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纤连蛋白糖基化调节成纤维细胞的黏附与铺展。

Fibronectin glycosylation modulates fibroblast adhesion and spreading.

作者信息

Jones G E, Arumugham R G, Tanzer M L

出版信息

J Cell Biol. 1986 Nov;103(5):1663-70. doi: 10.1083/jcb.103.5.1663.

Abstract

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.

摘要

研究了纤连蛋白的碳水化合物残基在该糖蛋白与成纤维细胞表面、明胶和肝素相互作用特异性方面的作用。衣霉素用于产生碳水化合物缺失的纤连蛋白;它由培养的成纤维细胞合成。使用亲和柱分析了未糖基化和糖基化的纤连蛋白结合明胶和肝素的能力。用纤连蛋白包被的表面定量测量细胞黏附和铺展。结果表明,碳水化合物的缺失显著增加了该蛋白与明胶的相互作用,并显著增强了其促进成纤维细胞黏附和铺展的能力。相比之下,纤连蛋白与肝素的结合不受糖基化的影响。综合数据表明,纤连蛋白的天冬酰胺连接的寡糖作为该糖蛋白生物学功能的调节剂。

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