Research Paper Volume 10, Issue 9 pp 2284—2315

Figure 11. Sumoylation-deficient Prdx6K122/142R fused to transduction protein domain (TAT) internalized in cells and blunted oxidative stress-induced aberrant Sumoylation. (A and B) Prdx6^-/- mLECs were transduced with Sumoylation-deficient protein, TAT-HA-Prdx6K122/142R conferred higher resistance to oxidative stress-induced Sumoylation than did Prdx6WT. Prdx6^-/- LECs were pretreated with TAT-HA-Prdx6 WT or TAT-HA-Prdx6K122/142R and then exposed to different concentrations of H₂O₂ (0, 25, 50 and 75µM) and/or UVB (0, 30, 60 and 90J/m²). 48h later, nuclear extracts containing equal amounts of proteins were processed for Sumo1-ELISA assay to assess the relative levels of Sp1 Sumoylation in Prdx6 WT (gray bars) and its mutant Prdx6K122/142R (black bars) transduced in cells as shown. Data represent the mean ± SD from three independent experiments (**p<0.05, *p<0.001). (C) Transduction of TAT-HA-Prdx6 and TAT-HA-Prdx6K122/142R into cells. An aliquot of 10 μg/ml recombinant protein was added to culture media and transduction of TAT-HA-Prdx6 (Lane 3) and TAT-HA-Prdx6K122/142 R (Lane 4) was assessed using WB by anti-Prdx6 antibody. (D) Represents the TAT-HA-Prdx6 and TAT-HA-Prdx6K122/142R following H₂O₂ and/or UVB oxidative exposure treatment schedule.