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Originally published In Press as doi:10.1074/jbc.M002945200 on September 19, 2000

J. Biol. Chem., Vol. 275, Issue 50, 39182-39192, December 15, 2000
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Expression of the alpha 5 Integrin Subunit Gene Promoter Is Positively Regulated by the Extracellular Matrix Component Fibronectin through the Transcription Factor Sp1 in Corneal Epithelial Cells in Vitro*

Kathy LaroucheDagger , Steeve Leclerc, Christian Salesse§, and Sylvain L. Guérin||

From the Oncology and Molecular Endocrinology Research Center, and § Ophthalmology Research Unit, CHUL/CHUQ and Laval University, Ste-Foy, Québec G1V 4G2, Canada

The accumulation of fibronectin (FN) in response to corneal epithelium injury has been postulated to turn on expression of the FN-binding integrin alpha 5beta 1. In this work, we determined whether the activity directed by the alpha 5 gene promoter can be modulated by FN in rabbit corneal epithelial cells (RCEC). The activity driven by chloramphenicol acetyltransferase/alpha 5 promoter-bearing plasmids was drastically increased when transfected into RCEC grown on FN-coated culture dishes. The promoter sequence mediating FN responsiveness was shown to bear a perfect inverted repeat that we designated the fibronectin-responsive element (FRE). Analyses in electrophoretic mobility shift assays provided evidence that Sp1 is the predominant transcription factor binding the FRE. Its DNA binding affinity was found to be increased when RCEC are grown on FN-coated dishes. The addition of the MEK kinase inhibitor PD98059 abolished FN responsiveness suggesting that alteration in the state of phosphorylation of Sp1 likely accounts for its increased binding to the alpha 5 FRE. The FRE also proved sufficient to confer FN responsiveness to an otherwise unresponsive heterologous promoter. However, site-directed mutagenesis indicated that only the 3' half-site of the FRE was required to direct FN responsiveness. Collectively, binding of FN to its alpha 5beta 1 integrin activates a signal transduction pathway that results in the transcriptional activation of the alpha 5 gene likely through altering the phosphorylation state of Sp1.

* This work was supported by grants from the Medical Research Council, the Fondation sur les Maladies de l'Oeil, and the Fonds de la Recherche en Santé du Québec Vision network.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 Supported by a Scholarship from the Natural Sciences and Engineering Research Council of Canada.

Scholars from the Fonds de la Recherche en Santé du Québec.

|| To whom correspondence should be addressed: Oncology and Molecular Endocrinology Research Center, CHUL Research Center, 2705 Laurier Blvd., Ste-Foy, Québec G1V 4G2, Canada. Tel.: 418-654-2296; Fax: 418-654-2761; E-mail: Sylvain.guerin@crchul.ulaval.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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