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Originally published In Press as doi:10.1074/jbc.M201630200 on April 4, 2002

J. Biol. Chem., Vol. 277, Issue 24, 21930-21938, June 14, 2002
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Unique Ability of Integrin alpha vbeta 3 to Support Tumor Cell Arrest under Dynamic Flow Conditions*,

Jan Pilch, Rolf Habermann, and Brunhilde Felding-HabermannDagger

From the Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037

Shear-resistant arrest of circulating tumor cells is required for metastasis from the blood stream. Arrest during blood flow can be supported by tumor cell interaction with attached, activated platelets. This is mediated by tumor cell integrin alpha vbeta 3 and cross-linking plasma protein ligands. To analyze the mechanism of tumor cell ligand interactions under dynamic flow conditions, we used real-time video microscopy and tested human melanoma cell binding to fibrinogen, von Willebrand Factor, or fibronectin matrices in a buffer perfusion system. When perfused at venous flow, melanoma cells arrested abruptly and began to spread immediately. This was uniquely mediated by integrin alpha vbeta 3 on all tested ligands, and required alpha vbeta 3 activation and actin polymerization. Under static conditions, alpha vbeta 3 cooperated with alpha vbeta 1 and alpha 5beta 1 in supporting melanoma cell adhesion to fibronectin. But even when activated, beta 1 integrins did not contribute to melanoma cell arrest during flow. Soluble ligand served as a cross-linker between attached and circulating tumor cells and enhanced melanoma cell arrest. Cohesion of activated melanoma cells was restricted to the matrix surface and did not occur in suspension. We conclude that the presence of alpha vbeta 3 in a functionally activated state provides a unique advantage for circulating tumor cells by promoting tumor cell arrest in the presence of flow-dependent shear forces.

* This work was supported by Grants DAMD 17-99-1-9368 from the United States Army Department of Defense, 5JB-0143 from the California Breast Cancer Research Program, and RO1 CA95458 from the National Institutes of Health (to B. F. H) and by fellowship PI 402 from the Deutsche Forschungsgemeinschaft (to J. P.). This is manuscript 14779-MEM of 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.

The on-line version of this article (available at www.jbc.org) contains the video demonstrations for Figs. 1, 2, and 8.

Dagger To whom correspondence should be addressed: Dept. of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Rd., Mail Drop MEM 175, La Jolla, CA 92037. Tel.: 858-784-2021; Fax: 858-784-2030; E-mail: brunie@scripps.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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