Source:http://linkedlifedata.com/resource/pubmed/id/10320932
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1999-6-29
|
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.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src),
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0067-8694
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
65
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
43-62
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:10320932-Amino Acid Sequence,
pubmed-meshheading:10320932-Animals,
pubmed-meshheading:10320932-Cadherins,
pubmed-meshheading:10320932-Cytoskeletal Proteins,
pubmed-meshheading:10320932-Extracellular Matrix,
pubmed-meshheading:10320932-Hepatocyte Growth Factor,
pubmed-meshheading:10320932-Humans,
pubmed-meshheading:10320932-Neoplasm Invasiveness,
pubmed-meshheading:10320932-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:10320932-Trans-Activators,
pubmed-meshheading:10320932-beta Catenin
|
pubmed:year |
1999
|
pubmed:articleTitle |
Extracellular regulation of cancer invasion: the E-cadherin-catenin and other pathways.
|
pubmed:affiliation |
Laboratory of Experimental Cancerology, University Hospital, Gent, Belgium.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|