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![AGK exerts its function by regulating
NF-κB signaling. AsPC-1 and PANC-1 cells harboring NF-κB-driven
luciferase reporter were transfected with (A) AGK-overexpressing
plasmids or (B) AGK-targeting siRNAs for 48 h, followed by
dual-luciferase assay. (C) Representative western blots showing
Flag-AGK, p-IKKα/β, total IKKα/β, p-IκBα, total IκBα, and GAPDH in
AsPC-1 (left) and PANC-1 (right) cells transfected with EV or
Flag-AGK. (D) Quantitative analysis of the normalized ratio of
phosphorylated IKKα/β (p-IKKα/β) to total IKKα/β from panel C. (E)
Representative western blots showing p65 subcellular localization
in cytoplasmic and nuclear fractions of cells transfected with EV
or Flag-AGK. GAPDH (cytosolic) and H3 (nuclear) served as loading
controls. (F) Representative western blotting results of p-p65 and
total p65 in AGK-overexpressing AsPC-1 and PANC-1 cells. (G)
Quantitative analysis of the normalized ratio of phosphorylated p65
(p-p65) to total p65 from panel F. (H) Representative western
blotting results of p-p65 and total p65 in AGK-knockdown AsPC-1 and
PANC-1 cells. (I) Quantitative analysis of the normalized ratio of
phosphorylated p65 (p-p65) to total p65 from panel H. (J) Western
blot showing that p65 knockdown (si-p65) abolishes AGK-induced p65
phosphorylation. (K) Quantitative analysis of the normalized ratio
of phosphorylated p65 (p-p65) to total p65 from panel J. (L) qPCR
analysis showing that AGK-mediated upregulation of MYC mRNA is
dependent on p65. (M) CCK-8 assay demonstrating that p65 knockdown
attenuated AGK-induced cell proliferation. (N) AsPC-1 and (O)
PANC-1 cells overexpressed with AGK were incubated with vehicle or
0.5 µM QNZ for 48 h, followed by CCK-8 assay. Data were presented
as mean ± SD. *P<0.05, **P<0.01, ***P<0.001,
****P<0.0001. AGK, acylglycerol kinase; p-, phosphorylated; EV,
empty vector; si, short interfering; NC, negative control; qPCR,
quantitative PCR; QNZ.,
N4-[2-(4-phenoxyphenyl)ethyl]-1,2-dihydroquinazoline-4,6-diamine.](/article_images/or/56/2/or-56-02-09145-g03.jpg)
