Markers of protein oxidation: different oxidants give rise to variable yields of bound and released carbonyl products

Headlam, Henrietta A.; Davies, Michael J.

doi:10.1016/j.freeradbiomed.2004.02.017

Cited by 117 publications

(93 citation statements)

References 30 publications

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“…A previous study of patients with vasculitis and patients with autoimmune diseases associated with vasculitis including SLE, also reported a decrease in serum MPO levels in SLE patients compared with controls, although no statistical analysis was performed (46). The increase in protein-bound carbonyls reported here may be an underestimation of the total yield of carbonyls formed, since it is known that protein oxidation yields both protein-bound and low molecular mass released carbonyls (47,48); only the former were quantified here. The ratio of bound to released carbonyls is dependent on the oxidant (48), and so, the total carbonyl yield cannot be extrapolated from previous data, since the oxidants involved in SLE are not known.…”

Section: Discussionmentioning

confidence: 84%

“…The increase in protein-bound carbonyls reported here may be an underestimation of the total yield of carbonyls formed, since it is known that protein oxidation yields both protein-bound and low molecular mass released carbonyls (47,48); only the former were quantified here. The ratio of bound to released carbonyls is dependent on the oxidant (48), and so, the total carbonyl yield cannot be extrapolated from previous data, since the oxidants involved in SLE are not known. The released carbonyls arise from fragmentation reactions of alkoxyl radicals generated on aliphatic side chains on proteins (47,48).…”

Section: Discussionmentioning

confidence: 84%

“…The ratio of bound to released carbonyls is dependent on the oxidant (48), and so, the total carbonyl yield cannot be extrapolated from previous data, since the oxidants involved in SLE are not known. The released carbonyls arise from fragmentation reactions of alkoxyl radicals generated on aliphatic side chains on proteins (47,48). When such reactions occur at the ␤-carbon (the first carbon of the side chain), an ␣-carbon radical is formed.…”

Section: Discussionmentioning

confidence: 99%

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Increased levels of serum protein oxidation and correlation with disease activity in systemic lupus erythematosus

Morgan¹,

Sturgess²,

Davies³

2005

Arthritis & Rheumatism

121

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Objective. To examine protein oxidation in systemic lupus erythematosus (SLE) and to correlate levels of protein oxidation products with disease activity.Methods. Serum was collected from SLE patients and healthy control subjects. Protein-bound carbonyls and the pro-oxidant enzyme myeloperoxidase (MPO) were quantified by enzyme-linked immunosorbent assay. Protein thiols were quantified using 5,5-dithionitrobenzoic acid. Protein-bound amino acids and methionine, tyrosine, and phenylalanine oxidation products were quantified by acid hydrolysis and highperformance liquid chromatography. Disease activity was assessed by the Systemic Lupus Erythematosus Disease Activity Index (SLEDAI). Levels of antidouble-stranded DNA (anti-dsDNA) antibodies were measured by radioimmunoassay.Results. Compared with control subjects, SLE patients exhibited elevated levels of protein carbonyls (0.108 ؎ 0.078 versus 0.064 ؎ 0.028 nmoles/mg of protein; P ‫؍‬ 0.046), decreased levels of protein thiols (3.9 ؎ 1.1 versus 4.9 ؎ 0.7 nmoles/mg of protein; P ‫؍‬ 0.003), decreased levels of protein-bound methionine (P ‫؍‬ 0.0007), and increased levels of protein-bound methionine sulfoxide (P ‫؍‬ 0.0043) and 3-nitrotyrosine (P ‫؍‬ 0.0477). SLE patients with high SLEDAI scores or elevated anti-dsDNA antibody levels exhibited increased oxidation compared with patients with low SLEDAI scores or low antibody levels. Serum MPO levels were decreased in SLE patients (P ‫؍‬ 0.03), suggesting that this enzyme is not responsible for the enhanced protein oxidation.Conclusion. We found elevated levels of multiple markers of protein oxidation in sera from SLE patients compared with controls, and these levels correlated with disease activity. The findings suggest that protein oxidation may play a role in the pathogenesis of chronic organ damage in SLE.

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Section: Discussionmentioning

confidence: 84%

Section: Discussionmentioning

confidence: 84%

Section: Discussionmentioning

confidence: 99%

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Increased levels of serum protein oxidation and correlation with disease activity in systemic lupus erythematosus

Morgan¹,

Sturgess²,

Davies³

2005

Arthritis & Rheumatism

121

View full text Add to dashboard Cite

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“…Chloramines decompose to yield protein carbonyls, a stable biomarker of protein oxidation and CVD risk [28,[40][41][42]. Formation of protein carbonyl was inhibited in a concentration dependent manner with ≥25 µM UCB significantly inhibiting protein oxidation (P<0.05; Figure 6A).…”

Section: Inhibition Of Protein Carbonyl Formation By Mpo Mediated Oximentioning

confidence: 99%

Bilirubin scavenges chloramines and inhibits myeloperoxidase-induced protein/lipid oxidation in physiologically relevant hyperbilirubinemic serum

Boon

Hawkins

Coombes

et al. 2015

Free Radical Biology and Medicine

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Hypochlorous acid (HOCl), an oxidant produced by myeloperoxidase (MPO), induces protein and lipid oxidation, which is implicated in the pathogenesis of atherosclerosis. Individuals with mildly elevated bilirubin concentrations (i.e. Gilbert's syndrome; GS) are protected from atherosclerosis, cardiovascular disease (CVD) and related-mortality. We aimed to investigate Albumin-bound UCB efficiently and specifically (3.9-125 µM; P<0.05) scavenged taurine-, glycine-and N-α-acetyl-lysine-chloramines. These results were translated into Gunn rat and GS serum/plasma which showed significantly (P<0.01) reduced chloramine formation after MPO-induced oxidation. Protein carbonyl and MDA formation were also reduced after MPO oxidation in plasma supplemented with UCB (P<0.05; 25 µM and 50 µM, respectively).Significant inhibition of protein and lipid oxidation was demonstrated within the physiological range of UCB, providing a hypothetical link to protection from atherosclerosis in hyperbilirubinaemic individuals. These data demonstrate a novel and physiologically relevant mechanism whereby UCB could inhibit protein and lipid modification, by quenching chloramines, induced by MPO-induced HOCl.

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“…2C [40,42,49]: the release of the side chain as a carbonyl compound leaves a radical on the a-carbon, which is then prone to backbone cleavage through mechanisms similar to that of the diamide or a-amidation pathways.…”

Section: Protein Backbone Oxidation and Cleavagementioning

confidence: 99%

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Barelli

Canellini

Thadikkaran

et al. 2008

Proteomics Clinical Apps

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Protein oxidation mechanisms result in a wide array of modifications, from backbone cleavage or protein crosslinking to more subtle modifications such as side chain oxidations. Protein oxidation occurs as part of normal regulatory processes, as a defence mechanism against oxidative stress, or as a deleterious processes when antioxidant defences are overcome. Because blood is continually exposed to reactive oxygen and nitrogen species, blood proteomics should inherently adopt redox proteomic strategies. In this review, we recall the biochemical basis of protein oxidation, review the proteomic methodologies applied to analyse redox modifications, and highlight some physiological and in vitro responses to oxidative stress of various blood components.

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Markers of protein oxidation: different oxidants give rise to variable yields of bound and released carbonyl products

Cited by 117 publications

References 30 publications

Increased levels of serum protein oxidation and correlation with disease activity in systemic lupus erythematosus

Increased levels of serum protein oxidation and correlation with disease activity in systemic lupus erythematosus

Bilirubin scavenges chloramines and inhibits myeloperoxidase-induced protein/lipid oxidation in physiologically relevant hyperbilirubinemic serum

Oxidation of proteins: Basic principles and perspectives for blood proteomics

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