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Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria
- Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria
- Chang T.-S.; Cho C.-S.; Park S.; Yu S.; Sang W.K.; Sue G.R.
- Ewha Authors
- 이서구; 강상원; 창동신
- SCOPUS Author ID
- 이서구; 강상원; 창동신
- Issue Date
- Journal Title
- Journal of Biological Chemistry
- Journal of Biological Chemistry vol. 279, no. 40, pp. 41975 - 41984
- SCI; SCIE; SCOPUS
- Document Type
- Various proapoptotic stimuli increase the production of superoxide and H 2O 2 by mitochondria. Whereas superoxide impairs mitochondrial function and is removed by Mn 2+-dependent superoxide dismutase, the role and metabolism of mitochondrial H 2O 2 during apoptosis have remained unclear. The effects on apoptotic signaling of depletion of peroxiredoxin (Prx) III, a mitochondrion-specific H 2O 2-scavenging enzyme, have now been investigated by RNA interference in HeLa cells. Depletion of Prx III resulted in increased intracellular levels of H 2O 2 and sensitized cells to induction of apoptosis by staurosporine or TNF-α. The rates of mitochondrial membrane potential collapse, cytochrome c release, and caspase activation were increased in Prx III-depleted cells, and these effects were reversed by ectopic expression of Prx III or mitochondrion-targeted catalase. Depletion of Prx III also exacerbated damage to mitochondrial macromolecules induced by the proapoptotic stimuli. Our results suggest that Prx III is a critical regulator of the abundance of mitochondrial H 2O 2, which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling.
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