Aquaporin-2 (AQP2) promotes renal cell migration by the modulation of integrin (31 trafficking and the turnover of focal adhesions. The aim of this study was to investigate whether AQP2 also works in cooperation with Na+/H+ exchanger isoform 1 (NHE1), another well-known protein involved in the regulation of cell migration. Our results showed that the lamellipodia of AQP2-expressing cells exhibit significantly smaller volumes and areas of focal adhesions and more alkaline intracellular pH due to increased NHE1 activity than AQP2-null cells. The blockage of AQP2, or its physically-associated calcium channel TRPV4, significantly reduced lamellipodia NHE1 activity. NHE1 blockage significantly reduced the rate of cell migration, the number of lamellipodia, and the assembly of F-actin only in AQP2-expressing cells. Our data suggest that AQP2 modulates the activity of NHE1 through its calcium channel partner TRPV4, thereby determining pH-dependent actin polymerization, providing mechanical stability to delineate lamellipodia structure and defining the efficiency of cell migration.
展开▼
机译：Aquaporin-2 (AQP2)促进肾细胞迁移整合素的调制(31贩卖焦粘连的营业额。研究旨在调查AQP2是否还有效在合作与Na + / H + 1换热器对碘氧基苯甲醚(NHE1),另一个知名的蛋白质参与细胞迁移的调控。表明AQP2-expressing的板状伪足细胞表现出明显的小卷领域的焦点粘连和碱性由于NHE1活动增加细胞内的pH值比AQP2-null细胞。其physically-associated钙通道TRPV4,显著降低板状伪足NHE1活动。NHE1堵塞率显著降低细胞迁移、板状伪足的数量和只在AQP2-expressing f -肌动蛋白的组装细胞。通过钙通道NHE1活动合作伙伴TRPV4,从而确定pH-dependent肌动蛋白聚合,提供机械描绘板状伪足结构和稳定定义细胞迁移的效率。
展开▼
