THE VERSICAN C-TYPE LECTIN DOMAIN RECOGNIZES THE ADHESION PROTEIN TENASCIN-R

The core proteins of large chondroitin sulfate proteoglycans contain a C-type lectin domain. The lectin domain of one of these proteoglycans , versican, was expressed as a recombinant 15-kDa protein and shown to bind to insolubilized fucose and GlcNAc. The lectin domain showed str ong binding in a gel blotting assay to a glycoprotein doublet in rat b rain extracts, The binding was calcium dependent and abolished by chem ical deglycosylation treatment of the ligand glycoprotein, The versica n-binding glycoprotein was identified as the cell adhesion protein ten ascin-R, and versican and tenascin-R were both found to be localized i n the granular layer of rat cerebellum, These results show that the ve rsican lectin domain is a binding domain with a highly targeted specif icity, It may allow versican to assemble complexes containing proteogl ycan, an adhesion protein, and hyaluronan.