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

Anders Aspberg, Christoph Binkert, Erkki Ruoslahti

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)10590-10594
JournalProceedings of the National Academy of Sciences
Issue number23
Publication statusPublished - 1995

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Connective Tissue Biology (013230151)

Subject classification (UKÄ)

  • Rheumatology and Autoimmunity


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