Glycosylation of the basic fibroblast growth factor receptor. The contribution of carbohydrate to receptor function.
Glycosylation of the basic fibroblast growth factor receptor. The contribution of carbohydrate to receptor function.
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DOI：
10.1016/s0021-9258(18)68179-7
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发表时间：
1988-10
期刊：
影响因子：
--
通讯作者：
J. Feige;A. Baird
中科院分区：
文献类型：
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作者：
J. Feige;A. Baird
我们研究了碱性成纤维细胞生长因子（bFGF）受体的糖基化，以确定碳水化合物是否有助于受体的结构和功能。使用交联和放射性受体测定的组合，我们证明了在婴儿仓鼠肾细胞中的两个bFGF受体具有100和125 kDa的蛋白质核心。它们被糖基化成115和140 kDa的高甘露糖形式，并进一步加工成130和150 kDa的成熟形式。因为肽：N-糖苷酶F，而不是内切-α-N-乙酰半乳糖胺酶可以减小bFGF受体的大小，所以受体的碳水化合物残基看起来都是N-连接的。去糖基化受体不能结合125 I-bFGF支持了糖残基是受体功能所需的观点。此外，麦胚凝集素凝集素抑制125 I-bFGF结合和bFGF的生物活性的能力表明，N-乙酰葡糖胺残基是受体的功能上重要的成分。
We have examined the glycosylation of the basic fibroblast growth factor (bFGF) receptor to determine whether carbohydrates contribute to receptor structure and function. Using a combination of cross-linking and radioreceptor assays, we demonstrated that the two bFGF receptors in baby hamster kidney cells have protein cores of 100 and 125 kDa. They are glycosylated to high mannose forms of 115 and 140 kDa and further processed to their mature forms of 130 and 150 kDa. Because peptide:N-glycosidase F, but not endo-alpha-N-acetylgalactosamidase can reduce the size of the bFGF receptors, the carbohydrate residues of the receptor appear all N-linked. The inability of deglycosylated receptors to bind 125I-bFGF supports the notion that the carbohydrate residues are required for receptor function. Furthermore, the capacity of the wheat germ agglutinin lectin to inhibit 125I-bFGF binding and the biological activity of bFGF suggests that N-acetylglucosamine residues are functionally significant components of the receptor.