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. 2019 Jul 19;294(36):13366–13377. doi: 10.1074/jbc.RA119.008967

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© 2019 Gao et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 7. — Adropin^34–76 treatment decreased PKA phosphorylation and increased AKT phosphorylation of IP3R in the liver. A, the phosphorylation levels of PKA substrate sites (n = 4) and the phosphorylation levels of AKT substrate sites in IP3R1 following immunoprecipitation (IP) of IP3R1 as well as total IP3R1 levels in whole-tissue lysates (n = 4–5) were determined by Western blotting (IB). α-Tubulin was used as the loading control for whole-tissue IP3R1. The same α-tubulin band was used as the loading control for the blots of pJNK (Thr¹⁸³/Tyr¹⁸⁵) and total JNK (Fig. 4D). **, p < 0.01, adropin versus vehicle. Error bars, S.E.