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. Author manuscript; available in PMC: 2018 Dec 1.
Published in final edited form as: Gastroenterology. 2017 Aug 30;153(6):1555–1567.e15. doi: 10.1053/j.gastro.2017.08.038

Figure 3. Gastrin mediated nuclear export of menin via CCKBR requires PKA.

Figure 3

(A) Representative blot showing phospho-PKA substrates in glial cultures isolated from mice (GAPDH, loading control). (B) Representative blot (top) and quantitation of PKA-cα expression (bottom) in nuclear fractions of glial cultures isolated from mice (n=8–10 mice). (C) PKA activity in glial cultures, expressed as units of enzyme activity (U) normalized to protein content of cell lysates (mg) (n=8 mice). (D) IF staining of menin in glial cultures isolated from duodenal lamina propria of C57 WT mice and treated with or without gastrin (20 nM, 8 h) in the presence or absence of 10 μM H-89 and KT5720 (KT), and forskolin (10 μM, 4 h). (E) Representative blots and quantitation of menin expression (F) in nuclear and cytoplasmic fractions of glial cultures isolated from C57WT mice and treated with or without gastrin (20 nM, 8 h), in the presence or absence of 10 μM H-89, KT5720 (KT) and forskolin (10 μM, 4 h). Data shown are the Median ± Interquartile Range of median. * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001. Scale bars: (D) – 20 μm