pubmed-article:10408833 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0699791 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C1518174 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0205161 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:10408833 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:10408833 | pubmed:issue | 3-4 | lld:pubmed |
pubmed-article:10408833 | pubmed:dateCreated | 1999-7-15 | lld:pubmed |
pubmed-article:10408833 | pubmed:abstractText | Dysfunction of the cadherin-catenin complex, a key component of adherens junctions, is thought to confer invasive potential to cells. The aim of this study is to examine the expression and function of the E-cadherin/catenin complex in gastric carcinoma cell lines. Expression of E-cadherin, alpha, beta and gamma-catenin and p120ctn, and of the adenomatous polyposis coli protein (APC), together with function of the cadherin-catenin complex was examined in a panel of gastric carcinoma cell lines, using immunocytochemistry, Western blotting and a cell-cell aggregation assay. Protein interactions were examined by sequential immunoprecipitation and immunoblotting with antibodies to E-cadherin, alpha, beta and gamma-catenin, p120ctn and APC. Abnormalities of E-cadherin, alpha- and beta-catenin expression, were associated with disturbance of E-cadherin-catenin complex composition, loss of membranous localization and loss of calcium-dependent aggregation in six gastric carcinoma cell lines. APC protein expression and interaction with beta-catenin was preserved in five cell lines. We demonstrate frequent abnormalities of expression and function of E-cadherin and catenins, and associated disturbance of E-cadherin-mediated intercellular adhesion in gastric carcinoma cell lines. These findings support the tumour suppressor role of the E-cadherin and its contribution to the development and progression of the neoplastic phenotype in gastric carcinoma. | lld:pubmed |
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pubmed-article:10408833 | pubmed:language | eng | lld:pubmed |
pubmed-article:10408833 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10408833 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10408833 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10408833 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10408833 | pubmed:month | May | lld:pubmed |
pubmed-article:10408833 | pubmed:issn | 0007-0920 | lld:pubmed |
pubmed-article:10408833 | pubmed:author | pubmed-author:FarthingM JMJ | lld:pubmed |
pubmed-article:10408833 | pubmed:author | pubmed-author:NodaMM | lld:pubmed |
pubmed-article:10408833 | pubmed:author | pubmed-author:PignatelliMM | lld:pubmed |
pubmed-article:10408833 | pubmed:author | pubmed-author:JawhariA UAU | lld:pubmed |
pubmed-article:10408833 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10408833 | pubmed:volume | 80 | lld:pubmed |
pubmed-article:10408833 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10408833 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10408833 | pubmed:pagination | 322-30 | lld:pubmed |
pubmed-article:10408833 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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