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Daphna, Efrati-Machluf; Sharabani, Michaela; Eynat, Peles; Aviram, Irit; Rimon, Sara

doi:10.1023/a:1006848730927

Cited by 69 publications

(19 citation statements)

References 29 publications

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“…In addition to HOCl cross-linking LDL via chloramines, which can subsequently react with lysine or histidine residues (66), a previously unsuspected oxidation pathway via cysteine-lysine interactions was also proposed, with likely relevance in the pathogenesis of atherosclerosis (68). Our evidence strongly supports this possibility, particularly as MPO (69) and S100A9 (Figs. 1D and 2E) bind glycosaminoglycans on EC and the ECM, and S100A8 preferentially forms non-covalent complexes with S100A9 (10), so the close proximity of these proteins may initially reduce oxidative damage.…”

Section: Figure 7 Separation Of Hocl-oxidized Proteinssupporting

confidence: 73%

S100A8 and S100A9 in Human Arterial Wall

McCormick

Rahimi

Bobryshev

et al. 2005

Journal of Biological Chemistry

165

163

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Atherogenesis is a complex process involving inflammation. S100A8 and S100A9, the Ca 2؉ -binding neutrophil cytosolic proteins, are associated with innate immunity and regulate processes leading to leukocyte adhesion and transmigration. In neutrophils and monocytes the S100A8-S100A9 complex regulates phosphorylation, NADPH-oxidase activity, and fatty acid transport. The proteins have anti-microbial properties, and S100A8 may play a role in oxidant defense in inflammation. Murine S100A8 is regulated by inflammatory mediators and recruits macrophages with a proatherogenic phenotype. S100A9 but not S100A8 was found in macrophages in ApoE ؊/؊ murine atherosclerotic lesions, whereas both proteins are expressed in human giant cell arteritis. Here we demonstrate S100A8 and S100A9 protein and mRNA in macrophages, foam cells, and neovessels in human atheroma. Monomeric and complexed forms were detected in plaque extracts. S100A9 was strongly expressed in calcifying areas and the surrounding extracellular matrix. Vascular matrix vesicles contain high levels of Ca 2؉ -binding proteins and phospholipids that regulate calcification. Matrix vesicles characterized by electron microscopy, x-ray microanalysis, nucleoside triphosphate pyrophosphohydrolase assay and cholesterol/phospholipid analysis contained predominantly S100A9. We propose that S100A9 associated with lipid structures in matrix vesicles may influence phospholipid-Ca 2؉ binding properties to promote dystrophic calcification. S100A8 and S100A9 were more sensitive to hypochlorite oxidation than albumin or low density lipoprotein and immunoaffinity confirmed S100A8-S100A9 complexes; some were resistant to reduction, suggesting that hypochlorite may contribute to protein cross-linking. S100A8 and S100A9 in atherosclerotic plaque and calcifying matrix vesicles may significantly influence redox-and Ca 2؉ -dependent processes during atherogenesis and its chronic complications, particularly dystrophic calcification.

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Section: Figure 7 Separation Of Hocl-oxidized Proteinssupporting

confidence: 73%

S100A8 and S100A9 in Human Arterial Wall

McCormick

Rahimi

Bobryshev

et al. 2005

Journal of Biological Chemistry

165

163

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“…(208) The nature of some of these caeruloplasmin-MPO complexes has been investigated. (209) Polyanionic glycosaminoglycans, such as the anticoagulant heparin, bind (cationic) MPO electrostatically, (28) and can liberate MPO sequestered in the artery wall. (210) This interaction with MPO may exacerbate damage to heparin, or other glycosaminoglycans to which it is bound, (84,155) but divert oxidation from other critical sites.…”

Section: Inhibition Of Myeloperoxidase Activitymentioning

confidence: 99%

Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention

Davies

2010

J. Clin. Biochem. Nutr.

361

228

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There is considerable interest in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase and lactoperoxidase, may play in a wide range of human pathologies. This has been sparked by rapid developments in our understanding of the basic biochemistry of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of biomarkers that can be used damage induced by these oxidants in vivo, and the recent identification of a number of compounds that show promise as inhibitors of these enzymes. Such compounds offer the possibility of modulating damage in a number of human pathologies. This reviews recent developments in our understanding of the biochemistry of myeloperoxidase, the oxidants that this enzyme generates, and the use of inhibitors to inhibit such damage.

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“…The main reason for this is the fact that MPO rapidly adsorbs at the surface of LDL and seems to have a strong interaction with the protein moiety of LDL [93, 94]. This adsorption phenomenon is due to the cationic characteristic of MPO, and it has been described on lipoproteins and also on endothelial cells [95]. LDL-MPO bound was first shown by Carr et al who observed a coprecipitation of apoB-100-containing lipoproteins and MPO.…”

Section: Modification Of Ldl Myeloperoxidase and Mox-ldlmentioning

confidence: 99%

Low-Density Lipoprotein Modified by Myeloperoxidase in Inflammatory Pathways and Clinical Studies

Delporte

Antwerpen

Vanhamme

et al. 2013

Mediators of Inflammation

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Oxidation of low-density lipoprotein (LDL) has a key role in atherogenesis. Among the different models of oxidation that have been studied, the one using myeloperoxidase (MPO) is thought to be more physiopathologically relevant. Apolipoprotein B-100 is the unique protein of LDL and is the major target of MPO. Furthermore, MPO rapidly adsorbs at the surface of LDL, promoting oxidation of amino acid residues and formation of oxidized lipoproteins that are commonly named Mox-LDL. The latter is not recognized by the LDL receptor and is accumulated by macrophages. In the context of atherogenesis, Mox-LDL accumulates in macrophages leading to foam cell formation. Furthermore, Mox-LDL seems to have specific effects and triggers inflammation. Indeed, those oxidized lipoproteins activate endothelial cells and monocytes/macrophages and induce proinflammatory molecules such as TNFα and IL-8. Mox-LDL may also inhibit fibrinolysis mediated via endothelial cells and consecutively increase the risk of thrombus formation. Finally, Mox-LDL has been involved in the physiopathology of several diseases linked to atherosclerosis such as kidney failure and consequent hemodialysis therapy, erectile dysfunction, and sleep restriction. All these issues show that the investigations of MPO-dependent LDL oxidation are of importance to better understand the inflammatory context of atherosclerosis.

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Cited by 69 publications

References 29 publications

S100A8 and S100A9 in Human Arterial Wall

S100A8 and S100A9 in Human Arterial Wall

Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention

Low-Density Lipoprotein Modified by Myeloperoxidase in Inflammatory Pathways and Clinical Studies

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