title: The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion.
abstract: 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.
authors: Burnham Institute, La Jolla, California 92037, USA.
authors: R
authors: R
authors: Miura
authors: A
authors: A
authors: Aspberg
authors: I M
authors: IM
authors: Ethell
authors: K
authors: K
authors: Hagihara
authors: R L
authors: RL
authors: Schnaar
authors: E
authors: E
authors: Ruoslahti
authors: Y
authors: Y
authors: Yamaguchi
mesh_terms: D000818:Animals; D001665:Binding Sites; D058581:Brevican; D002417:Cattle; D002448:Cell Adhesion; D011508:Chondroitin Sulfate Proteoglycans / Q000737:chemistry / Q000378:metabolism*; D006017:Glycolipids / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D037181:Lectins, C-Type; D008563:Membrane Lipids / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D019063:Tenascin / Q000378:metabolism
chemical_list: D058581:Brevican; D011508:Chondroitin Sulfate Proteoglycans; D006017:Glycolipids; D037102:Lectins; D037181:Lectins, C-Type; D008563:Membrane Lipids; D009419:Nerve Tissue Proteins; D019063:Tenascin