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Prepublished online as a Blood First Edition Paper on September 26, 2002; DOI 10.1182/blood-2002-06-1842. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-06-1842v1 101/4/1582    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Pluskota, E. Articles by Plow, E. F. Search for Related Content PubMed PubMed Citation Articles by Pluskota, E. Articles by Plow, E. F. Related Collections Hematopoiesis and Stem Cells Phagocytes Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 February 2003, Vol. 101, No. 4, pp. 1582-1590 PHAGOCYTES Convergence of the adhesive and fibrinolytic systems: recognition of urokinase by integrin M2 as well as by the urokinase receptor regulates cell adhesion and migration Elzbieta Pluskota, Dmitry A. Soloviev, and Edward F. Plow From the Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Foundation, Cleveland, OH. Previous studies demonstrated that integrin M2 (CD11b/18, Mac-1) forms a physical complex with the urokinase-type plasminogen activator receptor (uPAR/CD87) on leukocytes. In this study, we used human peripheral blood neutrophils and transfected cells expressing M2, uPAR, or both receptors to show that the integrin can directly interact with urokinase (uPA). We demonstrate that M2 supported adhesion and migration of these cells to uPA, and, in each case, blockade of M2 suppressed the response. Within uPA, both the kringle and proteolytic domains are recognized by M2, which are distinct from the growth factor domain that binds to uPAR. Within the M subunit of the integrin, the I domain interacts with uPA, which is distinct from the region that interacts with uPAR. On cells expressing uPAR and M2, both receptors mediated adhesion and migration. This cooperation was particularly apparent in the responses of neutrophils to uPA, where blockade of M2 reduced uPAR-mediated responses and engagement of uPAR enhanced recognition of uPA by M2. Thus, recognition of uPA by M2 allows for formation of a multicontact trimolecular complex, in which a single uPA ligand may bind simultaneously to both uPAR and M2. 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