Abstract
The mitochondrial Ca2+-independent phospholipase 2, isoform γ, (iPLA2γ) is directly activated by H2O2. Activation could be achieved by H2O2 reaction with reactive thiol groups. Our computational predictions revealed Cys559 and Cys714, to be the potential targets of human iPLA2γ to oxidative modifications. Purified recombinant iPLA2γ wild type and C559S, C714S, and C559S/C714S mutants were quantified for sulfenic acid modifications. Two methods utilizing BIAM addiction or Click-PEGylation reactions with subsequent Western analysis were used to test the reactivity and accessibility of the protein to redox modifications. Fully oxidized and reduced iPLA2γ forms exhibited different electrophoretic mobilities. Activity assays of recombinant iPLA2γ showed that all three mutants had lower catalytic activity induced by H2O2. Data are consistent with the upregulation of iPLA2γ by redox modification of reactive thiols and suggest S-sulfenylation as the post-translational modification of iPLA2γ.
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