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First published online 1 June 2004
doi: 10.1242/jcs.01149

Journal of Cell Science 117, 2909-2916 (2004)
Published by The Company of Biologists 2004
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Research Article

The soluble D2D388-274 fragment of the urokinase receptor inhibits monocyte chemotaxis and integrin-dependent cell adhesion

Federico Furlan1,*, Simone Orlando1,*, Carlo Laudanna2, Massimo Resnati1, Veronica Basso1, Francesco Blasi1,*,{ddagger} and Anna Mondino1,*

1 Department of Molecular Biology and Functional Genomics, San Raffaele Scientific Institute, Milan, 20132, Italy
2 Division of General Pathology, Department of Pathology, University of Verona, Verona, 37129, Italy

{ddagger} Author for correspondence (e-mail: francesco.blasi{at}hsr.it)

Accepted 11 February 2004

We have previously shown that chymotrypsin-cleaved soluble uPAR (D2D388-274) elicits migration of monocytic cells through interaction with FPRL-1, a G protein-coupled receptor that is homologous to the fMLP receptor. Here, we report that D2D388-274 also modulates the ability of monocytes to migrate in response to other chemokines. Pretreatment of monocytes with increasing amounts of D2D388-274 prevents cell migration in response to MCP-1, RANTES and fMLP. We demonstrate that D2D388-274 does not inhibit MCP-1 receptor binding, elicit CCR2 internalization and prevent MCP-1-induced intracellular Ca2+ increase. Thus, CCR2 receptor desensitization cannot account for D2D388-274-mediated inhibition of MCP-1-induced cell migration. Rather, we show that pretreatment of monocytes with D2D388-274 dramatically decreases chemokine-induced integrin-dependent rapid cell adhesion by interacting with FPRL-1. Together, our results indicate that chemokine-dependent cell migration can be regulated not only by homologous and heterologous receptor desensitization, but also by inhibition of integrin-dependent cell adhesion, an important step in cell transmigration.

Key words: Monocytes, Chemoattractants, Cell migration, Cell adhesion


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