Glutaredoxin catalyzes glutathione-dependent disulfide oxidoreduction reactions in a coupled system with NADPH, GSH and glutathione reductase. Padilla et al. (1995) purified the human placental glutaredoxin.
General function
Cell death/survival, Apoptosis
Comment
Glutaredoxin is a glutathione-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. Glutaredoxin (Grx) is a small protein with oxidoreductase activity which is involved in the cellular defence against oxidative stress.
Garcia-Pardo et al. (1999) have studied the presence of glutaredoxin in the human ovary during the ovulatory cycle using polyclonal antibodies developed against recombinant human Grx. Immunostaining was only detected between days 15 and 23 of the cycle and was localized exclusively in the corpus luteum. Grx-positive cells corresponded to granulosa-derived luteal cells (GLC) whereas the remaining luteal cell types were not immunostained. Loss of Grx immunoreactivity was coincident with the appearance of morphological signs of structural luteolysis, such as the presence of apoptotic cells. Garcia-Pardo et al. (1999)suggest that Grx, as a cellular antioxidant, plays an important role in the mechanisms of human CL development. Rozell et al. (1993) reported a strong glutaredoxin immunoreactivity in oocytes in the ovary.