Catalase S-Glutathionylation by NOX2 and Mitochondrial-Derived ROS Adversely Affects Mice and Human Neutrophil Survival

Catalase post-translational modifications as key targets in the control of erythrocyte redox homeostasis in children with obesity and insulin resistance

“…S-glutathionylation has been shown to either increase or decrease the enzyme activity of several proteins. In neutrophils, it has been observed that the induction of ROS production via NOX induces the S-glutathionization of catalase, inhibiting its activity [31], but it differs from what we found in erythrocytes of children with obesity and IR where the decrease in catalase activity matches with a decrease in S-glutathionylation levels. A justification for this could be that protein glutathionylation requires glutathione reductase activity and NADPH to ensure the availability of reduced glutathione (GSH) and, as we previously described, this glutathione recycling pathway is impaired in this group of children with obesity and IR [5], which would potentially limit the control capacity and protection role of this kind of PTM, in erythrocytes.…”

Nutritional deficiencies that may predispose to long COVID

“…Human catalase requires a heme-iron and NADPH (niacinamide/vitamin B 3 derived) cofactors and detoxifies hydrogen peroxide by its conversion to water and oxygen (Goyal and Basak 2010). Glutathionylation of catalase by NOX2 can result in PMN death (Nagarkoti et al 2019).…”