Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Nitric oxide modulates mitochondrial activity and apoptosis through protein S-nitrosylation for preimplantation embryo development

“…Janssen-Heininger et al suggested that SOD (the TBAP mimic Mn-SOD) supplementation would decrease superoxide and peroxynitrite, prolong the local action of NO, and consequently, increase protein S-nitrosylation [19]. The increase of S-nitrosylated proteins by TBAP in this study was associated with decreasing mitochondrial activity instead of increasing apoptosis.…”

“…The increase of S-nitrosylated proteins by TBAP in this study was associated with decreasing mitochondrial activity instead of increasing apoptosis. The concentrations of S-nitrothiols (S-nitrosylated Cys residues) and H 2 O 2 are kept under tight control to ensure that NO-and H 2 O 2− induced signaling events occur in spatially and temporally controlled settings [19]. The moderate increase of S-nitrosylation by TBAP might lead to reduced mitochondrial activity and a decreased rate of blastocyst formation; however, the set of S-nitrosylated proteins under such condition did not lead to apoptosis.…”

Immunometabolism: Is it under the eye of the clock?

“…Disruption of the clock leads to a loss of rhythmic transcription and expression of Nrf2 mRNA and protein, reduced levels of glutathione and increased oxidative damage to the lungs by pulmonary fibrosis [87]. ROS, such as superoxide and hydrogen peroxide are products of metabolism that increase during pathological conditions and are capable of inducing inflammation, either via non-specific damage of proteins or lipids, or by acting as signaling molecules [88,89]. ROS production can depend on NADPH oxidases or enzymes with oxidase activity [90], however, it can also be generated via mitochondrial oxidative-phosphorylation, either basally or due to metabolic dysfunction [91].…”

Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

“…There is mounting evidence that biologically relevant reactive oxygen species/reactive nitrogen species, particularly hydrogen peroxide (H 2 O 2 ) and nitric oxide (NO), affect cellular behavior in part through reversible modifications of cysteine residues in proteins. Specifically, H 2 O 2 can react with a cysteine thiol to form a sulfenic acid (SOH), 2 whereas NO promotes the conversion of a thiol to a nitrosothiol (SNO), a process known as S-nitrosylation (or S-nitrosation) (5)(6)(7)(8). Formation of SOH or SNO can in turn give rise to other thiol modifications, including S-glutathionylation or intra/intermolecular disulfide formation.…”