Fig. 4: Functional analysis of O-glycans within the receptor-binding region of peptide hormones.
From: An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles
a Schematic depiction of the Thr7 O-glycan positioned within the receptor-binding domain of the glucagon hormone family (see Supplementary Fig. 7e). b Schematic depiction of the Thr32 O-glycan positioned within the receptor-binding domain of the NPY hormone family38. c Structural representation of the sialyl-T O-glycan. d Potencies (Log10(EC50)) of glycosylated GCG, VIP, and GLP-1 determined in cell-based receptor activation assays (n = 3 independent experiments in duplicate determinations for all groups, except non-glyc. GCG where n = 5). e Potencies of NPY and PYY in their Thr32 glycoforms determined and shown as in d (n = 3 for all groups). All error bars represent mean ± S.E.M. Two-tailed one-way ANOVA (Tukey’s post hoc test) was performed in d and e except for comparisons within NPY2R+PYY-; NPY5R+PYY-, and NPY5R+NPY-assays in e where two-tailed Student’s t-test was performed. ns not significant; *p < 0.05; **p < 0.01; ***p < 0.001 (all significant p-values are <0.0001 except d GCGR-Tn/GCGR-T p = 0.0149; e NPY2R-PYY-Non-glyc/NPY2R-PYY-Tn p = 0.0027; NPY2R-NPY/NPY2R-NPY-Tn p = 0.0002; NPY2R-NPY-Tn/NPY2R-NPY-T p = 0.0046). Source data for d and e are provided as a Source data file.
