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J. Biol. Chem., Vol. 276, Issue 31, 28779-28788, August 3, 2001
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From the Laminin-5, consisting of the
A Unique Sequence of the Laminin
3 G Domain Binds to Heparin
and Promotes Cell Adhesion through Syndecan-2 and -4*
§,,,,
,
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
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 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.
*
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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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