Abstract
T‑cell acute lymphoblastic leukemia (T‑ALL) is a hematopoietic malignancy, which is associated with a poor prognosis. It is difficult to achieve complete remission or long‑term survival with conventional chemotherapy, partly due to decreased apoptosis. However, necroptosis can serve as an alternative pathway to induce cell death. The present study investigated whether the selective histone deacetylase (HDAC) inhibitor chidamide exerted a therapeutic effect on T‑ALL and explored the underlying mechanism. The results revealed that HDAC expression was increased in Jurkat and HUT‑78 cells treated compared with the control cell line (H9), and was accompanied by elevated cellular Fas‑associated death domain‑like interleukin‑1β converting enzyme inhibitory protein long form (c‑FLIPL) levels. Chidamide treatment (2 µmol/l) also induced mitochondrial dysfunction, necroptosis and apoptosis in T‑ALL cells in vitro. Furthermore, necroptosis was increased when apoptosis was blocked in T‑ALL cells. Additionally, chidamide (2 µmol/l) downregulated c‑FLIPL, HDAC1 and HDAC3 expression, and increased receptor‑interacting protein kinase 3 expression and the phosphorylation of mixed lineage kinase domain‑like pseudokinase in Jurkat and HUT‑78 cells. The results obtained in the present study revealed that chidamide may induce necroptosis via regulation of c‑FLIPL expression when apoptosis is inhibited in Jurkat and HUT‑78 cells.