Coenzyme Q0, a quinone derivative from Antrodia camphorata, triggered ROS-mediated cytoprotective autophagy in human promyelocytic leukemia cells

Abstract Our previous investigation revealed that Coenzyme Q 0 (CoQ 0 ), a quinone derivative from Antrodia camphorata , triggered ROS-dependent voltage-dependent anion channel 1 (VDAC-1)-mediated apoptosis in human promyelocytic leukemia (HL-60) cells. This research examined the efficacies of CoQ 0 (0–7 μM) on autophagy induction and the interaction between apoptosis and autophagy in HL-60 cells. CoQ 0 -triggered autophagy was associated with LC3-I/II accumulation, p62/SQSTM1 activation, autolysosome AVOs formation, ATG4B inhibition, ATG5/ATG7 expression, and Beclin-1/Bcl-2 dysregulation in HL-60 cells. Additionally, antioxidant N -acetylcysteine (NAC) prevented CoQ 0 -induced autophagy in HL-60 cells. Surprisingly, CoQ 0 -triggered cell death was enhanced by autophagy inhibitor 3-MA or CQ, indicating that autophagy acts as a survival mechanism. Additionally, autophagy suppression via 3-MA and/or CQ inhibitors strengthened the CoQ 0 -induced ROS generation and apoptosis (caspase-3 activation). Apoptosis suppression by caspase inhibitor Z -VAD-FMK or VDAC-1 silencing prevented the CoQ 0 -enhanced autophagy in HL-60 cells. Therefore, CoQ 0 together with autophagy inhibitors could be a potential therapy for human promyelocytic leukemia. • CoQ 0 , a quinone derivative from Antrodia camphorata , provoked autophagy in HL-60 cells. • NAC prevented CoQ 0 -induced autophagy indicating that CoQ 0 provoked ROS-arbitrated autophagy. • Autophagy suppression strengthened the CoQ 0 -induced ROS generation and apoptosis. • Apoptosis suppression or VDAC-1 silencing prevented the CoQ 0 -enhanced autophagy.