Introduction
O-linked glycosylation has commonly found in secreted and membrane-bound proteins and takes place in the Golgi. It refers to the binding of glycans to serine and threonine, following with a extent to hydroxyproline and hydroxylysine. The main type of O-glycosylation in secreted and membrane-bound proteins appears to be the addition of reducing terminal N-acetylgalactosamine (GalNAc). The O-linked glycan is also recognized as as 'mucin-type' glycan. In addition to the mucin-type O-linked glycans, many mammalian proteins present mannose (Man), fucose (Fuc), glucose (Glc), Gal or xylose (Xyl) as reducing terminal linkages. This group of O-linked glycan dominated protein localization and transportation, protein solubility, antigenicity and cell-cell interactions.
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Accord
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United States
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