Journal: Scientific Reports
Article Title: GalNT2-mediated O-glycosylation affects pancreas development and function in mice
doi: 10.1038/s41598-024-80276-7
Figure Lengend Snippet: LC‒MS/MS analysis of PNA-purified proteins derived from the pancreas of WT and GalNT2-TG mice. (A) Comparative staining of Tn antigen (VVA) and core-1 (PNA) in tissue sections of adult WT and Cosmc-KO murine pancreata. The magnification is 200x. (B) Biosynthesis pathway of O-glycans. Starting from a polypeptide, selected serines and tyrosines are modified by GalNT2 (and other ppGalNAcTs) with O-GalNAc (Tn antigen). This glycan is elongated by T-synthase to core-1, which is bound by PNA. (C) Venn diagram of identified PNA-purified proteins from WT and GalNT2-TG pancreata ( n = 2 each) and pathway analysis of WT proteins, including common and exclusively TG-derived proteins.
Article Snippet: In brief, agarose-bound PNA (AL-1073, Vector Laboratories) was used to enrich nonsialylated core 1-modified proteins, along with their potential interactors, from pancreatic lysates of WT and GalNT2-TG het mice at 7 weeks of age (2 biological replicates per group).
Techniques: Purification, Derivative Assay, Staining, Modification