| pubmed-article:9405357 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9405357 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9405357 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:9405357 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:9405357 | lifeskim:mentions | umls-concept:C0071216 | lld:lifeskim |
| pubmed-article:9405357 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:9405357 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:9405357 | pubmed:dateCreated | 1998-2-19 | lld:pubmed |
| pubmed-article:9405357 | pubmed:abstractText | The role of urokinase-type plasminogen activator (uPA) and its receptor (uPAR/CD87) in cell migration and invasion is well substantiated. Recently, uPA has been shown to be essential in cell migration, since uPA-/- mice are greatly impaired in inflammatory cell recruitment. We have shown previously that the uPA-induced chemotaxis requires interaction with and modification of uPAR/CD87, which is the true chemoattracting molecule acting through an unidentified cell surface component which mediates this cell surface chemokine activity. By expressing and testing several uPAR/CD87 variants, we have located and functionally characterized a potent uPAR/CD87 epitope that mimics the effects of the uPA-uPAR interaction. The chemotactic activity lies in the region linking domains 1 and 2, the only protease-sensitive region of uPAR/CD87, efficiently cleaved by uPA at physiological concentrations. Synthetic peptides carrying this epitope promote chemotaxis and activate p56/p59(hck) tyrosine kinase. Both chemotaxis and kinase activation are pertussis toxin sensitive, involving a Gi/o protein in the pathway. | lld:pubmed |
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| pubmed-article:9405357 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9405357 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9405357 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9405357 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9405357 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9405357 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9405357 | pubmed:author | pubmed-author:AppellaEE | lld:pubmed |
| pubmed-article:9405357 | pubmed:author | pubmed-author:BlasiFF | lld:pubmed |
| pubmed-article:9405357 | pubmed:author | pubmed-author:FazioliFF | lld:pubmed |
| pubmed-article:9405357 | pubmed:author | pubmed-author:HigashimotoYY | lld:pubmed |
| pubmed-article:9405357 | pubmed:author | pubmed-author:ResnatiMM | lld:pubmed |
| pubmed-article:9405357 | pubmed:author | pubmed-author:SideniusNN | lld:pubmed |
| pubmed-article:9405357 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9405357 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9405357 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9405357 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9405357 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9405357 | pubmed:pagination | 7279-86 | lld:pubmed |
| pubmed-article:9405357 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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