Pi Gst Increases Peroxidase Activity Of Prdx6 In Cultured Cells

Prdx6 is a non‐selenium GSH peroxidase that has an important role in ant‐oxidant defense. Previously, we have shown using in vitro assay and by liposome‐mediated delivery of the two proteins into the cells, that the regeneration of Prdx6's peroxidase activity requires πGST. Recently, we have shown that transfection with a plasmid construct expressing πGST into MCF7, a cell line that lacks endogenous πGST, increases the lipid peroxidase activity in the cells, presumably due to activation of endogenous Prdx6. Using the Duolink Proximity Ligation Assay we have shown that there is a dramatic increase in interaction between endogenous πGST and Prdx6 in mouse pulmonary microvascular endothelial cells upon their treatment with tert‐butyl hydroperoxide. Now, we have co‐transfected plasmids expressing πGST and Prdx6 into MCF7 cells. An increase in lipid peroxidase activity was obtained by transfecting Prdx6 and activity is significantly enhanced by co‐transfection with πGST. The functional interaction of Prdx6 with exogenous transfected πGST in MCF7 cells was also revealed by Duolink Proximity Ligation Assay. These cell culture studies are consistent with our previous finding that πGST is involved in regenerating the peroxidase activity of Prdx6.