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Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Urokinase Receptor and Integrin Interactions

Author(s): Matthias C. Kugler, Ying Wei and Harold A. Chapman

Volume 9, Issue 19, 2003

Page: [1565 - 1574] Pages: 10

DOI: 10.2174/1381612033454658

Price: $65

Abstract

Urokinase receptors (uPAR) were initially thought to function simply as a mechanism to concentrate the urokinase / plasmin system toward the cell surface. However, extensive evidence has accumulated that this glycolipidanchored receptor also functions in both the adhesive and signaling pathways of many migratory cells. Mechanisms by which uPAR exercises these functions involve complexing with other membrane proteins for signal transduction. One set of functional partners for uPAR on the cell surface are integrins. Recent studies point to important structural features of uPAR:integrin interactions, indicating uPAR to be a cis-acting integrin ligand. In vivo data reveal altered integrin function and cell migration when uPAR:integrin interactions are impaired. Together these observations support the idea that uPAR:integrin interactions may be a focal point of intervention in pathobiology where integrin function is crucial, such as tumor metastasis.

Keywords: urokinase, integrin, adhesion, receptor


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