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J. Biol. Chem., Vol. 275, Issue 40, 30907-30915, October 6, 2000 Identification of Motifs for Cell Adhesion within the Repeated Domains of Transforming Growth Factor-{beta}-induced Gene, {beta}ig-h3

Abstract

Jung-Eun Kim^§, Song-Ja Kim^§¶, Byung-Heon Lee, Rang-Woon Park^¶, Ki-San Kim^**, and In-San Kim^¶

From the Department of Biochemistry, the ^¶ Biomolecular Engineering Center, Kyungpook National University School of Medicine, Taegu 700-422, the Department of Biochemistry, Dongguk University School of Medicine, Kyungju 780-714, and the ^** Department of Ophthalmology, Keimyung University School of Medicine, Taegu 700-310, Korea

$beta$ ig-h3 is a transforming growth factor- $beta$ -inducible cell adhesion molecule that has four characteristic homologous repeated domains. We made recombinant $beta$ ig-h3 proteins, which were highly active in mediating human corneal epithelial (HCE) cell adhesion and spreading. The 2nd and the 4th repeated domains were sufficient to mediate HCE cell adhesion. A sequence analysis showed that aspartic acid (Asp) and isoleucine (Ile) of the 2nd and the 4th domains are highly conserved in many fasciclin 1 homologous (fas-1) domains. Substitution mutational study identified these two amino acids are essential for cell adhesion. Synthetic peptides containing Asp and Ile, NKDIL and EPDIM derived from the 2nd and the 4th domains, respectively, almost completely blocked cell adhesion mediated by not only wild type $beta$ ig-h3 but also each of the 2nd and the 4th domains. These peptides alone were fully active in mediating cell adhesion. In addition, we demonstrated the functional receptor for $beta$ ig-h3 is $alpha$ ₃ $beta$ ₁ integrin. These results, therefore, establish the essential motifs within the 2nd and the 4th domains of $beta$ ig-h3, which interact with $alpha$ ₃ $beta$ ₁ integrin to mediate HCE cell adhesion to $beta$ ig-h3 and suggest that other proteins containing Asp-Ile in their fas-1 domains could possibly function as cell adhesion molecules.

^* This work was supported by KOSEF General Research Grant 1999-2-209-008-5.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.

^§ Both authors contributed equally to this work.

To whom correspondence should be addressed: Dept. of Biochemistry, Kyungpook National University School of Medicine, 101 Dongin-dong, Jung-gu, Taegu 700-422, Korea. Tel.: 82-53-420-6933; Fax: 82-53-422-1466.

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