Abstract
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 language | English |
|---|---|
| Pages (from-to) | 10590-10594 |
| Journal | Proceedings of the National Academy of Sciences |
| Volume | 92 |
| Issue number | 23 |
| Publication status | Published - 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