After 60min of src activation , fodrin localized completely in the cell cytoplasm , while E - cadherin and beta - catenin were partly cytoplasmic with fragmented and spiky membranous staining .
In a v - src - transformed MDCK cell line , following 15min of src activation , beta - catenin began to detach from the cell membrane and localize to the cytoplasm , while fodrin and E - cadherin remained unchanged .
Fodrin , E - cadherin , and beta - catenin immunolocalization was studied in 54 cases of infiltrating ductal carcinoma of the breast and compared with an in vitro model in order to study the dynamic relationship between these components of an adhesion complex .
Both in vivo and in vitro findings clearly demonstrated a disruption of the E - cadherin / beta - catenin / fodrin / cytoskeleton linkage concomitant with the loss of cell - to - cell adhesion and change in cell shape , from epithelioid to a fibroblastoid phenotype .
Immunolocalization of the fodrin , E - cadherin , and beta - catenin adhesion complex in infiltrating ductal carcinoma of the breast - comparison with an in vitro model .
Fodrin staining remained mostly membranous while that of E - cadherin and beta - catenin was fragmented and spiky .