Irish journal of medical science · 2017
CCK1 receptor is involved in the regulation of protein lysine acetylation in GBC-SD cells and gallbladder carcinoma.
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Wu W, Ouyang B, Lu Z, Liu H, Tan Y, Cui P
Аннотация
BACKGROUND: CCK1 (cholecystokinin receptor 1) and protein lysine acetylation were associated with several cancers, respectively. However, whether they are involved in the alternation of gallbladder carcinoma is unknown.
AIMS: This study investigated the characteristics of CCK1 and protein lysine acetylation in GBC-SD cells and carcinoma of gallbladder.
METHODS: The expression and localization of CCK1 were detected by western blot analysis and indirect immunofluorescence. GBC-SD cells were treated with CCK-8 and CCK-8+CCK1 inhibitor. The protein lysine acetylation from cells, as well as tissues of gallbladder carcinoma, was examined by western blotting.
RESULTS: CCK1 receptor was expressed and localized in the GBC-SD cells. The synthetic octapeptide of CCK (CCK-8) could accelerate the lysine acetylation of a subset of proteins in dose-dependent manners in GBC-SD cells. Further investigation demonstrated that the specific inhibitor (CR1409) of CCK1 receptor could attenuate the CCK8-induced increase of protein lysine acetylation. In addition, we revealed that the rise of CCK1 receptor expression is associated with the increase of protein lysine acetylation in tissues from carcinoma of gallbladder.
CONCLUSIONS: CCK might regulate protein lysine acetylation via CCK1 receptor.
AIMS: This study investigated the characteristics of CCK1 and protein lysine acetylation in GBC-SD cells and carcinoma of gallbladder.
METHODS: The expression and localization of CCK1 were detected by western blot analysis and indirect immunofluorescence. GBC-SD cells were treated with CCK-8 and CCK-8+CCK1 inhibitor. The protein lysine acetylation from cells, as well as tissues of gallbladder carcinoma, was examined by western blotting.
RESULTS: CCK1 receptor was expressed and localized in the GBC-SD cells. The synthetic octapeptide of CCK (CCK-8) could accelerate the lysine acetylation of a subset of proteins in dose-dependent manners in GBC-SD cells. Further investigation demonstrated that the specific inhibitor (CR1409) of CCK1 receptor could attenuate the CCK8-induced increase of protein lysine acetylation. In addition, we revealed that the rise of CCK1 receptor expression is associated with the increase of protein lysine acetylation in tissues from carcinoma of gallbladder.
CONCLUSIONS: CCK might regulate protein lysine acetylation via CCK1 receptor.