Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration

Baldus, Stephan; Eiserich, Jason P.; Mani, Ali R.; Castro, Laura; Figueroa, Mario; Chumley, Phillip; Ma, Wenxin; Tousson, Albert; White, C. Roger; Bullard, Daniel C.; Brennan, Marie–Luise; Lusis, Aldons J.; Moore, Kevin; Freeman, Bruce Α.

doi:10.1172/jci200112617

Cited by 280 publications

(105 citation statements)

References 74 publications

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“…UFH and LMWH were found to inhibit MPO binding and protein nitrotyrosine formation (a hallmark of vascular inflammation) in both endothelial cells and rat aortic tissues. 12 Both heparins were also evidenced to cause a dose-dependent inhibition of MPO capture (as much as 10 times) by arterial and venous endothelial cells. 13 Recent interesting works showed that prophylactic UFH administration inhibited tissue MPO activity and improved pathological changes in animal models of pancreatitis, acute lung injury associated with sepsis and lipopolysaccharide exposition, and in ischemia/reperfusion injury of the lungs and heart.…”

Section: Discussionmentioning

confidence: 95%

Effects of enoxaparin on myeloperoxidase release during hemodialysis

Gozdzikiewicz

Borawski

Koc-Żórawska

et al. 2014

Hemodialysis International

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Myeloperoxidase (MPO) is a proteolytic and prooxidant enzyme largely assembled with the vascular wall, and a heparin-binding protein. We studied if low-molecular-weight heparin enoxaparin administered for hemodialysis (HD) anticoagulation causes systemic MPO activation. Plasma MPO levels were measured in patients undergoing maintenance HD with an intravenous bolus of enoxaparin. Patients were retested during HD employing dialyzers with heparin-grafted polyacrylonitrile membrane and no systemic enoxaparin administration. During enoxaparin-anticoagulated HD plasma MPO levels strikingly increased in all patients (8.6-fold at 10 minutes and 3.3-fold at 120 minutes, both P < 0.0001). The increments were directly associated with the enoxaparin dosage and strongly inversely with the predialysis levels of the enzyme. The increase in plasma MPO during systemic heparin-free HD was significantly less pronounced. Enoxaparin administered for HD anticoagulation induces a marked and dose-dependent increase in plasma MPO as a plausibly favorable result of the liberation of the enzyme from the vascular wall.

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Section: Discussionmentioning

confidence: 95%

Effects of enoxaparin on myeloperoxidase release during hemodialysis

Gozdzikiewicz

Borawski

Koc-Żórawska

et al. 2014

Hemodialysis International

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“…Interestingly both unfractionated heparin and its low-molecular weight derivative, enoxaparin, in standard endothelial cells and in rat aortic tissues significantly inhibit MPO binding and protein nitrotyrosine formation. Baldus et al, therefore suggest that “Endothelial transcytosis of MPO confers specificity to vascular ECM proteins as targets of tyrosine nitration” [126]. Another important research topic regarding the endothelium barrier is the study of interchange among migrating leukocytes, ECM components and NPs during inflammation.…”

Section: Extracellular Matrixmentioning

confidence: 99%

Mechanistic understanding of nanoparticles’ interactions with extracellular matrix: the cell and immune system

et al. 2017

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Extracellular matrix (ECM) is an extraordinarily complex and unique meshwork composed of structural proteins and glycosaminoglycans. The ECM provides essential physical scaffolding for the cellular constituents, as well as contributes to crucial biochemical signaling. Importantly, ECM is an indispensable part of all biological barriers and substantially modulates the interchange of the nanotechnology products through these barriers. The interactions of the ECM with nanoparticles (NPs) depend on the morphological characteristics of intercellular matrix and on the physical characteristics of the NPs and may be either deleterious or beneficial. Importantly, an altered expression of ECM molecules ultimately affects all biological processes including inflammation. This review critically discusses the specific behavior of NPs that are within the ECM domain, and passing through the biological barriers. Furthermore, regenerative and toxicological aspects of nanomaterials are debated in terms of the immune cells-NPs interactions.

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“…Together with other enzymes and bactericidal proteins MPO deactivates, kills and destroys foreign microorganisms [1]. This strongly cationic protein is known to bind to the negatively charged endothelial membrane, whereby this binding is favoured by the presence of heparin/heparancontaining glycosaminoglycans [2,3] and an interaction of MPO with albumin [4].…”

Section: Introductionmentioning

confidence: 99%

Interaction of hypohalous acids and heme peroxidases with unsaturated phosphatidylcholines

2005

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The formation of chlorohydrins, bromohydrins, and iodohydrins from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) by the myeloperoxidase-hydrogen peroxide-halide system was evaluated by means of matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry. This approach allows to detect different kinds of the halogenation reaction even in one mass spectrum. Using a mixture of Cl-, Br-, I-, and SCN- at physiological concentrations, a bromination of POPC dominates by the MPO-hydrogen peroxide-halide system. Hypothiocyanite does apparently not react with the double bond of POPC, but increasing amounts of SCN- cause a decrease of the bromohydrin peaks. An interconversion between different hypohalous acids produced by the myeloperoxidase-hydrogen peroxide-halide system determines the pattern of halogenohydrins in POPC. Especially, hypochlorous acid is able to oxidise Br- to hypobromous acid.

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Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration

Cited by 280 publications

References 74 publications

Effects of enoxaparin on myeloperoxidase release during hemodialysis

Effects of enoxaparin on myeloperoxidase release during hemodialysis

Mechanistic understanding of nanoparticles’ interactions with extracellular matrix: the cell and immune system

Interaction of hypohalous acids and heme peroxidases with unsaturated phosphatidylcholines

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