Post translational modification s-nitrosylation

S-Nitrosylation refers to a covalent attachment of an NO moiety to sulfhydryl residues of proteins. The sulfhydryl

residues belongs to a subset of specific cysteine residues in proteins, the resulting SNO is an S-nitrosoprotein. SNOs

have a short half-life in the cytoplasm because of the host of reducing enzymes, including glutathione (GSH) and

thioredoxin, that denitrosylate proteins. Therefore, SNOs are often stored in membranes, vesicles, the interstitial

space and lipophilic protein folds to protect them from denitrosylation. For example, caspases, which mediate

apoptosis, are stored in the mitochondrial intermembrane space as SNOs.

Similar to phosphorylation, S-Nitrosylation is a reversible precess. The denitrosylation is an enzymatic catalyzing

process that reverses the S-Nitrosylation process. However, S-nitrosylation is not a random event, and only specific

cysteine residues are S-nitrosylated. Under physiologic conditions, protein S>-nitrosylation and SNOs provide

protection preventing further cellular oxidative and nitrosative stress. Aberrant S-Nitrosylation may lead to protein

misfolding, synaptic damage, and apoptosis. Dysfunction of the SNO signaling has been implicated in the

pathogenesis of many diseases, such as Alzheimer’s disease cardiovascular diseases.

Because proteins may contain multiple cysteines and due to the labile nature of SNOs, S-nitrosylated cysteines can

be difficult to detect and distinguish from non-S-nitrosylated amino acids. Creative Proteomics has established a

highly sensitive HPLC-MS/MS pipeline that can analyze S-nitrosylated cysteines in both eukaryotic and prokaryotic

organisms. In addition, we have optimized our protocol, to enable more fast and sensitive site mapping service for S-

nitrosylated cysteines.

Learn more about post translational modification s-nitrosylation athttps://www.creative-

proteomics.com/services/s-nitrosylation.htm