MTA1 regulates E-cadherin through the phosphorylation and activation of AKT (p-AKT).

<p>(A) A Western blotting analysis showed that treatment with MTA1 siRNA could inhibit AKT phosphorylation after a 48 hours siRNA treatment. An asterisk (*) and diamond (◊) indicates a statistically significant difference (p<0.05) in the MTA1 and E-cadherin levels, respectively, compared with the negative-control siRNA-transfected cells. (B) The cells were incubated with either the p-AKT inhibitor wortmannin (100 nM) or DMSO for various times from 24 hours to 48 hours, and the cellular proteins were extracted. A Western blotting analysis showed that wortmannin treatment promoted the expression of E-cadherin and inhibited the expression of MTA1 after 24 hours. An asterisk (*), diamond (◊), or triangle (Δ) indicates a statistically significant difference (p<0.05) in the MTA1, E-cadherin or p-AKT levels, respectively, compared with the DMSO-treated cells. (C) The forced over expression of p-AKT by transient transfection of the myr-AKT plasmid decreased the expression of E-cadherin and increased the expression of MTA1 after 24 hours. The quantification of the bands is shown (top). (D) The cells were transfected with MTA1 siRNA in the presence or absence of the myr-AKT plasmid or wortmannin for 48 hours. A Western blotting analysis was used to evaluate the changes in E-cadherin expression. An asterisk (*), diamond (◊), or triangle (Δ) indicates a statistically significant difference (p<0.05) in the MTA1, E-cadherin or p-AKT levels, respectively, compared with the negative-control siRNA-transfected cells. The quantification of the bands intensities is shown (top). All experiments were repeated three times.