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The versican C-type lectin domain recognizes the adhesion protein tenascin-R.

1995; National Academy of Sciences; Volume: 92; Issue: 23 Linguagem: Inglês

10.1073/pnas.92.23.10590

1091-6490

Anders Aspberg, C. Binkert, Erkki Ruoslahti,

Cell Adhesion Molecules Research

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 strong binding in a gel blotting assay to a glycoprotein doublet in rat brain extracts. The binding was calcium dependent and abolished by chemical deglycosylation treatment of the ligand glycoprotein. The versican-binding glycoprotein was identified as the cell adhesion protein tenascin-R, and versican and tenascin-R were both found to be localized in the granular layer of rat cerebellum. These results show that the versican lectin domain is a binding domain with a highly targeted specificity. It may allow versican to assemble complexes containing proteoglycan, an adhesion protein, and hyaluronan.