[No authors listed]
Heat stress may induce intestinal epithelial cell apoptosis; however, the molecular mechanisms have not yet been identified. The present study used IECâ6 rat small intestinal epithelial cells to investigate heat stressâinduced production of reactive oxygen species which may be involved in nuclear factor (NF)âκB activation during heat stress. IECâ6 cells were transfected with NFâκB p65âspecific small interfering RNA (siRNA), and observed a significant increase in cell apoptosis and caspaseâ3 cleavage; however, in cells transfected with adenovirus that constitutively overexpressed p65, the opposite results were obtained. Furthermore, p65 knockdown increased the heat stressâinduced expression and activity of heat shock transcription factor 1 (HSF1); conversely, p65 overexpression slightly decreased HSF1 activity. The levels of heat stressâinduced câJun phosphorylation were also examined: Knockdown of p65 resulted in a reduction of câJun phosphorylation, whereas p65 overexpression resulted in increased phosphorylation. Furthermore, siRNAâmediated knockdown of HSF1 in IECâ6 cells significantly increased heat stressâinduced apoptosis. Cells pretreated with câJun peptide, an inhibitor of câJun activation, exhibited a significant reduction in apoptosis. These findings indicated that heat stress stimulation in IECâ6 cells induced the proâapoptotic role of NFâκB by regulating HSF1 and câJun activation.
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