The versican C-type lectin domain recognizes the adhesion protein tenascin-R.
收藏PubMed Central1995-11-07 更新2026-05-02 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC40657/
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资源简介：
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. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1995-11-07
