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Originally published In Press as doi:10.1074/jbc.M008220200 on October 26, 2000

J. Biol. Chem., Vol. 276, Issue 6, 3983-3990, February 9, 2001
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Urokinase-type Plasminogen Activator Receptor (CD87) Is a Ligand for Integrins and Mediates Cell-Cell Interaction*

Takehiko Tarui, Andrew P. MazarDagger , Douglas B. Cines§, and Yoshikazu Takada

From the Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, Dagger  Attenuon, LLC, San Diego, California 92121, and the § Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

Binding of urokinase-type plasminogen activator (uPA) to its receptor (uPAR/CD87) regulates cellular adhesion, migration, and tumor cell invasion. However, it is unclear how glycosyl phosphatidylinositol-anchored uPAR, which lacks a transmembrane structure, mediates signal transduction. It has been proposed that uPAR forms cis-interactions with integrins as an associated protein and thereby transduces proliferative or migratory signals to cells upon binding of uPA. We provide evidence that soluble uPAR (suPAR) specifically binds to integrins alpha 4beta 1, alpha 6beta 1, alpha 9beta 1, and alpha vbeta 3 on Chinese hamster ovary cells in a cation-dependent manner. Anti-integrin and anti-uPAR antibodies effectively block binding of suPAR to these integrins. Binding of suPAR to alpha 4beta 1 and alpha vbeta 3 is blocked by known soluble ligands and by the integrin mutations that inhibit ligand binding. These results suggest that uPAR is an integrin ligand rather than, or in addition to, an integrin-associated protein. In addition, we demonstrate that glycosyl phosphatidylinositol-anchored uPAR on the cell surface specifically binds to integrins on the apposing cells, suggesting that uPAR-integrin interaction may mediate cell-cell interaction (trans-interaction). These previously unrecognized uPAR-integrin interactions may allow uPAR to transduce signals through the engaged integrin without a hypothetical transmembrane adapter and may provide a potential therapeutic target for control of inflammation and cancer.

* This work was supported by National Institutes of Health Grants GM47175 and GM49899 (to Y. T.) and HL60169 (to D. C.). This is publication 13186-VB from The Scripps Research Institute.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Vascular Biology, CAL-10, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-784-7636; Fax: 858-784-7645; E-mail: takada@scripps.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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