Histone acetylation, BET proteins, and periodontal inflammation

Abstract

Periodontitis is one of the most common inflammatory diseases in humans. The susceptibility to periodontitis is largely determined by the host response, and the severity of inflammation predicts disease progression. Upon microbial insults, host cells undergo massive changes in their transcription program to trigger an appropriate response (inflammation). It is not surprising that successful keystone pathogens have developed specific mechanisms to manipulate the gene expression network in host cells. Emerging data has indicated that epigenetic regulation plays a significant role in inflammation. Acetylation of lysine residues on histones is a major epigenetic modification of chromatin, highly associated with the accessibility of chromatin and activation of transcription. Specific histone acetylation patterns are observed in inflammatory diseases including periodontitis. Bromo‐ and extraterminal domain (BET) proteins recognize acetylated histones and then recruit transcription factors and transcription elongation complexes to chromatin. BET proteins are regulated in inflammatory diseases and small molecules blocking the function of BET proteins are promising “epi‐drugs” for treating inflammatory diseases.

Regulation of metabolism and inflammation: Links with oral and systemic health

“…Emerging evidence reports the significance of epigenetic regulation in driving inflammatory comorbidities, including periodontal diseases (Larsson et al, 2022). Clayton et al (2023) provided a comprehensive overview of epigenetic changes during periodontitis with a focus on histone acetylation and Bromo-and extraterminal domain (BET) proteins. Histone acetylation, a key epigenetic modification, enhances DNA accessibility and RNA transcription.…”