Abstract
Acetylation and deacetylation are posttranslational modifications (PTMs) which affect the regulation of chromatin structure and its remodeling. Acetylation of histone 3 at lysine placed on position 18 (H3K18Ac) plays an important role in driving progression of many types of cancer, including breast, colon, lung, hepatocellular, pancreatic, prostate, and thyroid cancer. The aim of this review is to analyze and discuss the newest findings regarding the role of H3K18Ac and acetylation of other histones in carcinogenesis. We summarize the level of H3K18Ac in different cancer cell lines and analyze its association with patients’ outcomes, including overall survival (OS), progression-free survival (PFS), and disease-free survival (DFS). Finally, we describe future perspectives of cancer therapeutic strategies based on H3K18 modifications.
Highlights
In eukaryotic cells, chromatin structure is highly organized and is divided into basic repeating units called nucleosomes
This study has shown that the IFNγ-producing cells of the host immune system counteract the silencing of GPR109A mediated by DNA methylation to suppress cancer development [111]
H3K18ac levels were observed in hepatocellular carcinoma (HCC) cells compared to non-tumor hepatocytes, and SIRT7 expression was weakly correlated with H3K18Ac. These results suggest that other mechanisms may be involved in deacetylation of H3K18Ac in HCC [113]
Summary
Chromatin structure is highly organized and is divided into basic repeating units called nucleosomes. N-tails of histones within the nucleosome octamer are considered a well-known target for specific chromatin epigenetic posttranslational modifications (PTMs) [14,15]. Removal of acetyl-groups from lysine residues by HDACs has an impact on chromatin integrity [33,34,35,36]. Removal of acetyl-groups from lysine residues by HDACs has an impact on compaction through interaction between positively charged N-tail histone residues and negatively chromatin compaction through interaction between positively charged N-tail histone residues and charged DNA. Acetylation lysine residues causes relaxation of chromatin structure and provides easier access for transcription factors (TF). Removal of acetyl-groups (gray) from lysine residues leads to chromatin compaction and its inactivation [38]. Complexes, associated with a widesurvival, spectrum cellular activities, includingremodeling cell proliferation, In general, histone acetylation occurs in two different states. We present a short description and classification of HATs and HDACs and the
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