Histone deacetylase 2 (HDAC2) (HDAC2)

Histone deacetylase 2 (HDAC2) is a Class I enzyme that plays a critical role in epigenetic regulation by removing acetyl groups from lysine residues on histone tails [1]. This deacetylation process promotes chromatin condensation, which typically leads to the transcriptional repression of various genes [2]. HDAC2 is often found within large multi-protein complexes like NuRD and Sin3, which are essential for its stability and recruitment to specific DNA sites [3]. In many types of cancer, HDAC2 is overexpressed, contributing to the silencing of tumor suppressor genes and promoting uncontrolled cell proliferation [4]. Beyond oncology, HDAC2 has been identified as a key negative regulator of synaptic plasticity and memory formation, making it a target for treating neurodegenerative diseases like Alzheimer's [5]. Sodium propionate is a short-chain fatty acid that functions as a non-selective inhibitor of HDAC2 and other Class I and IIa HDACs [6]. By inhibiting the enzymatic activity of HDAC2, sodium propionate induces histone hyperacetylation, which can restore the expression of silenced genes and exert anti-inflammatory effects [7]. Therapeutic targeting of HDAC2 with small molecules like sodium propionate or more potent synthetic inhibitors remains a significant area of research for both cancer and cognitive disorders [8].

Other names

HDAC2RPD3Histone deacetylase 2Mammalian RPD3

Histone deacetylase 2 (HDAC2) catalyzes the removal of acetyl groups from the N-terminal lysine residues of histones H3 and H4, facilitating chromatin condensation and transcriptional repression [1, 2]. Sodium propionate acts as a competitive inhibitor that binds to the zinc-containing catalytic site of the enzyme, preventing deacetylation and leading to histone hyperacetylation and the activation of previously silenced genes [6, 7].