Abstract
Acetylation and deacetylation of histones have important roles in transcriptional regulation in eukaryotic cells. 1 Glozak MA Seto E Histone deacetylases and cancer. Oncogene. 2007; 26: 5420-5432 Crossref PubMed Scopus (776) Google Scholar The acetylation status of histones is decided by the activity of histone acetyltransferases (HATs) and histone deacetylases (HDACs). HATs acetylate the ɛ-amino group of lysine residues on histones, thereby neutralising their positive charge and diminishing their ability to bind negatively charged DNA. An open chromatin configuration provides accessibility for transcription factors. Cross-talk between histone acetylation or methylation and DNA methylation has profound implications for gene expression. HDACs remove the acetyl groups, thereby allowing compacted chromatin to reform. So far, 18 HDAC isoforms have been identified and classified based on homology with yeast HDACs. HDACs also have many non-histone protein substrates, such as transcription factors and signal transduction mediators. Association of patterns of class I histone deacetylase expression with patient prognosis in gastric cancer: a retrospective analysisHigh HDAC expression is significantly associated with nodal spread and is an independent prognostic marker for gastric cancer. Additionally, we postulate that immunohistochemical detection of HDAC as a companion diagnostic method might predict treatment response to HDIs, thereby enabling selection of patients for this specific targeted treatment in gastric cancer. Full-Text PDF
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