Fig. 5
6G increases the interaction between VEGFR2 and VE-cad/β-catenin and enhances complex-regulated F-actin remodeling. a VEGFR2/VE-cad complex strongly interacted with β-catenin in response to VEGFa, and 6G increased this interaction. b 6G increased the phosphorylation of VEGFR2 and increased its interaction with VE-cad. c Knock down VEGFR2, VE-cadherin and β-catenin in HUVECs. There was no correlation between the expression of VEGFR2, VE-cad and β-catenin. e VEGFR2, VE-cad and β-catenin physically interact with one another, and β-catenin acts as a “bridge” to connect activated VEGFR2 and VE-cad. f Confocal image of VE-cad, VEGFR2 and β-catenin. Results demonstrated that there were significant co-localization of VE-cad, VEGFR2 and β-catenin in the cell membrane. g Distance of pseudopodium and co-localization ratio of cells in control, VEGFa and VEGFa/6G group. *, P < 0.05; **, P < 0.01, one-way ANOVA. h Single-molecule imaging of VEGFR2, VE-cad and β-catenin. VEGFR2/VE-cad/β-catenin complex was formed at the cell membrane, and this was enhanced by 6G. i Schematic showed the interaction of p-VEGFR2 with VE-cad and β-catenin induced alterations in F-actin organization to regulate cellular extensions in HUVECs. Results were obtained from three independent experiments, each performed in triplicate, and the error bars represent SD (*P < 0.05, **P < 0.01)