It is hypothesized that activation of death receptors disrupts the redox homeostasis of cells
and that this contributes to the induction of apoptosis. The redox status of the peroxiredoxins …

Various proapoptotic stimuli increase the production of superoxide and H 2 O 2 by
mitochondria. Whereas superoxide impairs mitochondrial function and is removed by Mn 2+ …

Cell death pathways such as apoptosis can be activated in response to oxidative stress,
enabling the disposal of damaged cells. In contrast, controlled intracellular redox events are …

Isothiocyanates are phytochemicals with anti-cancer properties that include the ability to
trigger apoptosis. A substantial body of evidence suggests that reaction of the electrophilic …

Cellular redox is controlled by the thioredoxin (Trx) and glutathione (GSH) systems that
scavenge harmful intracellular reactive oxygen species (ROS). Oxidative stress also evokes …

Peroxiredoxins decompose peroxides through reversible oxidation of their active site
cysteines. The redox state of the 2-Cys peroxiredoxins, 1, 2 and 3, was investigated in …

Peroxiredoxin II, a cytosolic isoform of the antioxidant enzyme family, has been implicated in
cancer-associated cell death and apoptosis, but its functional role in the heart remains to be …

The proteomics analysis reported here shows that a major cellular response to oxidative
stress is the modification of several peroxiredoxins. An acidic form of the peroxiredoxins …

Peroxiredoxin 5 is a mammalian thioredoxin peroxidase ubiquitously expressed in tissues.
Peroxiredoxin 5 can be intracellularly localized to mitochondria, peroxisomes, the cytosol …

Thioredoxin‐2 (Trx‐2) is a mitochondria‐specific member of the thioredoxin superfamily.
Mitochondria have a crucial role in the signal transduction for apoptosis. To investigate the …