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pubmed-article:11556845pubmed:abstractTextThe 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:11556845pubmed:copyrightInfoCopyright 2001 Cancer Research Campaign http://www.bjcancer.com.lld:pubmed
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pubmed-article:11556845pubmed:articleTitleThe topology of plasminogen binding and activation on the surface of human breast cancer cells.lld:pubmed
pubmed-article:11556845pubmed:affiliationDepartment of Biological Sciences, University of Wollongong, NSW Australia, 2522.lld:pubmed
pubmed-article:11556845pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11556845pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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