THE VERSICAN C-TYPE LECTIN DOMAIN RECOGNIZES THE ADHESION PROTEIN TENASCIN-R
THE VERSICAN C-TYPE LECTIN DOMAIN RECOGNIZES THE ADHESION PROTEIN TENASCIN-R
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DOI：
10.1073/pnas.92.23.10590
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发表时间：
1995-11-07
影响因子：
11.1
通讯作者：
RUOSLAHTI, E
中科院分区：
文献类型：
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作者：
ASPBERG, A;BINKERT, C;RUOSLAHTI, E
大硫酸软骨素蛋白聚糖的核心蛋白含有C型凝集素结构域。这些蛋白聚糖之一，多功能蛋白聚糖，凝集素结构域表达为重组15 kDa的蛋白质，并显示结合不溶性岩藻糖和GlcNAc。在凝胶印迹分析中，凝集素结构域与大鼠脑提取物中的糖蛋白双联体显示出强结合，这种结合是钙依赖性的，并且配体糖蛋白的化学去糖基化处理消除了这种结合。将多功能蛋白聚糖结合糖蛋白鉴定为细胞粘附蛋白tenascin-R，并且发现多功能蛋白聚糖和tenascin-R均定位于大鼠小脑的颗粒层，这些结果表明，多能蛋白聚糖凝集素结构域是一个具有高度靶向特异性的结合结构域，它可能允许多能蛋白聚糖组装含有蛋白聚糖、粘附蛋白和透明质酸的复合物。
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.