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. 2019 Feb 1;54(4):1183–1194. doi: 10.3892/ijo.2019.4707

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Copyright: © Chen et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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The H3K27 acetylation process is mediated by CBP. (A) CBP level was detected in OSCC and HOK cells via an immunofluorescence assay. (B) The enrichment of CBP at PLAC2 promoter was assessed in cells with a chromatin immunoprecipitation assay. ^*P<0.05. (C) The knockdown effect of si-CBP was evaluated with a western blot analysis assay. (D) The enrichment of H3K27ac was assessed in cells with CBP knockdown, ^*P<0.05, compared with CAL-27 or SCC-9 cells. (E) Reverse transcription-quantitative polymerase chain reaction was used to determine the expression level of PLAC2 in OSCC cells upon knockdown of CBP. ^*P<0.05 compared with the si-NC group. PLAC2, placenta-specific protein 2; CBP, cAMP-response element binding protein-binding protein; H3K27ac, histone H3 on lysine 27 acetylation; OSCC, oral squamous cell carcinoma; si, small interfering; NC, negative control.