Molecular and Functional Interdependence of the Urokinase-Type Plasminogen Activator System with Integrins

Verfasser / Beitragende:
[U. Reuning, V. Magdolen, S. Hapke, M. Schmitt]
Ort, Verlag, Jahr:
2003
Enthalten in:
Biological Chemistry, 384/8(2003-08-20), 1119-1131
Format:
Artikel (online)
ID: 378853074
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245 0 0 |a Molecular and Functional Interdependence of the Urokinase-Type Plasminogen Activator System with Integrins  |h [Elektronische Daten]  |c [U. Reuning, V. Magdolen, S. Hapke, M. Schmitt] 
520 3 |a The serine protease urokinase-type plasminogen activator (uPA), its inhibitor PAI-1, and its cellular receptor uPA-R (CD87) are of crucial importance during cellular invasion and migration, required for a variety of physio- and pathophysiological processes. It has become increasingly evident in recent years that the uPA/uPA-R-system has far more functional properties than plasminogen activation alone. This is reflected by its involvement in cellular events such as proliferation, adhesion, migration, and chemotaxis. Since uPA-R lacks a transmembrane domain and thus on its own is not capable of transmitting signals into cells, association and functional cooperation with other signaling molecules/receptors is needed. In this respect, one group of adhesion and signaling receptors, the integrins, have been identified which constitute, together with the uPA/uPA-R-system, an interdependent biological network by which the uPA/uPA-R-system broadly affects integrin functions and vice versa. Moreover, there is a growing body of evidence that cellular uPA, uPA-R, and PAI-1 expression is under control of specific ECM/integrin interactions and also that integrins are regulated by components of the uPA/uPARsystem. By this multifaceted crosstalk, cells may modulate their proteolytic, adhesive, and migratory activities and monitor ECM integrity in their microenvironment. 
540 |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG 
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