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Originally published In Press as doi:10.1074/jbc.M101420200 on May 23, 2001

J. Biol. Chem., Vol. 276, Issue 31, 28779-28788, August 3, 2001
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A Unique Sequence of the Laminin alpha 3 G Domain Binds to Heparin and Promotes Cell Adhesion through Syndecan-2 and -4*

Atsushi UtaniDagger §, Motoyoshi Nomizu, Hiroshi MatsuuraDagger , Kozue Kato, Takashi KobayashiDagger , Ushio TakedaDagger , Shinichi Aota||, Peter K. Nielsen**, and Hiroshi ShinkaiDagger

From the Dagger  Department of Dermatology, School of Medicine, Chiba University, Chiba 260, Japan, the  Graduate School of Environmental Earth Science, Hokkaido University, Sapporo 060, Japan, || The Biomolecular Engineering Research Institute, Osaka 565, Japan, and the ** Craniofacial Developmental Biology and Regeneration Branch, NIDCR, National Institutes of Health, Bethesda, Maryland 20892-4370

Laminin-5, consisting of the alpha 3, beta 3, and gamma 2 chains, is localized in the skin basement membrane and supports the structural stability of the epidermo-dermal linkage and regulates various cellular functions. The alpha  chains of laminins have been shown to have various biological activities. In this study, we identified a sequence of the alpha 3 chain C-terminal globular domain (LG1-LG5 modules) required for both heparin binding and cell adhesion using recombinant proteins and synthetic peptides. We found that the LG3 and LG4 modules have activity for heparin binding and that LG4 has activity for cell adhesion. Studies with synthetic peptides delineated the A3G75aR sequence (NSFMALYLSKGR, residues 1412-1423) within LG4 as a major site for both heparin and cell binding. Substitution mutations in LG4 and A3G75aR identified the Lys and Arg of the A3G75aR sequence as critical for these activities. Cell adhesion to LG4 and A3G75aR was inhibited by heparitinase I treatment of cells, suggesting that cell binding to the A3G75aR site was mediated by cell surface heparan sulfate proteoglycans. We showed by affinity chromatography that syndecan-2 from fibroblasts bound to LG4. Solid-phase assays confirmed that syndecan-2 interacted with the A3G75aR peptide sequence. Stably transfected 293T cells with expression vectors for syndecan-2 and -4, but not glypican-1, specifically adhered to LG4 and A3G75aR. These results indicate that the A3G75aR sequence within the laminin alpha 3 LG4 module is responsible for cell adhesion and suggest that syndecan-2 and -4 mediate this activity.

* This work was supported by Grant-in-aid 11670817 for Scientific Research from the Ministry of Education, Science, Culture and Sports of Japan and by the Dermatological Basic Research Shiseido Fund (to A. U.).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: Dept. of Dermatology, School of Medicine, Chiba University, 1-8-1 Inohana-cho, Chuou-ku Chiba-city 260, Japan. Tel.: 81-43-222-7171; Fax: 81-43-226-2128; E-mail: Utani@derma01.m.chiba-u.ac.jp.

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