2018
DOI: 10.18632/aging.101450
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Abstract: Non-enzymatic protein modifications occur inevitably in all living systems. Products of such modifications accumulate during aging of cells and organisms and may contribute to their age-related functional deterioration. This review presents the formation of irreversible protein modifications such as carbonylation, nitration and chlorination, modifications by 4-hydroxynonenal, removal of modified proteins and accumulation of these protein modifications during aging of humans and model organisms, and their enhan… Show more

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Cited by 49 publications
(43 citation statements)
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References 258 publications
(43 reference statements)
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“…Levels of nitrites and carbonyl groups, as indicators of nitrosative damage and a protein marker of oxidative stress, respectively, were similar when comparing EGCG-treated and non-treated P23H groups. EGCG reduced levels of both biomarkers in control animals, which were reported to increase with age, probably by modulation of nitric oxide synthase enzymes (NOS) and its free radical scavenger activity [82][83][84][85][86]. EGCG was shown to protect the GSH/glutathione peroxidase system [87], increasing or maintaining the ratio GSH/GSSG, and thereby improving the oxidative status of treated rats [26].…”
Section: Discussionmentioning
confidence: 99%
“…Levels of nitrites and carbonyl groups, as indicators of nitrosative damage and a protein marker of oxidative stress, respectively, were similar when comparing EGCG-treated and non-treated P23H groups. EGCG reduced levels of both biomarkers in control animals, which were reported to increase with age, probably by modulation of nitric oxide synthase enzymes (NOS) and its free radical scavenger activity [82][83][84][85][86]. EGCG was shown to protect the GSH/glutathione peroxidase system [87], increasing or maintaining the ratio GSH/GSSG, and thereby improving the oxidative status of treated rats [26].…”
Section: Discussionmentioning
confidence: 99%
“…MPO also oxidizes tyrosine to tyrosyl radical [ 154 ]. MPO mediates protein nitrosylation, forming 3-chlorotyrosine (3-Cl-Tyr) and dityrosine crosslinks [ 155 , 156 ] ( Table 2 ).…”
Section: Oxidative Stressmentioning
confidence: 99%
“…Oxidative stress due to free radicals gener-ate which attack phospholipid polyunsaturated fatty acids in cellular membrane can lead to lipid peroxidation, thereby results in formation of major end products 4-hydroxyl-2-nonenal (HNE), acrolein, and malondialdehyde, causing neurotoxicity to neurons [39]. HNE reacts with proteins forming stable covalent adducts to lysine, cysteine, and histidine residues, thereby producing carbonyl functionalities to the proteins, leading to oxidative damage called protein oxidation, and these protein carbonyls are mostly abundant in frontal, temporal, occipital, hippocampus, and inferior parietal lobe [40,41]. RNS-like peroxynitrite causes tyrosine nitration of protein (3-nitrotyrosine and di tyrosine).…”
Section: Oxidative Stress and Tau Hyperphosphorylationmentioning
confidence: 99%