Mucin-type glycosylation

Seitz O, Kunz H, A novel allylic anchor for solid-phase synthesis of protected and unprotected O-glycosylated mucin-type glycopeptides, Angew. Chem. Int. Ed. Engl., 34 803-805, 1995. 

Seitz and Kunz advanced the art of solid-phase synthesis by developing a novel allylic anchor (Hycron) whose virtues were exemplified in a synthesis of protected and unprotected O-glycosylated Mucin-type ycopeptides. Anchoring though allyl esters not only allows peptide derivatives to be detached without affecting acid- and base-labile structural elements, but also provides orthogonal... 

H. C. Hang and C. R. Bertozzi, The chemistry and biology of mucin-type O-linked glycosylation, Bioorg. Med. Chem., 13 (2005) 5021-5034. 

Figure 14.2 Representative oligosaccharide structures found on mammalian glycoproteins and glycolipids. The complex oligosaccharides may be bi-, tri-, or tetra-antennary the branches may be more or less elongated with 1—>4 linked lactosamine units, and they may or may not be sialylated. The SLex, Lea, and Leb structures represent the different blood group determinants often present on lipids, and the elongated core 2 structure is a mucin-type glycosylation. Proteoglycans have a common core to which a variety of linear acidic polysaccharides are attached.

Spiro R.G. (2002). Protein glycosylation nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12 43R-56R Strous G.J. and Dekker J. (1992) Mucin-type glycoproteins. Crit Rev Biochem Mol Biol 27,... 

Hansen, J. E., Lund, O., Tolstrup, N., Gooley, A. A., Williams, K. L. Brunak, S. (1998). NetOglyc prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility. Glycoconj J15,115-30. 

Unlike A-glycosylation that always begins with en bloc transfer of the Glc3Man9GlcNAc2 14-mer core structure, mucin-type... 

Dube DH, Prescher JA, Quang CN, Bertozzi CR. Probing mucin-type O-linked glycosylation in living animals. Proc. Natl. Acad. Sci. U.S.A. 2006 103 4819-4824. 

Here, we delineate the biosynthetic pathways of the most common types of protein glycosylation occurring in the secretory pathway mucin-type O-linked glycosylation, A-linked glycosylation, and the formation of glycosaminoglycans. In addition, we will briefly visit the biosynthesis of some less-common varieties of protein glycosylation. 

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