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Histone deacetylase (HDAC) inhibitors block enzymes that remove acetyl groups from histones and other proteins. Deacetylation compacts chromatin and generally represses transcription, so HDAC inhibitors are widely used to study gene regulation. Trichostatin A was characterized in 1990 as a specific inhibitor of mammalian histone deacetylase. The first mammalian HDAC was cloned in 1996 and found to be related to the yeast transcriptional regulator Rpd3p. Isoform-selective tools include entinostat for HDAC1 and HDAC3, and Tubastatin A HCl for HDAC6, a microtubule-associated deacetylase. Broad-spectrum hydroxamates such as vorinostat and panobinostat, together with the cyclic depsipeptide romidepsin, complete the range.
