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J Biol Chem, Vol. 274, Issue 16, 11431-11438, April 16, 1999
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From the The lecticans are a group of chondroitin sulfate
proteoglycans characterized by the presence of C-type lectin domains.
Despite the suggestion that their lectin domains interact with
carbohydrate ligands, the identity of such ligands has not been
elucidated. We previously showed that brevican, a nervous
system-specific lectican, binds the surface of B28 glial cells (Yamada,
H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B.,
Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784-7795). In this paper, we demonstrate that two
classes of sulfated glycolipids, sulfatides and HNK-1-reactive
sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for
brevican. The lectin domain of brevican binds sulfatides and SGGLs in a
calcium-dependent manner as expected of a C-type lectin
domain. Intact, full-length brevican also binds both sulfatides and
SGGLs. The lectin domain immobilized as a substrate supports adhesion
of cells expressing SGGLs or sulfatides, which was inhibited by
monoclonal antibodies against these glycolipids or by treatment of the
substrate with SGGLs or sulfatides. Our findings demonstrate that the
interaction between the lectin domains of lecticans and sulfated
glycolipids comprises a novel cell substrate recognition system, and
suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo.
Burnham Institute, La Jolla, California
92037 and the ¶ Department of Pharmacology and Neuroscience,
Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205
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