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Originally published In Press as doi:10.1074/jbc.M006097200 on December 15, 2000

J. Biol. Chem., Vol. 276, Issue 11, 8436-8444, March 16, 2001
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Carbohydrate-Carbohydrate Binding of Ganglioside to Integrin alpha 5 Modulates alpha 5beta 1 Function*

Xiaoqi WangDagger , Ping SunDagger , Abbas Al-QamariDagger , Tadashi Tai§, Ikuo Kawashima§, and Amy S. PallerDagger

From the Dagger  Departments of Pediatrics and Dermatology, Children's Memorial Institute for Education and Research, Northwestern University Medical School, Chicago, Illinois 60614 and the § Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan

Gangliosides GT1b and GD3, components of keratinocyte membranes, inhibit keratinocyte adhesion to fibronectin. Although ganglioside sialylation is known to be important, the mechanism of inhibition is unknown. Using purified insect recombinant alpha 5 and beta 1 proteins and alpha 5beta 1 integrin from lysed keratinocyte-derived SCC12 cells, we have shown that GT1b and GD3 inhibit the binding of alpha 5beta 1 to fibronectin. Co-immunoprecipitation of GT1b and alpha 5beta 1 from SCC12 cells and direct binding of GT1b and GD3 to affinity-purified alpha 5beta 1 from SCC12 cells and insect recombinant alpha 5beta 1, particularly the alpha 5 subunit, further suggest interaction between ganglioside and alpha 5beta 1. The carbohydrate moieties of integrin appear to be critical since gangliosides are unable to bind deglycosylated forms of alpha 5beta 1 from SCC12 and insect cells or poorly glycosylated recombinant alpha 5beta 1 from Escherichia coli cells. The GT1b-alpha 5beta 1 interaction is inhibited by concanavalin A, suggesting that GT1b binds to mannose structures in alpha 5beta 1. The preferential binding of GT1b to high mannose rather than reduced mannose ovalbumin further implicates the binding of GT1b to mannose structures. These data provide evidence that highly sialylated gangliosides regulate alpha 5beta 1-mediated adhesion of epithelial cells to fibronectin through carbohydrate-carbohydrate interactions between GT1b and the alpha 5 subunit of alpha 5beta 1 integrin.

* This work was supported by National Institutes of Health Grant R01 AR44619.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 and reprint requests should be addressed: Div. of Dermatology 107, Children's Memorial Hospital, 2300 Children's Plaza, Chicago, IL 60614. Tel.: 773-880-4698; Fax: 773-880-3025; E-mail: apaller@northwestern.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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