Oxidative Stress in Aging: Advances in Proteomic Approaches

Table 1

Major posttranslational protein oxidative modifications during oxidative stress mediated aging.

Type of modification	Consists of
Irreversible
Carbonylation	Covalent adduction of lipid aldehydes, often six, nine, or 12 carbons, to the side chains of lysine, histidine, and cysteine residues
3-Nitrotyrosilation	Formed between reactive nitrogen species and a protein’s tyrosine residue
Reversible
S-Sulfenation	Generation of sulfur-hydroxylation product (P-SOH) may be a prelude to sulfination, sulfonation, disulfide bond formation, and sulfenyl-amide bond formation
S-Nitrosylation	Covalent incorporation of a nitric oxide moiety into thiol groups to form S-nitrosothiol (SNO)
S-Glutathionylation	Covalent attachment of glutathione (GSH) to protein thiol groups
Disulfide formation	Disulfide bonds are usually formed from the oxidation of sulfhydryl (–SH) groups
4-Hydroxy-2-nonenal; (HNE) modification	Is a major lipid peroxidation product formed during oxidative stress