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Originally published In Press as doi:10.1074/jbc.M201100200 on February 11, 2002

J. Biol. Chem., Vol. 277, Issue 17, 14467-14474, April 26, 2002
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The EIIIA Segment of Fibronectin Is a Ligand for Integrins alpha 9beta 1 and alpha 4beta 1 Providing a Novel Mechanism for Regulating Cell Adhesion by Alternative Splicing*

Yung-Feng LiaoDagger , Philip J. Gotwals§, Victor E. Koteliansky§, Dean Sheppard, and Livingston Van De WaterDagger ||**

From the Dagger  Center for Engineering in Medicine and Surgical Service, Massachusetts General Hospital and Harvard Medical School, the Shriners Burns Hospital, Boston, Massachusetts 02114, the || Center for Cell Biology and Cancer Research, Albany Medical College, Albany, New York 12208, § Biogen, Inc., Cambridge, Massachusetts 02142, and the  Lung Biology Center, Department of Medicine, University of California, San Francisco, California 94143

Alternative splicing of the fibronectin gene transcript gives rise to forms that include the EIIIA (or ED-A) segment. EIIIA-containing fibronectins are prominently expressed during embryogenesis and wound healing and appear to mediate changes in cell adhesion and gene expression. Nonetheless, integrins that bind the EIIIA segment have not been identified. We previously mapped the epitope for two function-blocking monoclonal antibodies to the C-C' loop region of the EIIIA segment (Liao, Y.-F., Wieder, K. G., Classen, J. M., and Van De Water, L. (1999) J. Biol. Chem. 274, 17876-17884). The sequence of this epitope (39PEDGIHELFP48) resembles the sequence within tenascin-C to which the integrin alpha 9beta 1 binds. We now report that either integrin alpha 9beta 1 or alpha 4beta 1 can mediate cell adhesion to the EIIIA segment. Moreover, this interaction is blocked both by epitope-mapped EIIIA antibodies as well as by the respective anti-integrins. Deletion mutants of the EIIIA segment that include the C-C' loop and flanking sequence bind cells expressing either alpha 9beta 1 or alpha 4beta 1. Adhesion of alpha 4beta 1-containing MOLT-3 cells to the EIIIA segment stimulates phosphorylation of p44/42 MAP kinase. Our observation that two integrins bind the EIIIA segment establishes a novel mechanism by which cell adhesion to fibronectin is regulated by alternative splicing.

* This work was supported in part by National Institutes of Health Grant GM56442 (to L. V. D. W.) and HL/AI33259, HL47412, HL53949, and HL56385 (to D. S.).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: Center for Cell Biology and Cancer Research, Mail Code 165, Albany Medical College, 47 New Scotland Avenue, Albany, NY 12208. Tel.: 518-262-9945; Fax: 518-262-9189; E-mail: VandewL@mail.amc.edu.

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