Histone deacetylase 1, Histone deacetylase 2, Histone deacetylase 3, Histone deacetylase 8 (HDAC1, HDAC2, HDAC3, HDAC8)

Class I histone deacetylases (HDAC1, HDAC2, HDAC3, HDAC8) are enzymes that remove acetyl groups from ε-N-acetyl lysine residues of histone and non-histone proteins, a key process in chromatin remodeling and epigenetic regulation of gene expression[5][6][1]. These HDACs repress transcription by promoting chromatin condensation, control cell cycle progression, cellular differentiation, and apoptosis, and are linked to the pathogenesis of cancer and other diseases involving epigenetic dysregulation[7][8][2]. They act primarily as components of multiprotein complexes recruited to specific DNA loci[8]. HDACs are validated therapeutic targets, especially in oncology, with several approved and experimental HDAC inhibitors designed to modulate their activity and restore normal gene expression patterns.

Other names

HDAC1HDAC2HDAC3HDAC8Class I histone deacetylasesRpd3-like HDACs

Inhibition of HDAC activity increases acetylation of histone and non-histone proteins, leading to chromatin relaxation and increased transcription of silenced genes. This leads to induction of cell cycle arrest, promotion of apoptosis in malignant cells, and reactivation of tumor suppressor genes.