Immunolocalization of the fodrin, E-cadherin, and beta-catenin adhesion complex in infiltrating ductal carcinoma of the breast-comparison with an in vitro model.

@article{Sormunen1999ImmunolocalizationOT,
  title={Immunolocalization of the fodrin, E-cadherin, and beta-catenin adhesion complex in infiltrating ductal carcinoma of the breast-comparison with an in vitro model.},
  author={Raija T. Sormunen and Anthony S-y Leong and Jukka P V{\"a}{\"a}r{\"a}niemi and Suraj Shawn Fernando and Sinikka Eskelinen},
  journal={The Journal of pathology},
  year={1999},
  volume={187 4},
  pages={416-23}
}
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. In low-grade tumours, the staining patterns were similar for both fodrin and E-cadherin, with localization of these proteins to the cell membranes. beta-Catenin showed reduced membrane staining compared with non-neoplastic epithelium. High… CONTINUE READING

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CadherinsGene product plays role in biological processCell Adhesion
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 .
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 .
Plasma membraneIs associated anatomy of gene productCadherins
In low - grade tumours , the staining patterns were similar for both fodrin and E - cadherin , with localization of these proteins to the cell membranes .
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 .
Membranous localization of E - cadherin showed a positive correlation with oestrogen and progesterone expression , whereas loss of membranous E - cadherin and cytoplasmic accumulation of fodrin was more often observed in high - grade carcinomas and showed a positive correlation with p53 expression .
Membranous localization of E - cadherin showed a positive correlation with oestrogen and progesterone expression , whereas loss of membranous E - cadherin and cytoplasmic accumulation of fodrin was more often observed in high - grade carcinomas and showed a positive correlation with p53 expression .
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 .
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 .
Fodrin staining remained mostly membranous while that of E - cadherin and beta - catenin was fragmented and spiky .
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 .
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 , 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 .
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 .
Fodrin staining remained mostly membranous while that of E - cadherin and beta - catenin was fragmented and spiky .
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 .
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 , 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 .
beta cateninGene product plays role in biological processCell Adhesion
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 .
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