Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces
Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces
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DOI：
10.1093/glycob/cwq039
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发表时间：
2010-07-01
期刊：
影响因子：
4.3
通讯作者：
Akaike, Toshihiro
中科院分区：
文献类型：
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作者：
Ise, Hirohiko;Kobayashi, Satoshi;Akaike, Toshihiro
波形蛋白和结蛋白是分别在各种间充质和骨骼肌细胞中发现的中间丝蛋白。这些蛋白质在细胞质结构的稳定中起重要作用。在这里，我们发现，使用人工仿生glycopolymers，波形蛋白和结蛋白具有N-乙酰葡糖胺（GlcNAc）结合凝集素样的性质上的各种波形蛋白和结蛋白表达细胞，如心肌细胞和血管平滑肌细胞的细胞表面。通过共聚焦激光显微镜和表面等离子体共振分析，这些蛋白质的杆II结构域被证明定位于细胞表面，并直接结合到人工仿生GlcNAc轴承聚合物。这些糖聚合物与凝集素强烈相互作用，是分析凝集素-碳水化合物相互作用的有用工具，因为糖聚合物与凝集素结合可以诱导凝集素由于多价糖苷配体结合而聚集。此外，免疫细胞化学和下拉分析与His标记的波形蛋白杆II结构域蛋白表明，波形蛋白杆II结构域与O-GlcNAc蛋白相互作用。这些结果表明，O-GlcNAc蛋白可能是一个候选人的生理GlcNAc轴承配体与波形蛋白和结蛋白相互作用。这些发现证明了波形蛋白和结蛋白的一种新功能，其不涉及细胞质结构的稳定化，通过该细胞质结构，这些蛋白质通过其GlcNAc结合凝集素样性质与细胞表面上的生理性GlcNAc承载配体如O-GlcNAc蛋白相互作用。
Vimentin and desmin are intermediate filament proteins found in various mesenchymal and skeletal muscle cells, respectively. These proteins play an important role in the stabilization of the cytoplasmic architecture. Here, we found, using artificial biomimicking glycopolymers, that vimentin and desmin possess N-acetylglucosamine (GlcNAc)-binding lectin-like properties on the cell surfaces of various vimentin- and desmin-expressing cells such as cardiomyocytes and vascular smooth muscle cells. The rod II domain of these proteins was demonstrated to be localized to the cell surface and to directly bind to the artificial biomimicking GlcNAc-bearing polymer, by confocal laser microscopy and surface plasmon resonance analysis. These glycopolymers strongly interact with lectins and are useful tools for the analysis of lectin-carbohydrate interactions, since glycopolymers binding to lectins can induce the clustering of lectins due to multivalent glycoside ligand binding. Moreover, immunocytochemistry and pull-down assay with His-tagged vimentin-rod II domain protein showed that the vimentin-rod II domain interacts with O-GlcNAc proteins. These results suggest that O-GlcNAc proteins might be one candidate for physiological GlcNAc-bearing ligands with which vimentin and desmin interact. These findings demonstrate a novel function of vimentin and desmin that does not involve stabilization of the cytoplasmic architecture by which these proteins interact with physiological GlcNAc-bearing ligands such as O-GlcNAc proteins on the cell surface through their GlcNAc-binding lectin-like properties.