Histone deacetylase class I/IV (HDAC class I/IV)

Histone deacetylases are enzymes that remove acetyl groups from lysine residues on the N-terminal tails of core histones as well as from non-histone proteins. This action leads to chromatin condensation and transcriptional repression by increasing the positive charge on histones, thereby strengthening their interaction with DNA. The human genome encodes several classes of HDACs: Class I includes HDAC1, 2, 3, and 8—primarily nuclear enzymes involved in regulating gene expression through chromatin remodeling. Class IV consists solely of HDAC11. Both classes play critical roles in cellular processes such as cell cycle progression, apoptosis regulation, differentiation, inflammation modulation via transcription factors like MEF2 or HIF pathways (notably for some members), and metabolic homeostasis. Aberrant activity or expression has been implicated in cancer development/progression as well as other diseases such as neurodegeneration and inflammatory disorders. Several small-molecule inhibitors targeting these enzymes have been developed for therapeutic use—especially in oncology—by promoting hyperacetylation that reactivates silenced genes involved in growth inhibition or apoptosis.[1][4][5][6]

Other names

HDACsHistone deacetylasesClass I histone deacetylasesClass IV histone deacetylase (HDAC11)

Inhibition of histone deacetylation leading to increased acetylation of histones and non-histone proteins, resulting in altered gene expression and induction of cell cycle arrest or apoptosis in cancer cells[1][4].