OBJECTIVE To investigate the relationship between p 120^ctn translocation and hepatocellular carcinoma cell malignant features and the relationship between p 120^ctn and β-catenin translocation in cell signaling. METHODS Human hepatocellular carcinoma cells were over expressed with p120^ctn isoform 3A using a DNA transfection method. The effects of transfection and expression of p120^ctn and its binding capacity to E-cadherin were examined using immunoprecipitation and immunoblotting methods. p120^ctn subcellular localization and its relation with β-catenin were detected using immunofluorescent microscopy, p120^ctn phosphorylation was produced by EGF treatment. Cell adhesion, cell migration and cell proliferation were also examined in this study. RESULTS We found that p 120^ctn expression was increased after transfection and the binding capacity of p120^ctn to E-cadherin was enhanced. Tyrosine phosphorylation of p120^ctn increased after transfection and EGF treatment. p120^ctn and β-catenin cellular localization displayd a membrane and cytoplasmic expression pattern, but they translocated into the nucleus for relocalization after p120^ctn overexpression plus EGF stimulation. Cell adhesion ability was increased and migration ability reduced after transfection without EGF. Following transfection without EGF cellular proliferation was reduced, but increased after EGF treatment. CONCLUSION Our results suggest that p120^ctn plays an important role in hepatocellular carcinoma cell adhesion, migration and proliferation. In addition there is a relationship between p120^ctn and β-catenin subcellular localization and signaling.
