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.
Dall'Olio F. (2000). The sialyl-α2,6-lactosaminyl-structure: Biosynthesis and functional role. GLYCOCONJUGATE JOURNAL, 17(10), 669-676 [10.1023/A:1011077000164].
The sialyl-α2,6-lactosaminyl-structure: Biosynthesis and functional role
Dall'Olio F.
2000
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.