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海胆胚胎中细胞与棘皮粘连蛋白的组织特异性、时间性变化。

Tissue-specific, temporal changes in cell adhesion to echinonectin in the sea urchin embryo.

作者信息

Burdsal C A, Alliegro M C, McClay D R

机构信息

Department of Zoology, Duke University, Durham, North Carolina 27706.

出版信息

Dev Biol. 1991 Apr;144(2):327-34. doi: 10.1016/0012-1606(91)90425-3.

Abstract

Echinonectin is a dimeric, glycoprotein found in the hyaline layer of the developing sea urchin embryo. It was found that echinonectin supports adhesion of embryonic cells in vitro. Previous studies have shown that the protein hyalin also supports adhesion. The purpose of this study was to examine the specificity of cell-echinonectin interactions during sea urchin development. Primary mesenchyme cells (PMCs) ingress into the blastocoel during gastrulation. In the process the PMCs lose contact with the hyaline layer. It was found experimentally that differentiating PMCs decreased their adhesion to hyalin at the time of ingression. It was of interest, therefore, to determine whether there was a coordinate loss of adhesion to echinonectin at ingression as well. When cell-echinonectin interactions were quantified using a centrifugal force-based adhesion assay, it was shown that micromeres adhered well to echinonectin. At the time of ingression, PMCs displayed reduced adhesion to echinonectin just as had been found when hyalin was tested as a substrate. There was no change in adhesion of presumptive ectoderm or endoderm to echinonectin over the same time period. Early in gastrulation presumptive ectoderm and endoderm adhered to echinonectin only half as strongly as to equimolar concentrations of hyalin. After gastrulation endoderm cells were observed to retain the same relative affinity to hyalin and echinonectin, while ectoderm cells became equally adhesive for both hyalin and echinonectin. Quantitatively, this represents an overall increase in the affinity of ectodermal cells for echinonectin. Adhesion to combined substrata of echinonectin and hyalin was reduced but not abolished by monoclonal antibodies specific for echinonectin. The antibodies did not cross-react with hyalin. We conclude that both echinonectin and hyalin independently act as adhesive substrata for the developing sea urchin embryo. PMCs lose an affinity for echinonectin and ectodermal cells later increase their affinity for this substrate.

摘要

棘皮粘连蛋白是一种二聚体糖蛋白,存在于发育中的海胆胚胎的透明层中。研究发现,棘皮粘连蛋白在体外能支持胚胎细胞的黏附。先前的研究表明,透明蛋白也能支持黏附。本研究的目的是检测海胆发育过程中细胞与棘皮粘连蛋白相互作用的特异性。原肠胚形成期间,初级间充质细胞(PMC)进入囊胚腔。在此过程中,PMC与透明层失去接触。实验发现,正在分化的PMC在进入时降低了它们与透明蛋白的黏附。因此,确定在进入时是否也存在与棘皮粘连蛋白黏附的协同丧失是很有意义的。当使用基于离心力的黏附试验对细胞与棘皮粘连蛋白的相互作用进行定量时,发现小分裂球能很好地黏附于棘皮粘连蛋白。在进入时,PMC对棘皮粘连蛋白的黏附减少,这与以透明蛋白为底物时的情况相同。在同一时期,假定的外胚层或内胚层对棘皮粘连蛋白的黏附没有变化。在原肠胚形成早期,假定的外胚层和内胚层对棘皮粘连蛋白的黏附强度仅为等摩尔浓度透明蛋白的一半。原肠胚形成后,观察到内胚层细胞对透明蛋白和棘皮粘连蛋白保持相同的相对亲和力,而外胚层细胞对透明蛋白和棘皮粘连蛋白的黏附力变得相同。从数量上看,这代表外胚层细胞对棘皮粘连蛋白的亲和力总体增加。针对棘皮粘连蛋白的单克隆抗体可降低但不能消除对棘皮粘连蛋白和透明蛋白组合底物的黏附。这些抗体与透明蛋白不发生交叉反应。我们得出结论,棘皮粘连蛋白和透明蛋白均独立地作为发育中的海胆胚胎的黏附底物。PMC失去对棘皮粘连蛋白的亲和力,而外胚层细胞后来增加了对该底物的亲和力。

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