Mayeux P, Casadevall N, Muller O, Lacombe C
ICGM, Inserm U152, Hôpital Cochin, Paris, France.
FEBS Lett. 1990 Aug 20;269(1):167-70. doi: 10.1016/0014-5793(90)81145-e.
Murine erythropoietin-responsive Rauscher Red 5-1.5 cells were used to determine the contribution of glycosylation to the size and function of the erythropoietin receptor. The half life of the receptors was determined to be 4 h. The number of receptors was not significantly decreased in cells treated for 48 h with inhibitors of glycosylation (tunicamycin, glucosamine or swainsonine) and their affinity was slightly enhanced in tunicamycin- or glucosamine-treated cells. Erythropoietin was cross-linked with two proteins of 104 and 86 kDa. Their molecular masses were not significantly reduced in cells treated with the glycosylation inhibitors. When immunoprecipitated cross-linked receptors were digested with endoglycosidases, the molecular masses of both proteins were only slightly modified giving values of 100 and 82 kDa. Thus we can conclude that the proteins cross-linked to erythropoietin are very weakly glycosylated.
使用对小鼠促红细胞生成素敏感的劳舍尔红5-1.5细胞来确定糖基化对促红细胞生成素受体大小和功能的影响。受体的半衰期确定为4小时。用糖基化抑制剂（衣霉素、氨基葡萄糖或苦马豆素）处理48小时的细胞中，受体数量没有显著减少，并且在衣霉素或氨基葡萄糖处理的细胞中它们的亲和力略有增强。促红细胞生成素与104 kDa和86 kDa的两种蛋白质交联。在用糖基化抑制剂处理的细胞中，它们的分子量没有显著降低。当用内切糖苷酶消化免疫沉淀的交联受体时，两种蛋白质的分子量仅略有改变，分别为100 kDa和82 kDa。因此我们可以得出结论，与促红细胞生成素交联的蛋白质糖基化程度非常低。
