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siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis

机译:siRNA介导的Hep3B细胞中37 / 67-kDa高亲和力层粘连蛋白受体的沉默诱导凋亡

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摘要

The laminin-binding protein, variously called the 37/67-kDa high affinity laminin receptor or p40, mediates the attachment of normal cells to the laminin network, and also has a role as a ribosomal protein. Over-expression of this protein has been strongly correlated with the metastatic phenotype. However, few studies have investigated the cellular consequence of the ablation of this gene’s expression. To address this issue, the expression of the 37/67-kDa high affinity laminin receptor was knocked out with several siRNA constructs via RNA interference in transformed liver (Hep3B) cells. In each case where the message was specifically ablated, apoptosis was induced, as determined by annexin V/propidium iodide staining, and by double staining with annexin V and an antibody directed against the 37/67-kDa high affinity laminin receptor. These results suggest that this protein plays a critical role in maintaining cell viability.
机译:层粘连蛋白结合蛋白(也称为37 / 67-kDa高亲和力层粘连蛋白受体或p40)介导正常细胞与层粘连蛋白网络的附着,并具有核糖体蛋白的作用。该蛋白的过表达与转移表型密切相关。但是,很少有研究调查该基因表达被切除后的细胞结果。为了解决这个问题,通过转化肝细胞(Hep3B)中的RNA干扰,用几种siRNA构建体敲除了37 / 67-kDa高亲和层粘连蛋白受体的表达。在每种情况下,信息均被特异性消除,通过膜联蛋白V /碘化丙啶染色,以及通过膜联蛋白V和针对37 / 67-kDa高亲和力层粘连蛋白受体的抗体进行双重染色,可以诱导凋亡。这些结果表明该蛋白在维持细胞活力中起关键作用。

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