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Protease Crosstalk with Integrins: the Urokinase Receptor Paradigm

Journal: Thrombosis and Haemostasis
ISSN: 0340-6245
Issue: 2001: 86/1 (July, State of the Art) pp.1-508
Pages: 124-9

Protease Crosstalk with Integrins: the Urokinase Receptor Paradigm

Harold A. Chapman, Ying Wie
Pulmonary and Critical Care Division, University of California at San Francisco, San Francisco, CA, USA

Summary

Migratory cells use both adhesion receptors and proteolytic enzymes to regulate their interaction with and response to extracellular matrices. Cooperation between integrins and proteases operates at several levels: integrin signaling induces proteases, proteases co-localize with integrins, and proteases regulate the interface between integrins and the intracellular cytoskeleton. One protease system intimately connected to integrins is the urokinase/urokinase receptor(uPAR)/plasmin system. Recent studies indicate urokinase promotes the ligand-like binding of its receptor to a set of b1 and b2 integrins, this binding in turn affecting integrin signaling and cell migration. The glycolipid anchor of uPAR associates with cholesterol-rich membrane rafts. Binding of uPAR to integrins may enrich integrin clusters with signaling molecules such as src-family kinases that localize to rafts and are important to integrin function. Signals derived from integrin/uPAR complexes promote the function of other integrins. Thus the urokinase/plasmin system coordinates with integrins to regulate cell: matrix interactions.