Direct binding of NF-κB p65 protein to STC1 promoter and regulated the expression of STC1.

Abstract

<p>(A) The binding sites of STC1 were tested in CaSki cells by chromatin coimmunoprecipitation. The site was found to bind to NFκB p65. (B) Western blotting detected the activity of PARP, caspase-3, STC1, and NF-κB p65 in CaSki cells. CaSki cells were treated with thapsigargin (3 µM) for 12 h. (C) Western blotting detected the activity of p65, STC1, and caspase-3 in CaSki cells. CaSki cells were treated with increasing time of TNFα (10 mg/L) for 2.5 h. (D) Western blotting detected the activity of p65 and STC1 in CaSki cells. CaSki cells were treated with PDTC (10 µM) for 60 min. (E) Subcellular activity of p65 and STC1 in CaSki cells was analyzed by Western blotting. CaSki cells were treated with siRNA knockdown of p65 for 72 h. (F) The expression of p65 and STC1 in CaSki was detected by RT-PCR at mRNA level. CaSki cells were treated with siRNA knockdown of p65 for 48 h. (G) Schematic representation of some findings in this work.</p