Expression of Cadherin‐Catenin Cell Adhesion Molecules, Phosphorylated Tyrosine Residues and Growth Factor Receptor‐tyrosine Kinases in Gastric Cancers
| Autor: | Shingo Akimoto, Atsushi Ochiai, Masafumi Inomata, Setsuo Hirohashi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
Cancer Research
Protein tyrosine phosphatase Biology Receptor tyrosine kinase Article Tyrosine phosphorylation chemistry.chemical_compound Stomach Neoplasms Cell Adhesion Humans Receptors Growth Factor Tyrosine Phosphorylation Phosphotyrosine beta Catenin β‐Catenin Staining and Labeling GRB7 Receptor Protein-Tyrosine Kinases Cadherins Molecular biology key words Immunohistochemistry Neoplasm Proteins Cytoskeletal Proteins Oncology chemistry Biochemistry biology.protein Undifferentiated gastric cancer Trans-Activators Cadherin‐mediated cell adhesion Tyrosine kinase Platelet-derived growth factor receptor |
| Zdroj: | Japanese Journal of Cancer Research : Gann |
| ISSN: | 1876-4673 0910-5050 |
| Popis: | Tyrosine phosphorylation of beta-catenin, an intracytoplasmic E-cadherin-binding protein, has been shown to disrupt the cadherin-mediated cell adhesion system in vitro. In order to investigate the relationships of expression and tyrosine phosphorylation of cadherin-catenin molecules and expression of growth factor receptor-tyrosine kinase with loose cell-to-cell adhesion, immunohistochemical staining for E-cadherin, alpha- and beta-catenin, phosphorylated tyrosine residues and tyrosine kinase receptors, including c-erbB-2, epidermal growth factor-receptor (EGF-R), c-met and K-sam, in 17 undifferentiated- and 10 differentiated-type human gastric cancers was performed. Loss or reduced expressions of E-cadherin and alpha- and beta-catenin (11, 11, 10 cancers, respectively) were observed in the former, but not the latter. Diffuse cytoplasmic staining of E-cadherin, alpha- and beta-catenin and phosphotyrosine residues was observed frequently in the undifferentiated-type cancers. The cytoplasmic localization of phosphotyrosine residues in undifferentiated-type cancers was correlated significantly with K-sam expression (P0.01) and diffuse cytoplasmic staining of E-cadherin (P0.05) and beta-catenin (P0.05). Expression of K-sam protein was detected significantly more frequently in undifferentiated- (6/17; P0.05) than differentiated-type adenocarcinomas whereas the converse applied to c-erbB-2 expression (8/10 of the latter, P0.05). Tyrosine phosphorylation of beta-catenin was directly confirmed in the protein extracts of one undifferentiated-type gastric cancer. These data indicate that alteration of tyrosine phosphorylation status associated with K-sam expression may cause the cytoplasmic distribution of cadherin-catenin molecules and loose cell-cell adhesion in undifferentiated-type gastric cancers. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text