pubmed-article:7954478 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0042172 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0334227 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0108280 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C0001515 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C1524003 | lld:lifeskim |
pubmed-article:7954478 | lifeskim:mentions | umls-concept:C1517945 | lld:lifeskim |
pubmed-article:7954478 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:7954478 | pubmed:dateCreated | 1994-12-27 | lld:pubmed |
pubmed-article:7954478 | pubmed:abstractText | Cadherin cell adhesion molecules play an essential role in creating tight intercellular association and are considered to work as an invasion suppressor system of cancer cells. They form a molecular complex with catenins, a group of cytoplasmic proteins including alpha- and beta-catenins. While alpha-catenin has been demonstrated to be crucial for cadherin function, the role of beta-catenin is not yet fully understood. In this study, we analyzed the cadherin-catenin system in two human cell lines, HSC-39 and its putative subline HSC-40A, derived from a signet ring cell carcinoma of stomach. These cells grow as loose aggregates or single cells, suggesting that their cadherin system is not functional. In these cell lines, an identical 321-base pair in-frame mRNA deletion of beta-catenin was identified; this led to a 107-amino-acid deletion in the NH2-terminal region of the protein. Southern blot analysis disclosed a homozygous deletion in part of the beta-catenin gene. On the other hand, these cells expressed E-cadherin, alpha-catenin, and plakoglobin of normal size. Immunoprecipitation analyses showed that E-cadherin was coprecipitated with the mutated beta-catenin but not with alpha-catenin, and antibodies against beta-catenin did not copurify alpha-catenin. However, the recombinant fusion protein containing wild-type beta-catenin precipitated alpha-catenin from these cells. These results suggest that the dysfunction of E-cadherin in these cell lines is due primarily to its failure to interact with alpha-catenin, and that this defect results from the mutation in beta-catenin. Thus, it is most likely that the association between E-cadherin and alpha-catenin is mediated by beta-catenin, and that this process is blocked by NH2-terminal deletion in beta-catenin. These findings indicate that genetic abnormality of beta-catenin is one of the mechanisms responsible for loosening of cell-cell contact, and may be involved in enhancement of tumor invasion in human cancers. | lld:pubmed |
pubmed-article:7954478 | pubmed:language | eng | lld:pubmed |
pubmed-article:7954478 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954478 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7954478 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7954478 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954478 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7954478 | pubmed:month | Dec | lld:pubmed |
pubmed-article:7954478 | pubmed:issn | 0008-5472 | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:OyamaTT | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:OchiaiAA | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:WUT RTR | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:TsukitaSS | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:KanaiYY | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:ItoFF | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:YanagiharaKK | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:AkimotoSS | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:ShibamotoSS | lld:pubmed |
pubmed-article:7954478 | pubmed:author | pubmed-author:NagafuchiAA | lld:pubmed |
pubmed-article:7954478 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7954478 | pubmed:day | 1 | lld:pubmed |
pubmed-article:7954478 | pubmed:volume | 54 | lld:pubmed |
pubmed-article:7954478 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7954478 | pubmed:authorsComplete | N | lld:pubmed |
pubmed-article:7954478 | pubmed:pagination | 6282-7 | lld:pubmed |
pubmed-article:7954478 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:7954478 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7954478 | pubmed:articleTitle | A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines. | lld:pubmed |
pubmed-article:7954478 | pubmed:affiliation | Pathology Division, National Cancer Center Research Institute, Tokyo, Japan. | lld:pubmed |
pubmed-article:7954478 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7954478 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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