Fibronectin glycosylation modulates fibroblast adhesion and spreading.
Fibronectin glycosylation modulates fibroblast adhesion and spreading.
复制标题
纤连蛋白糖基化调节成纤维细胞粘附并扩散。
DOI：
10.1083/jcb.103.5.1663
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发表时间：
1986-11
期刊：
影响因子：
--
通讯作者：
Tanzer ML
中科院分区：
文献类型：
--
作者：
Jones GE;Arumugham RG;Tanzer ML
纤维连接蛋白的碳水化合物残基与该糖蛋白与成纤维细胞表面、明胶和肝素相互作用的特异性有关。衣霉素被用来生产碳水化合物耗竭的纤维连接蛋白；它是由培养的成纤维细胞合成的。使用亲和层析柱分析了未糖化和糖化的纤维连接蛋白与明胶和肝素的结合能力。纤维连接蛋白涂层表面用于定量测量细胞的黏附和铺展。结果表明，碳水化合物的缺乏显著增加了蛋白质与明胶的相互作用，并显著增强了其促进成纤维细胞黏附和铺展的能力。相反，纤维连接蛋白与肝素的结合不受糖基化的影响。复合数据表明，纤维连接蛋白的天冬氨酸氨基转移酶连接的寡糖作为糖蛋白的生物功能的调节器。
The role of the carbohydrate residues of fibronectin concerning the specificities of that glycoprotein to interact with fibroblastic cell surfaces, gelatin, and heparin was examined. Tunicamycin was used to produce carbohydrate-depleted fibronectin; it was synthesized by cultured fibroblasts. Unglycosylated and glycosylated fibronectins were analyzed for their ability to bind gelatin and heparin, using affinity columns. Fibronectin-coated surfaces were used to quantitatively measure cell adhesion and spreading. The results showed that the lack of carbohydrates significantly increased the interaction of the protein with gelatin and markedly enhanced its ability to promote adhesion and spreading of fibroblasts. In contrast, the binding of fibronectin to heparin was not influenced by glycosylation. The composite data indicate that the Asn-linked oligosaccharides of fibronectin act as modulators of biological functions of the glycoprotein.