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- W3108543863 abstract "Mucin-type O-glycans, based on GalNAc α-linked to Ser/Thr in protein backbones, are widespread throughout the animal kingdom. Their unique properties allow mucins to form an essential protective barrier on epithelial tissues in mammals. The biosynthesis of all O-glycans is initiated by the transfer of GalNAc to Ser or Thr residues on proteins located in the Golgi apparatus. This is followed by specific pathways that form four common O-glycan core structures. Further conversion into hundreds of complex O-glycans is accomplished by families of glycosyltransferases and sulfotransferases. Some of these enzymes are specific for the biosynthesis of O-glycans while others can act on additional substrates that include N-glycans and glycolipids. Mucin-type O-glycans have multiple functions. They bind bacteria and viruses, they function as receptors for carbohydrate binding proteins and are important components of the immune response. Glycosyltransferase expression and activity have been found to be abnormal in disease conditions. The structural characterization of these enzymes has revealed common protein folds and mechanisms, and this knowledge may be useful in understanding the assembly and alteration of O-glycans in disease, and to develop new tools for therapeutic modulations of O-glycosylation. This review summarizes the known biosynthesis of mucin-type O-glycans and their functions in health and disease." @default.
- W3108543863 created "2020-12-07" @default.
- W3108543863 creator A5058971301 @default.
- W3108543863 creator A5061857544 @default.
- W3108543863 date "2021-01-01" @default.
- W3108543863 modified "2023-09-23" @default.
- W3108543863 title "Mucin-Type O-Glycans: Biosynthesis and Functions" @default.
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