LPS-induced NF-κB activation requires Ca2+ as a mediator in isolated pancreatic acinar cells of rat

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Objective To investigate the effect of Ca2+ on lipopolysaccharide (IPS)-induced NF-KB activation in pancreatic acinar cells and the role of NF-κB in LPS-induced acinar cell injury.Methods Male rat pancreatic acinar cells were isolated by collagenase digestion, then exposed to varying concentrations of LPS (from 1 to 20 mg/L) in the presence or absence of EGTA. At various time points (30 minutes, 1 hour, 2 hours, 4 hours and 10 hours) after treatment with the agents, cell viability was determined by MTT. Nuclear translocation of NF-κB’ s subunit p65 was visualized by immunofluorescence staining and nuclei protein was extracted to perform EMSA which was used to assay the activity of NF-κB binding to the DNA sequence containing the recognition site of NF-κB.Results LPS induced cell damage in a time- and concentration-dependent manner while EGTA attenuated LPS-induced cell damage ( P < 0. 05) . NF-KB p65 immunofluorescence staining had increased intensity in the cytoplasm and indicated that nuclear tran Objective To investigate the effect of Ca2 + on lipopolysaccharide (IPS) -induced NF-KB activation in pancreatic acinar cells and the role of NF-κB in LPS-induced acinar cell injury. Methods Male rat pancreatic acinar cells were isolated by collagenase digestion, then At various time points (30 minutes, 1 hour, 2 hours, 4 hours and 10 hours) after treatment with the agents, cell (from 1 to 20 mg / viability was determined by MTT. Nuclear translocation of NF-κB ’s subunit p65 was visualized by immunofluorescence staining and nuclei protein was extracted to perform EMSA which was used to assay the activity of NF-κB binding to the DNA sequence containing the recognition site of NF-κB LPS induced cell damage in a time- and concentration-dependent manner while EGTA attenuated LPS-induced cell damage (P <0.05). NF-KB p65 immunofluorescence staining had increased intensity in the cytoplasm and indicated that nuclear tran
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