| First Author | Zhou S | Year | 2013 |
| Journal | Int J Biochem Cell Biol | Volume | 45 |
| Issue | 2 | Pages | 401-7 |
| PubMed ID | 23164639 | Mgi Jnum | J:213113 |
| Mgi Id | MGI:5582892 | Doi | 10.1016/j.biocel.2012.11.005 |
| Citation | Zhou S, et al. (2013) Functional interaction of glutathione S-transferase pi and peroxiredoxin 6 in intact cells. Int J Biochem Cell Biol 45(2):401-7 |
| abstractText | Peroxiredoxin 6 (Prdx6) is a 1-Cys member of the peroxiredoxin superfamily that plays an important role in antioxidant defense. Glutathionylation of recombinant Prdx6 mediated by pi glutathione S-transferase (GST) is required for reduction of the oxidized Cys and completion of the peroxidatic catalytic cycle in vitro. This study investigated the requirement for piGST in intact cells. Transfection with a plasmid construct expressing piGST into MCF7, a cell line that lacks endogenous piGST, significantly increased phospholipid peroxidase activity as measured in cell lysates and protected intact cells against a peroxidative stress. siRNA knockdown indicated that this increased peroxidase activity was Prdx6 dependent. Interaction between piGST and Prdx6, evaluated by the Duolink Proximity Ligation Assay, was minimal under basal conditions but increased dramatically following treatment of cells with the oxidant, tert-butyl hydroperoxide. Interaction was abolished by mutation of C47, the active site for Prdx6 peroxidase activity. Depletion of cellular GSH by treatment of cells with buthionine sulfoximine had no effect on the interaction of Prdx6 and piGST. These data are consistent with the hypothesis that oxidation of the catalytic cysteine in Prdx6 is required for its interaction with piGST and that the interaction plays an important role in regenerating the peroxidase activity of Prdx6. |
