Fig. 5

Western blot analysis showed that knockdown of GSTM1 by siRNA decreased the phosphorylated levels of NF-kB p65 and STAT3 (pSer727) and a model to summarize the results in this report was presented. a Western blot analysis showed that knockdown of GSTM1 in U87 cells at 48 h decreased the phosphorylated NF-kB p65 (phospho-p65) and phosphorylated STAT3 (pSer727) levels, but not the phosphorylated MAP kinase levels. The average levels of proteins from densitomer scanning normalized by β-actin were shown in the bottom of the protein bands. Bar graph showed the levels of different proteins that were quantified and normalized with β-actin by Western blot analysis (triplicate results were shown in Fig. 5a, Additional file 1: Fig. S5). Data from three independent experiments are expressed as mean ± s.d. The asterisk (*) indicated statistical significance (P < 0.05) between GSTM1 siRNA and scrambled siRNA groups. b A model summarizes that GSTM1 overexpression induces the STAT3 and NF-kB pathways. The possible mechanism may go through GSH-conjugated targets that subsequently induce the phosphorylation of STAT3 and/or NF-kB p65