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Papers In Press, published online ahead of print May 23, 2001
Dermatology, Chiba University, School of Medicine, Chiba-city 260
Corresponding Author: utani{at}derma01.m.chiba-u.ac.jp
Laminin-5, consisting of the
J. Biol. Chem, 10.1074/jbc.M101420200
Submitted on February 14, 2001
Revised on May 23, 2001
Accepted on May 23, 2001
A unique sequence of the laminin
3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4
3, 
3, and 
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 a chains of laminins have been shown to have various biological activities. In this study, we identified a sequence of the 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 3 LG4 module is responsible for cell adhesion and suggest that syndecan-2 and -4 mediate this activity.
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