H 2 S stimulated bioenergetics in chicken erythrocytes and the underlying mechanism

The production of H S and its effect on bioenergetics in mammalian cells may be evolutionarily preserved. Erythrocytes of birds, but not those of mammals, have the nucleus and mitochondrion. In the present study, we reported the endogenous production of H S in chicken erythrocytes, which was mainly catalyzed by 3-mercaptopyruvate sulfur transferase (MST). ATP content of erythrocytes was increased by MST-generated endogenous H S under normoxic, but not hypoxic conditions. NaHS, a H S salt, increased ATP content under normoxic, but not hypoxic condition. ATP contents in the absence or presence of NaHS were eliminated by different inhibitors for mitochondrial electron transport chain in chicken erythrocytes. Succinate and glutamine, but not glucose, increased ATP content. NaHS treatment similarly increased ATP contents in the presence of glucose, glutamine or succinate, respectively. Furthermore, the expression and activity of sulfide quinone oxidoreductase were enhanced by NaHS. The structural integrity of chicken erythrocytes was largely maintained during 2-week NaHS treatment in vitro while most of erythrocytes without NaHS treatment were lysed. In conclusion, H S may regulate cellular bioenergetics as well as cell survival of chicken erythrocytes, in which the functionality of electron transport chain is involved. H S may have different regulatory roles and mechanisms in bioenergetics of mammalian and bird cells.