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为了研究蛋白激酶B (PKB)对上皮钙粘着蛋白 (E cadherin)的调节 ,使用了用胰岛素处理的野生型SMMC 772 1细胞及稳定表达持续激活PKB的SMMC 772 1细胞株 (Gag PKB/SMMC 772 1) .用RNA印迹法和蛋白质印迹法检测细胞E cadherin表达 ,发现通过胰岛素刺激或在细胞中表达持续激活PKB从而增加PKB活性 ,不影响E cadherin的转录和蛋白质合成 ,但用流式细胞术和免疫荧光定位E cadherin ,则发现PKB活性增加能明显驱动E cadherin到细胞表面 ,从而导致部分通过E cadherin途径的细胞粘聚增加和细胞调亡的抑制 .因此 ,我们提供新的证据表明 ,增加PKB活性可驱动有功能的E cadherin分子到细胞表面 .
To investigate the regulation of E cadherin by protein kinase B (PKB), wild-type SMMC 772 1 cells treated with insulin and SMMC 772 1 cell line stably expressing PKB (Strain Gag PKB / SMMC 772 1) .E-cadherin expression was detected by Northern blotting and Western blotting, and it was found that PKB activity was enhanced by insulin stimulation or expression in cells, which did not affect the transcription and protein synthesis of E cadherin. However, flow cytometry And immunofluorescence mapping of E cadherin, it was found that an increase in PKB activity can significantly drive E cadherin to the cell surface, resulting in increased cell cohesion and inhibition of apoptosis through the E cadherin pathway.Thus, we provide new evidence that increasing PKB activity drives functional E cadherin molecules to the cell surface.