Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2-3
|
| pubmed:dateCreated |
1997-9-23
|
| pubmed:abstractText |
The urokinase receptor (u-PAR), a protein anchored to cell membrane by a glycosyl phosphatidylinositol, plays a central role in cancer cell invasion and metastasis by binding urokinase plasminogen activator (u-PA), thereby facilitating plasminogen activation. Plasmin can promote cell migration either directly or by activating metalloproteinases that degrade some of the components of the extra cellular matrix. However, the IGR-OV1-Adria cell line contains the u-PAR but does not migrate even in the presence of exogenous u-PA, although the parental IGR-OV1 cell line migrates normally in the presence of u-PA. We therefore investigated the role of cell signalling for u-PA induced cell locomotion. We show that cell migration induced by u-PA-u-PAR complex is always associated with tyrosine kinase activation for the following reasons: (1) the blockade of the u-PAR by a chimeric molecule (albumin-ATF) inhibits not only the u-PA-induced cell migration, but also the signalling in IGR-OV1 line; (2) the binding of u-PA to u-PAR on non-migrating IGR-OV1-Adria cells was not associated with tyrosine kinase activation; (3) the inhibition of tyrosine kinase also blocked cell migration of IGR-OV1. Therefore tyrosine kinase activation seems to be essential for the u-PA-induced cell locomotion possibly by the formation of a complex u-PAR-u-PA with a protein whose transmembrane domain can ensure cell signalling. Thus, IGR-OV1 and IGR-OV1-Adria cell lines represent a good model for the analysis of the mechanism of u-PA-u-PAR-induced cell locomotion.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinolysin,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/PLAUR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Plasminogen Activator Inhibitor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Urokinase Plasminogen...,
http://linkedlifedata.com/resource/pubmed/chemical/Urokinase-Type Plasminogen Activator
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
14
|
| pubmed:volume |
411
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
322-6
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9271229-Blotting, Western,
pubmed-meshheading:9271229-Cell Movement,
pubmed-meshheading:9271229-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:9271229-Female,
pubmed-meshheading:9271229-Fibrinolysin,
pubmed-meshheading:9271229-Glycosylphosphatidylinositols,
pubmed-meshheading:9271229-Humans,
pubmed-meshheading:9271229-Immunohistochemistry,
pubmed-meshheading:9271229-Microscopy, Confocal,
pubmed-meshheading:9271229-Ovarian Neoplasms,
pubmed-meshheading:9271229-Phosphorylation,
pubmed-meshheading:9271229-Phosphotyrosine,
pubmed-meshheading:9271229-Plasminogen Activator Inhibitor 1,
pubmed-meshheading:9271229-Receptors, Cell Surface,
pubmed-meshheading:9271229-Receptors, Urokinase Plasminogen Activator,
pubmed-meshheading:9271229-Signal Transduction,
pubmed-meshheading:9271229-Tumor Cells, Cultured,
pubmed-meshheading:9271229-Urokinase-Type Plasminogen Activator
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Defective cell migration in an ovarian cancer cell line is associated with impaired urokinase-induced tyrosine phosphorylation.
|
| pubmed:affiliation |
Laboratoire Sainte Marie, Hôtel Dieu, Parvis de Notre Dame, Paris, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|