Human glutathione transferases catalyze the reaction between glutathione and nitrooleic acid.

ABSTRACT: Nitroalkene fatty acids (NO₂-FAs) are formed endogenously. They regulate cell signaling pathways and are being developed clinically to treat inflammatory diseases. NO₂-FAs are electrophilic and form thioether adducts with glutathione (GSH), which are exported from cells. Glutathione transferases (GSTs), a superfamily of enzymes, contribute to the cellular detoxification of hydrophobic electrophiles by catalyzing their conjugation to GSH. Herein, we evaluated the capacity of five human GSTs (M1-1, M2-2, M4-4, A4-4, and P1-1) to catalyze the reaction between nitrooleic acid (NO₂-OA) and GSH. The reaction was monitored by HPLC-ESI-MS/MS, and catalytic activity was detected with hGSTs M1-1 and A4-4. Using stopped-flow spectrophotometry, a 1400- and 7500-fold in

SUBMITTER: Steglich M 

PROVIDER: S-EPMC11999266 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature