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Investigating the effect of Fuc-O-NAP on the glycosylation of Helicobacter pylori Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2024-01-01
Creator: Panhasith Ung
Access: Access restricted to the Bowdoin Community
Probing mucin-type O-linked glycosylation in living animals
Date: 2006-03-28
Creator: Danielle H. Dube, Jennifer A. Prescher, Chi M. Quang, Carolyn R. Bertozzi
Access: Open access
- Changes in O-linked protein glycosylation are known to correlate with disease states but are difficult to monitor in a physiological setting because of a lack of experimental tools. Here, we report a technique for rapid profiling of O-linked glycoproteins in living animals by metabolic labeling with N-azidoacetylgalactosamine (GalNAz) followed by Staudinger ligation with phosphine probes. After injection of mice with a peracetylated form of GalNAz, azide-labeled glycoproteins were observed in a variety of tissues, including liver, kidney, and heart, in serum, and on isolated splenocytes. B cell glycoproteins were robustly labeled with GalNAz but T cell glycoproteins were not, suggesting fundamental differences in glycosylation machinery or metabolism. Furthermore, GalNAz-labeled B cells could be selectively targeted with a phosphine probe by Staudinger ligation within the living animal. Metabolic labeling with GalNAz followed by Staudinger ligation provides a means for proteomic analysis of this posttranslational modification and for identifying O-linked glycoprotein fingerprints associated with disease. © 2006 by The National Academy of Sciences of the USA.