Peroxynitrite-mediated oxidation of plasma fibronectin

Degendorfer, Georg; Chuang, Christine Y.; Kawasaki, Hiroaki; Hammer, Astrid; Malle, Ernst; Yamakura, Fumiyuki; Davies, Michael J.

doi:10.1016/j.freeradbiomed.2016.06.013

Cited by 50 publications

(47 citation statements)

References 88 publications

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“…Similarly, our current study indicated that Mg metal reduced the levels of MDA and 4‐HNE in MSCs. In addition, 3‐NT, a biomarker of oxidative protein damage, reveals peroxynitrite‐mediated protein damage . As expected, Mg metal presented the ability of decreasing the 3‐NT levels in MSCs that treated with or without UV radiation.…”

Section: Discussionsupporting

confidence: 69%

“…In addition, 3-NT, a biomarker of oxidative protein damage, reveals peroxynitrite-mediated protein damage. 46 As expected, Mg metal presented the ability of decreasing the 3-NT levels in MSCs that treated with or without UV radiation. Hence, we identified herein that Mg metal has the capability to reduce the lipid peroxidation and protein tyrosine nitration in MSCs after UV radiation.…”

Section: Discussionsupporting

confidence: 66%

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Effect of magnesium on reducing the UV‐induced oxidative damage in marrow mesenchymal stem cells

Chen

Xiong

Zhao

et al. 2019

J Biomedical Materials Res

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Oxidative stress could cause damage to lipids, proteins and DNA, which is induced by the imbalance between the production of reactive oxygen species (ROS) and the biological system ability to counteract or detoxify their harmful effects. The oxidative stress damage significantly contributes to a number of diseases. Magnesium (Mg) is endowed with a novel function of removing excess ROS by releasing H2 during the degradation. In this study, in order to explore the property of anti‐oxidative damage of Mg metal, rat bone marrow mesenchymal stem cells (MSCs) oxidative damaged by ultraviolet (UV) radiation was employed to co‐culture with Mg metal. The effect of Mg metal on the response of antioxidant enzymes and mitochondria in MSCs was studied. We found that Mg metal could reduce the cellular oxidative stress damage and elevate the activities of antioxidant enzymes to maintain redox homeostasis. In addition, Mg metal could reduce the risk of UV‐induced cell apoptosis by increasing the ratio of Bcl‐2/Bax, elevating the mitochondrial membrane potential and blocking the release of cytochrome c. This finding showed Mg metal might have the potential for treating diseases caused by oxidative stress damage. © 2019 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 107A: 1253–1263, 2019.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionsupporting

confidence: 66%

Effect of magnesium on reducing the UV‐induced oxidative damage in marrow mesenchymal stem cells

Chen

Xiong

Zhao

et al. 2019

J Biomedical Materials Res

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“…Evidence has also been presented for ECM damage by other oxidants associated with both normal metabolism and inflammation, such as peroxynitrous acid, and for the presence of modified ECM species in human atherosclerotic lesions (e.g. [6,7,[9][10][11]72]). However the exact nature, sites and extents of modification induced by MPO and its oxidants (e.g.…”

Section: Discussionmentioning

confidence: 99%

“…Recent studies have shown that the ECM is highly susceptible to oxidative damage due to its high abundance, its low rate of turnover (which can results in accumulation of damage during ageing and disease) and the relatively low levels of extracellular antioxidant, repairs and catabolic systems [5][6][7]. Considerable data has been presented that demonstrates that oxidants generated by activated leukocytes (neutrophils, monocytes, tissue macrophages) can induce structural and functional changes to ECM proteins and proteoglycans (proteins with covalently attached GAGs), with damage evident in multiple tissue samples, including within human atherosclerotic lesions [7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Chlorination and oxidation of the extracellular matrix protein laminin and basement membrane extracts by hypochlorous acid and myeloperoxidase

Nybo

Deiterich

Gamon

et al. 2018

Free Radical Biology and Medicine

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A B S T R A C TBasement membranes are specialized extracellular matrices that underlie arterial wall endothelial cells, with laminin being a key structural and biologically-active component. Hypochlorous acid (HOCl), a potent oxidizing and chlorinating agent, is formed in vivo at sites of inflammation via the enzymatic action of myeloperoxidase (MPO), released by activated leukocytes. Considerable data supports a role for MPO-derived oxidants in cardiovascular disease and particularly atherosclerosis. These effects may be mediated via extracellular matrix damage to which MPO binds. Herein we detect and quantify sites of oxidation and chlorination on isolated laminin-111, and laminin in basement membrane extracts (BME), by use of mass spectrometry. Increased modification was detected with increasing oxidant exposure. Mass mapping indicated selectivity in the sites and extent of damage; Met residues were most heavily modified. Fewer modifications were detected with BME, possibly due to the shielding effects. HOCl oxidised 30 (of 56 total) Met and 7 (of 24) Trp residues, and chlorinated 33 (of 99) Tyr residues; 3 Tyr were dichlorinated. An additional 8 Met and 10 Trp oxidations, 14 chlorinations, and 18 dichlorinations were detected with the MPO/H 2 O 2 /Clsystem when compared to reagent HOCl. Interestingly, chlorination was detected at Tyr 2415 in the integrin-binding region; this may decrease cellular adhesion. Co-localization of MPO-damaged epitopes and laminin was detected in human atherosclerotic lesions. These data indicate that laminin is extensively modified by MPO-derived oxidants, with structural and functional changes. These modifications, and compromised cell-matrix interactions, may promote endothelial cell dysfunction, weaken the structure of atherosclerotic lesions, and enhance lesion rupture.

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“…[4] All 20 amino acids are potential substrates of oxidative damage[5] that could trigger misfolding, and eventually protein aggregation. [6]…”

mentioning

confidence: 99%

Mechanical Deformation Accelerates Protein Ageing

et al. 2017

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A hallmark of tissue ageing is the irreversible oxidative modifications of its constituent proteins. We show that single proteins, kept unfolded and extended by a mechanical force, undergo accelerated ageing in times scales of minutes to days. A protein forced to be continuously unfolded loses completely its ability to contract by folding, becoming a labile polymer. Ageing rates vary among different proteins, but in all cases they lose their mechanical integrity. Random oxidative modification of cryptic side chains exposed by mechanical unfolding can be slowed by the addition of antioxidants such as ascorbic acid, or accelerated by oxidants. By contrast, proteins kept in the folded state and probed over week-long experiments show greatly reduced rates of ageing. We demonstrate a novel assay where protein ageing can be greatly accelerated: the constant unfolding of a protein for hours to days is equivalent to decades of exposure to free radicals under physiological conditions.

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Peroxynitrite-mediated oxidation of plasma fibronectin

Cited by 50 publications

References 88 publications

Effect of magnesium on reducing the UV‐induced oxidative damage in marrow mesenchymal stem cells

Effect of magnesium on reducing the UV‐induced oxidative damage in marrow mesenchymal stem cells

Chlorination and oxidation of the extracellular matrix protein laminin and basement membrane extracts by hypochlorous acid and myeloperoxidase

Mechanical Deformation Accelerates Protein Ageing

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