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Originally published In Press as doi:10.1074/jbc.M205307200 on July 10, 2002

J. Biol. Chem., Vol. 277, Issue 37, 34391-34400, September 13, 2002
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Focal Adhesion Kinase Activated by beta 4 Integrin Ligation to mCLCA1 Mediates Early Metastatic Growth*

Mossaad Abdel-Ghany, Hung-Chi Cheng, Randolph C. Elble, and Bendicht U. PauliDagger

From Cancer Biology Laboratories, Department of Molecular Medicine, Cornell University College of Veterinary Medicine, Ithaca, New York 14853

Early metastatic growth occurs at sites of vascular arrest of blood-borne cancer cells and is entirely intravascular. Here we show that lung colonization by B16-F10 cells is licensed by beta 4 integrin adhesion to the mouse lung endothelial Ca2+-activated chloride channel protein mCLCA1. In a manner independent of Met, beta 4 integrin-mCLCA1-ligation leads to complexing with and activation of focal adhesion kinase (FAK) and downstream signaling to extracellular signal-regulated kinase (ERK). FAK/ERK signaling is Src-dependent and is interrupted by adhesion blocking antibodies and by dominant-negative (dn)-FAK mutants. Levels of ERK activation in B16-F10 cells transfected with wild-type or mutant FAK are closely associated with rates of proliferation and bromodeoxyuridine (BrdUrd) incorporation of tumor cells grown in mCLCA1-coated dishes, the ability to form tumor cell colonies on CLCA-expressing endothelial cell monolayers, and the extent of pulmonary metastatic growth. Parallel with the transfection rates, B16-F10 cells transfected with dn-FAK mutants and injected intravenously into syngeneic mice generate approximately half the number and size of lung colonies that vector-transfected B16-F10 cells produce. For the first time, beta 4 integrin ligation to its novel CLCA-adhesion partner is shown to be associated with FAK complexing, activation, and signaling to promote early, intravascular, metastatic growth.

* This work was supported by Public Health Service Grant CA47668 from the NCI, National Institutes of Health, by Grant DAMD17-00-1-0619 from the U. S. Army Medical Research and Materiel Command, and by a donation from the American Boxer Dog Club (Mrs. Billie McFadden).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.

Dagger To whom correspondence should be addressed: Cancer Biology Laboratories, Department of Molecular Medicine, Cornell University College of Veterinary Medicine, C4 161 Veterinary Medical Center, Ithaca, NY 14853. Tel.: 607-253-3343; Fax: 607-253-3708; E-mail: bup1@cornell.edu.

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