| pubmed-article:10320932 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C0006826 | lld:lifeskim |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C2699153 | lld:lifeskim |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C1269955 | lld:lifeskim |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:10320932 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10320932 | pubmed:dateCreated | 1999-6-29 | lld:pubmed |
| pubmed-article:10320932 | pubmed:abstractText | The E-cadherin-catenin complex is pivotal for the regulation of cancer invasion. It not only serves cell-cell adhesion but also transduces signals from the micro-environment to other molecular complexes possibly implicated in invasion. Both functions are disturbed when the extracellular part of E-cadherin is cleaved off. Moreover, upon release into the environment, the E-cadherin fragments may interfere with intact complexes, as indicated by experiments with His-Ala-Val (HAV)-containing peptides that are homologous to parts of the first extracellular domain of E-cadherin. Scatter factor/hepatocyte growth factor (SF/HGF), on binding to its c-met tyrosine kinase receptor, can induce invasion through tyrosine phosphorylation of beta-catenin. SF/HGF-induced invasion is also associated with phosphorylation of pp125FAK, and both invasion and phosphorylation are inhibited by platelet-activating factor (PAF). Activation of the membrane-bound non-receptor tyrosine kinase pp60src can also induce invasion. Signal transduction pathways starting from pp60src include E-cadherin-associated beta-catenin as well as the focal adhesion kinase pp125FAK. Whereas all invasion-inducing pathways implicate phosphoinositide 3-kinase, the PAF pathway seems to be E-cadherin-catenin-independent. We conclude that cancer cell invasion is regulated by paracrine and autocrine factors that are released upon cross-talk with the host cells. | lld:pubmed |
| pubmed-article:10320932 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10320932 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10320932 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10320932 | pubmed:issn | 0067-8694 | lld:pubmed |
| pubmed-article:10320932 | pubmed:author | pubmed-author:MareelMM | lld:pubmed |
| pubmed-article:10320932 | pubmed:author | pubmed-author:GespachCC | lld:pubmed |
| pubmed-article:10320932 | pubmed:author | pubmed-author:BruyneelEE | lld:pubmed |
| pubmed-article:10320932 | pubmed:author | pubmed-author:ChastreEE | lld:pubmed |
| pubmed-article:10320932 | pubmed:author | pubmed-author:NoéTT | lld:pubmed |
| pubmed-article:10320932 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10320932 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:10320932 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10320932 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10320932 | pubmed:pagination | 43-62 | lld:pubmed |
| pubmed-article:10320932 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:meshHeading | pubmed-meshheading:10320932... | lld:pubmed |
| pubmed-article:10320932 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10320932 | pubmed:articleTitle | Extracellular regulation of cancer invasion: the E-cadherin-catenin and other pathways. | lld:pubmed |
| pubmed-article:10320932 | pubmed:affiliation | Laboratory of Experimental Cancerology, University Hospital, Gent, Belgium. | lld:pubmed |
| pubmed-article:10320932 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10320932 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:10320932 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10320932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10320932 | lld:pubmed |
