Lycorine induces cell-cycle arrest in the G0/G1 phase in K562 cells via HDAC inhibition

Li, Lv; Dai, Hong-Juan; Ye, Mao; Wang, Shu-Ling; Xiao, Xiao-Juan; Zheng, Jie; Chen, Hui-Yong; Luo, Yu-hao; Liu, Jing

Histone acetylation and deacetylation regulate the chromatin structure and gene activation. Histone acetylation is catalyzed by histone acetyltransferases (HATs) and associated with transcriptional activation, whereas histone deacetylation is mediated by histone deacetylases (HDACs) and correlated with chromatin condensation and transcriptional repression [3] . Both of these processes play crucial roles in various biological functions, including cell growth, differentiation, and apoptosis. Dysregulation of these pathways contributes to human cancer development. Several studies have indicated that HDAC inhibitors, compounds that interfere with the function of HDAC, exhibit antitumor activity against various tumor cells by blocking cell cycle progression and inducing apoptosis. Sodium butyrate, an HDAC inhibitor, can suppress breast cancer cell proliferation by blocking the G1/S phase of the cell cycle and activating the apoptosis pathway [4] . Two HDAC inhibitors, suberoylanilide hydroxamic acid (Vorinostat) and romidepsin (Depsipeptide, FK228), were recently approved by the U.S. Food and Drug Administration (USA) for the treatment of cutaneous T-cell lymphoma [5] .