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   <subfield code="a">The plasminogen activation system in tumor growth, invasion, and metastasis</subfield>
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   <subfield code="c">[P. A. Andreasen*, R. Egelund, H. H. Petersen]</subfield>
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   <subfield code="a">Abstract.: Generation of the serine proteinase plasmin from the extracellular zymogen plasminogen can be catalyzed by either of two other serine proteinases, the urokinase- and tissue-type plasminogen activators (uPA and tPA). The plasminogen activation system also includes the serpins PAI-1 and PAI-2, and the uPA receptor (uPAR). Many findings, gathered over several decades, strongly suggest an important and causal role for uPA-catalyzed plasmin generation in cancer cell invasion through the extracellular matrix. Recent evidence suggests that the uPA system is also involved in cancer cell-directed tissue remodeling. Moreover, the system also supports cell migration and invasion by plasmin-independent mechanisms, including multiple interactions between uPA, uPAR, PAI-1, extracellular matrix proteins, integrins, endocytosis receptors, and growth factors. These interactions seem to allow temporal and spatial reorganizations of the system during cell migration and a selective degradation of extracellular matrix proteins during invasion. The increased knowledge about the plasminogen activation system may allow utilization of its components as targets for anti-invasive therapy.</subfield>
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   <subfield code="a">Birkhäuser Verlag Basel,, 2000</subfield>
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   <subfield code="a">Key words. Serine proteinases</subfield>
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   <subfield code="a">Andreasen*</subfield>
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