Fig. 2 Characterizing GLP1R signaling pathways and pharmacology activated by eGLP1-MALAT1-ASO (•) and eGLP1-FOXO1-ASO (▪) compared to eGLP1 peptide (○)

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Fig. 2 Characterizing GLP1R signaling pathways and pharmacology activated by eGLP1-MALAT1-ASO (•) and eGLP1-FOXO1-ASO (▪) compared to eGLP1 peptide (○) and exenatide (ρ). Characterizing GLP1R signaling pathways and pharmacology activated by eGLP1-MALAT1-ASO (•) and eGLP1-FOXO1-ASO (▪) compared to eGLP1 peptide (○) and exenatide (ρ). (A) Displacement of 125I-GLP1 in membranes from GLP1R overexpressing HEK293. eGLP1-MALAT1-ASO (•) and eGLP1-FOXO1-ASO (▪) displaced 125I-GLP1 equally well as the eGLP1 peptide (○) and exenatide (ρ). Functional assays measuring G protein signaling by (B) DMR and (C) cAMP accumulation in GLP1R-HEK293 cells showed that eGLP1-MALAT1-ASO (•) and eGLP1-FOXO1-ASO (▪) were equally potent as the eGLP1 peptide (○) and exenatide (△), with only minor impact from conjugation of MALAT1-ASO and FOXO1-ASO to the eGLP1 peptide. (D) β-Arrestin2 recruitment in GLP1R-CHO-K1 and (E) receptor internalization in GLP1R-U2OS using PathHunter assays showed similar potencies for eGLP1, exenatide, and ASO-conjugated eGLP1, but with reduced maximal effect for both eGLP1-MALAT1-ASO (•) and eGLP1-FOXO1-ASO (▪). Data are presented as mean ± SEM using exenatide as reference for 100% effect. (F) Effect of 10 nM exenatide (ρ), eGLP1-Ctrl-ASO (x), FOXO1-ASO (□), eGLP1-FOXO1-ASO (▪), MALAT1-ASO (○), or eGLP1- MALAT1-ASO (•) on glucose GSIS in human reconstituted islet microtissues. Islets were treated with high glucose, and the compounds and insulin content were measured in the culture medium. Data were normalized to secretion at 11 mM glucose and presented as geometric mean ± 95% confidence interval (CI). Statistical analysis by one-way analysis of variance (ANOVA) adjusted for multiple comparisons. C. Ämmälä et al. Sci Adv 2018;4:eaat3386 Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).