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- W2118002029 abstract "Mucin-type O-linked glycoproteins are involved in a variety of biological interactions in higher eukaryotes. The biosynthesis of these glycoproteins is initiated by a family of polypeptide N-acetyl-alpha-galactosaminyltransferases (ppGalNAcTs) that modify proteins in the secretory pathway. The lack of a defined consensus sequence for the ppGalNAcTs makes the prediction of mucin-type O-linked glycosylation difficult based on primary sequence alone. Herein we present a method for labeling mucin-type O-linked glycoproteins with a unique chemical tag, the azide, which permits their selective covalent modification from complex cell lysates. From a panel of synthetic derivatives, we identified an azido GalNAc analog (N-azidoacetylgalactosamine, GalNAz) that is metabolized by numerous cell types and installed on mucin-type O-linked glycoproteins by the ppGalNAcTs. The azide serves as a bioorthogonal chemical handle for selective modification with biochemical or biophysical probes using the Staudinger ligation. The approach was validated by labeling a recombinant glycoprotein that is known to possess O-linked glycans with GalNAz. In addition, GalNAz efficiently labeled mucin-type O-linked glycoproteins expressed at endogenous levels. The ability to label mucin-type O-linked glycoproteins with chemical tags should facilitate their identification by proteomic strategies." @default.
- W2118002029 created "2016-06-24" @default.
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- W2118002029 date "2003-12-01" @default.
- W2118002029 modified "2023-10-16" @default.
- W2118002029 title "A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation" @default.
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- W2118002029 doi "https://doi.org/10.1073/pnas.2335201100" @default.
- W2118002029 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/299823" @default.
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