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• W2301803950 endingPage "C351" @default.
• W2301803950 startingPage "C344" @default.
• W2301803950 abstract "Supraphysiological concentrations of cholecystokinin (CCK) induce chemokine expression in rat pancreatic acini through the activation of the transcription factor NF-kappaB. In the current study, the intracellular signals involved in these pathophysiological effects of CCK were investigated. CCK induction of mob-1 expression in isolated rat pancreatic acini was blocked by the protein kinase C (PKC) inhibitors GF-109203X and Ro-32-0432 and by the intracellular Ca(2+) chelator BAPTA. CCK induced NF-kappaB nuclear translocation, and DNA binding was also blocked by GF-109203X and BAPTA. Direct activation of PKC with TPA induced mob-1 chemokine expression and activated NF-kappaB DNA binding to a similar extent as did CCK. Increasing intracellular Ca(2+) using ionomycin had no effect on mob-1 mRNA levels or NF-kappaB activity. Both CCK and TPA treatments decreased inhibitory kappaB-alpha (IkappaB-alpha) levels, whereas ionomycin had no effect. However, the effects of TPA on IkappaB-alpha degradation were less complete than for CCK. In combination, TPA and ionomycin degraded IkappaB-alpha to a similar extent as CCK. Therefore, activation of NF-kappaB and mob-1 expression by supraphysiological CCK is likely mediated by both PKC activation and elevated intracellular Ca(2+)." @default.
• W2301803950 created "2016-06-24" @default.
• W2301803950 creator A5028009560 @default.
• W2301803950 creator A5070360488 @default.
• W2301803950 date "2000-02-01" @default.
• W2301803950 modified "2023-09-24" @default.
• W2301803950 title "CCK stimulates<i>mob</i>-1 expression and NF-κB activation via protein kinase C and intracellular Ca²⁺" @default.
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• W2301803950 doi "https://doi.org/10.1152/ajpcell.2000.278.2.c344" @default.
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