The interaction between β-catenin, GSK3β and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer
- G. Davies
- W. G. Jiang
- M. D. Mason
- Corresponding author:
Published online on: Sunday, April 1, 2001
The effect of HGF/SF was examined on the interactions between APC, GSK3β and β-catenin in prostate cancer cells LNCapFGC (E-cadherin positive) and PC-3 (E-cadherin negative). Using immunoprecipitation, APC was found to be co-precipitated with either GSK3β or β-catenin in both cell lines. Stimulation with HGF/SF showed no change in the co-precipitation status of these protein molecules. In contrast, co-precipitation between GSK3β and β-catenin was only observed in LNCapFGC cells, and increased upon continued exposure to the motogen HGF/SF. Furthermore, using immunofluorescence, stimulation with HGF/SF was found to increase the level of co-localised cytoplasmic staining between β-catenin and GSK3β, in prostate cancer cells. RT-PCR revealed that there were no mutations within the binding regions between β-catenin and GSK3β. It is concluded, that uncomplexed cytoplasmic pools of β-catenin associate more readily with the Axin complex in the absence of E-cadherin. Whereas, in the presence of E-cadherin, β-catenin is stabilised by forming tight cell-cell contacts which may influence the invasive potential of cancer cells.