Effect of anomeric linkage on the sialylation of glycosides by cells
Effect of anomeric linkage on the sialylation of glycosides by cells
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DOI：
10.1080/07328300500208107
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发表时间：
2005-01-01
影响因子：
1
通讯作者：
Hatanaka, K
中科院分区：
文献类型：
--
作者：
Kasuya, MCZ;Ikeda, M;Hatanaka, K
研究了糖基引物法和细胞法合成唾液酸苷的方法。化学合成α中心点和β中心点糖引物，并将其导入B16黑色素瘤细胞，启动寡糖合成。将α-和β-十二烷基乳糖苷掺入B16细胞后，半乳糖残基发生唾液酸化，得到GM3型低聚糖。β-十二烷基半乳糖苷可被唾液酸化，而α-十二烷基半乳糖苷未被唾液酸化。α-和β-十二烷基葡萄糖苷引物均未延长。在细胞对引物的糖基化过程中，本研究证实唾液酸基转移酶耐受受体的修饰，并允许引物延长，而不考虑与苷元单位的α-或β-连接。然而，末端半乳糖残基的存在是细胞酶发生唾液酸化所必需的，该残基与相邻的糖或苷元单元相连。
The synthesis of sialylated glycosides using saccharide primers and cells was investigated. alpha center dot and beta center dot Saccharide primers were chemically synthesized and introduced into B16 melanoma cells to prime oligosaccharide synthesis. Incorporation of alpha- and beta-dodecyl lactosides into B16 cells resulted in the sialylation of the galactose residue to give GM3-type oligosaccharides. The beta-dodecyl galactoside primer was sialylated but the alpha-dodecyl galactoside primer was not. Both the alpha- and beta-dodecyl glucoside primers were not elongated. In the glycosylation of primers by cells, this research confirmed that sialyl transferases tolerate acceptor modifications and are permissive to primer elongation regardless of the alpha- or beta-linkage to the aglycon unit. However, the presence of the terminal galactose residue that is beta-linked to the adjacent saccharide or aglycon unit is essential for sialylation by cellular enzymes to occur.