Histone deacetylase 1; Histone deacetylase 3 (HDAC1; HDAC3)

Histone deacetylase 1 (HDAC1) and histone deacetylase 3 (HDAC3) are Class I HDAC enzymes that catalyze the removal of acetyl groups from lysine residues on histone and non-histone proteins, crucial for the regulation of chromatin structure and gene expression[1][4][5][7]. HDAC1 is strictly nuclear and constitutes part of large corepressor complexes, while HDAC3 shuttles dynamically between nucleus and cytoplasm, modulating diverse biological processes from circadian rhythm to inflammation[7][4]. Both HDAC1 and HDAC3 play essential roles in cell cycle regulation, apoptosis, differentiation, and the cellular response to stress and DNA damage[1][3][4]. Aberrant HDAC1/3 activity is implicated in cancer, neurodegeneration, inflammatory states, and fibrosis[2][4][6][8]. Several drugs targeting HDAC1/HDAC3, including FDA-approved HDAC inhibitors (vorinostat, romidepsin), are used in clinical cancer therapy, with ongoing efforts to develop more selective, safer inhibitors for broader indications[2][8]. HDACs also set the stage for combinatorial therapies in epigenetic and inflammatory diseases[2][6][8].

Other names

HDAC1 (for Histone deacetylase 1)HDAC3 (for Histone deacetylase 3)Histone deacetylase I (deprecated, sometimes used for early HDACs)Rpd3 homolog (context: yeast HDAC1)

Inhibition of HDAC enzyme activity: prevents removal of acetyl groups from histone and sometimes non-histone proteins, resulting in relaxed chromatin and upregulation of previously silenced gene transcription. Induction of cell cycle arrest, apoptosis, and differentiation, particularly in cancer cells. Modulation of inflammatory pathways (HDAC3 and NF-κB acetylation). Epigenetic reprogramming.