Mucin-type O-linked glycosylation is the most abundant form of O-linked glycosylation in higher eukaryotes. It begins with the addition of ?-N-acetyl-D-galactosamine (GalNAc) to<br/>serine and threonine residues of membrane-bound and secreted proteins initiated by a family of polypeptide N-acetylgalactosamine transferases (ppGalNAcTs). After the addition of the GalNAc residue, various glycosyltransferases further elaborate to create large structures of carbohydrates. Misregulation of the various glycosyltransferases or changes in the downstream elaborations have ties to various diseases such as cancer, hematological disorders, and Wiskott-Aldrick syndrome. Currently there is no specific metabolic chemical reporter (MCR) for mucin-type glycosylation. Here, we show efforts towards synthesizing MCRs specific for mucin-type glycosylation in hopes of revealing more about this abundant form of glycosylation.

Efforts in the development of a metabolic chemical reporter specific for mucin-type glycosylation

2019 Fall National Meeting

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