The sialyl-α2,6-lactosaminyl-structure: Biosynthesis and functional role

被引：90

作者：

Dall'Olio F. ^{[1
]}

机构：

[1] Dipto. di Patologia Sperimentale, Universita di Bologna, 40126 Bologna

来源：

Glycoconjugate Journal | 2000年 / 17卷 / 10期

关键词：

α2,6-sialylation; CD22; CDw75; Glycosyltransferases; Sialyltransferases; ST6Gal.I;

D O I：

10.1023/A:1011077000164

中图分类号：

学科分类号：

摘要：

Sialylation represents one of the most frequently occurring terminations of the oligosaccharide chains of glycoproteins and glycolipids. Sialic acid is commonly found α2,3- or α2,6-linked to galactose (Gal), α2,6-linked to N-acetylgalactosamine (GalNAc) or α2,8-linked to another sialic acid. The biosynthesis of the various linkages is mediated by the different members of the sialyltransferase family. The addition of sialic acid in α2,6-linkage to the galactose residue of lactosamine (type 2 chains) is catalyzed by β-galactoside α2,6-sialyltransferase (ST6Gal.I). Although expressed by a single gene, this enzyme shows a complex pattern of regulation which allows its tissue- and stage-specific modulation. The cognate oligosaccharide structure, NeuAca2,6Gal.β1,4GIcNAc, is widely distributed among tissues and is involved in biological processes such as the regulation of the immune response and the progression of colon cancer. This review summarizes the current knowledge on the biochemistry of ST6Gal.I and on the functional role of the sialyl-α2,6-Lactosaminyl structure.

引用

页码：669 / 676

页数：7

共 140 条

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