The p50 homodimer is capable of suppressing the transactivation activities of NF-κB by occupying the same κB sites and recruiting corepressor complexes containing histone deacetylases (HDAC) [56]. We found that the p50 homodimer is the dominant κB binding factor in the human PFC. Bioinformatic analysis demonstrated that the proportion of genes with putative κB elements was significantly higher in the set of genes upregulated in the PFC of alcoholics compared to the set of downregulated genes. The most plausible explanation for these observations is that in alcoholics the p50 homodimer-induced repression of gene transcriptions weakens due to the p50 homodimer downregulation thus allowing the recruitment of NF-κB that activates transcription from κB elements.
