appears to dissolve in 1Mglycine. However, after this treatment, there persists over the surfaces of the blastomeres a layer of material, referred to here as the apical lamina (AL), that sloughs off as an adhesive convoluted bag upon gradual dissociation of the embryo. Isolated hyaline layers, referred to as HL-AL complexes, were analyzed by urea-SDS-polyacrylamide gel electrophoresis. A major protein of the HL-AL complex, hyalin, bands or precipitates in the stacking gel. Two other major proteins, both strongly PAS positive, migrate with apparent molecular weights of 175K and 145K daltons. As with intact embryos, the glycine wash removes the hyalin protein from the isolated HL-AL complex, leaving the undissolved AL which consists primarily of the 175K- and 145K-dalton proteins. The embryo's own perivitelline-localized cortical granule peroxidase heavily radioiodinates the proteins of the HL-AL complex, further verifying their apical, extracellular location. Unlike hyalin, the AL proteins do not precipitate with calcium ions. Compared to the entire HL-AL complex, the AL contains a greater percentage of carbohydrate. No sialic acid is associated with the HL-AL complex, but the AL contains some sulfate. In contrast to a published report based on ultrastructural staining, no biochemical evidence was found in this study for the presence of collagen or significant glycosaminoglycan within the HL-AL complex. No developmental differences were observed in AL proteins from 1-hr-old embryos compared to those from blastulae. However, there is evidence suggesting heterogeneity and developmental differences in hyalin. The possible organization of hyalin and the AL proteins into separate layers surrounding the embryo is discussed. The influence of the AL proteins in morphogenesis and cell adhesion is considered, and hypothetical roles attributed to the HL and hyalin are critically questioned.