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首页> 外文期刊>Cell and Tissue Research >Immunohistochemical study of dissociation and association of adherens junctions in splenic sinus endothelial cells
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Immunohistochemical study of dissociation and association of adherens junctions in splenic sinus endothelial cells

机译：粘附结合在脾窦内皮细胞中粘附结的免疫组织化学研究

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摘要

It is not yet clear whether cellular junctions between splenic sinus endothelial cells are open or closed. In order to clarify this, immunolocalization of thrombomodulin (TM), endothelial protein C receptor (EPCR), protease-activated receptor 1 (PAR1), sphingosine 1-phosphate receptor 1 (S1P(1)), beta-catenin phosphorylated at Try142 (beta-catenin Y142) and beta-catenin phosphorylated at Try654 (beta-catenin Y654), which are related proteins that regulate dissociation and association of the adherens junctions of endothelial cells, are examined in rats using laser microscopy and electron microscopy. TM, EPCR, PAR1 and S1P(1) were colocalized in the entire circumference of the endothelial cells, as well as in the caveolar membranes and junctional membranes of adjacent endothelial cells. These molecules may protect the adherens junctions of the endothelial cells. On the other hand, beta-catenin Y142 and beta-catenin Y 654 colocalized with alpha-catenin and beta-catenin, respectively and in addition, beta-catenin Y142 and beta-catenin Y 654 were localized in the vicinity of the adherens junctions of the endothelial cells from immunogold electron microcopy. The adherens junctions are considered to be partially dissociated at the site where beta-catenin Y142 and beta-catenin Y 654 are localized. Thus, the system that protects the adherens junctions and the system that dissociates them may concurrently coexist in the endothelial cells and dissociation and association of the adherens junctions may be constantly repeated at the cell boundary of the endothelial cells.
机译：目前尚不清楚脾窦内皮细胞之间的细胞连接是开放的还是闭合的。为了阐明这一点，血栓调节蛋白（TM）、内皮蛋白C受体（EPCR）、蛋白酶激活受体1（PAR1）、鞘氨醇1-磷酸受体1（S1P（1））、在Try142处磷酸化的β-连环蛋白（β-连环蛋白Y142）和在Try654处磷酸化的β-连环蛋白（β-连环蛋白Y654）的免疫定位，在大鼠中使用激光显微镜和电子显微镜对调节内皮细胞粘附连接分离和结合的相关蛋白质进行了检查。TM、EPCR、PAR1和S1P（1）在内皮细胞的整个周长以及相邻内皮细胞的小窝膜和连接膜中共定位。这些分子可以保护内皮细胞的粘附连接。另一方面，β-连环蛋白Y142和β-连环蛋白Y 654分别与α-连环蛋白和β-连环蛋白共定位，此外，β-连环蛋白Y142和β-连环蛋白Y 654通过免疫金电子显微镜定位在内皮细胞贴壁连接附近。粘附连接被认为在β-连环蛋白Y142和β-连环蛋白Y 654定位的部位部分解离。因此，保护粘附连接的系统和分离粘附连接的系统可以同时共存于内皮细胞中，并且粘附连接的分离和结合可以在内皮细胞的细胞边界处不断重复。

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