pubmed-article:11556845 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11556845 | lifeskim:mentions | umls-concept:C0002812 | lld:lifeskim |
pubmed-article:11556845 | lifeskim:mentions | umls-concept:C1512505 | lld:lifeskim |
pubmed-article:11556845 | lifeskim:mentions | umls-concept:C0032140 | lld:lifeskim |
pubmed-article:11556845 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:11556845 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
pubmed-article:11556845 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:11556845 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:11556845 | pubmed:dateCreated | 2001-9-14 | lld:pubmed |
pubmed-article:11556845 | pubmed:abstractText | The urokinase-dependent activation of plasminogen by breast cancer cells plays an important role in metastasis. We have previously shown that the metastatic breast cancer cell line MDA-MB-231 over-expresses urokinase and binds and efficiently activates plasminogen at the cell surface compared to non-metastatic cells. The aim of this study was to further characterise plasminogen binding and determine the topology of cell surface-bound plasminogen in terms of its potential for activation. The lysine-dependent binding of plasminogen at 4 degrees C to MDA-MB-231 cells was stable and resulted in an activation-susceptible conformation of plasminogen. Topologically, a fraction of bound plasminogen was co-localised with urokinase on the surfaces of MDA-MB-231 cells where it could be activated to plasmin. At 37 degrees C plasmin was rapidly lost from the cell surface. Apart from actin, other candidate plasminogen receptors were either not expressed or did not co-localise with plasminogen at the cell surface. Thus, based on co-localisation with urokinase, plasminogen binding is partitioned into two functional pools on the surface of MDA-MB-231 cells. In conclusion, these results shed further light on the functional organisation of the plasminogen activation cascade on the surface of a metastatic cancer cell. | lld:pubmed |
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pubmed-article:11556845 | pubmed:language | eng | lld:pubmed |
pubmed-article:11556845 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11556845 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11556845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11556845 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11556845 | pubmed:month | Sep | lld:pubmed |
pubmed-article:11556845 | pubmed:issn | 0007-0920 | lld:pubmed |
pubmed-article:11556845 | pubmed:author | pubmed-author:RansonMM | lld:pubmed |
pubmed-article:11556845 | pubmed:author | pubmed-author:AndronicosN... | lld:pubmed |
pubmed-article:11556845 | pubmed:copyrightInfo | Copyright 2001 Cancer Research Campaign http://www.bjcancer.com. | lld:pubmed |
pubmed-article:11556845 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11556845 | pubmed:day | 14 | lld:pubmed |
pubmed-article:11556845 | pubmed:volume | 85 | lld:pubmed |
pubmed-article:11556845 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11556845 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11556845 | pubmed:pagination | 909-16 | lld:pubmed |
pubmed-article:11556845 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:11556845 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11556845 | pubmed:articleTitle | The topology of plasminogen binding and activation on the surface of human breast cancer cells. | lld:pubmed |
pubmed-article:11556845 | pubmed:affiliation | Department of Biological Sciences, University of Wollongong, NSW Australia, 2522. | lld:pubmed |
pubmed-article:11556845 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11556845 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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