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Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
The data reveal that NO2− may regulate inflammatory processes through oxidative mechanisms, perhaps by contributing to the tyrosine nitration and chlorination observed in vivo.
Myeloperoxidase Serum Levels Predict Risk in Patients With Acute Coronary Syndromes
Given its proinflammatory properties, MPO may serve as both a marker and mediator of vascular inflammation and further points toward the significance of PMN activation in the pathophysiology of ACS.
Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium
Formation of Reactive Nitrogen Species during Peroxidase-catalyzed Oxidation of Nitrite
- A. van der Vliet, J. Eiserich, B. Halliwell, C. Cross
- Biology, ChemistryThe Journal of Biological Chemistry
- 21 March 1997
The results suggest that NO2−, at physiological or pathological levels, is a substrate for the mammalian peroxidases MPO and lactoperoxidase and that formation of NO2· via per oxidase-catalyzed oxidation ofNO2− may provide an additional pathway contributing to cytotoxicity or host defense associated with increased NO· production.
Concentration-dependent Effects of Nitric Oxide on Mitochondrial Permeability Transition and Cytochrome cRelease*
The mitochondrial permeability transition pore and associated release of cytochrome c are thought to be important in the apoptotic process and it is proposed that this pathway represents an additional mechanism underlying the antiapoptotic effects of NO⋅.
Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase
Myeloperoxidase, an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense reactions, can directly modulate vascular inflammatory responses by regulating NO bioavailability during acute inflammation.
Soluble epoxide hydrolase is a therapeutic target for acute inflammation.
- K. Schmelzer, L. Kubala, J. Newman, In‐Hae Kim, J. Eiserich, B. Hammock
- BiologyProceedings of the National Academy of Sciences…
- 12 July 2005
It is demonstrated that the soluble epoxide hydrolase (sEH) is a key pharmacologic target for treating acute systemic inflammation and has therapeutic efficacy in the treatment and management of acute inflammatory diseases.
Myeloperoxidase mediates neutrophil activation by association with CD11b/CD18 integrins.
- D. Lau, H. Mollnau, S. Baldus
- Biology, MedicineProceedings of the National Academy of Sciences…
- 11 January 2005
Results reveal that binding of MPO to CD11b/CD18 integrins stimulates PMN signaling pathways to induce PMN activation in a mechanism independent of MPo catalytic activity.
Reactive nitrogen species and tyrosine nitration in the respiratory tract: epiphenomena or a pathobiologic mechanism of disease?
- A. van der Vliet, J. Eiserich, M. Shigenaga, C. Cross
- BiologyAmerican journal of respiratory and critical care…
- 1 July 1999
Since its discovery as a biologic messenger molecule just over a decade ago, nitric oxide (NO · ) has become well recognized for its participation in diverse biologic processes in nearly all aspects…
Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration.
It is shown that MPO concentrates in the subendothelial matrix of vascular tissues by a transcytotic mechanism and serves as a catalyst of ECM protein tyrosine nitration, and significantly contributes to NO(2)Tyr formation in vivo.