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Inhibition of Myeloperoxidase

2020
Myeloperoxidase participates in innate immune defense mechanism through formation of microbicidal reactive oxidants and diffusible radical species. A unique activity is its ability to use chloride as a cosubstrate with hydrogen peroxide to generate chlorinating oxidants such as hypochlorous acid, a potent antimicrobial agent.
Soubhye, Jalal   +3 more
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Influence of myeloperoxidase-catalyzing reaction on the binding between myeloperoxidase and anti-myeloperoxidase antibodies

Human Immunology, 2012
In the current study, whether myeloperoxidase (MPO)-catalyzing reaction could influence the antigenicity of MPO was investigated. Hypochlorite acid, the main product of the catalytic reaction, could lower the binding between MPO-antineutrophil cytoplasmic antibodies (ANCA) and MPO when the available chlorine was higher than 0.031×10(-3) g/l.
Peng-Cheng, Xu   +4 more
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Myeloperoxidase Deficiency

Hematology/Oncology Clinics of North America, 1988
MPO activity is critical for optimal microbicidal activity of normal PMNs. In the absence of MPO, auxiliary mechanisms protect most MPO-deficient hosts from clinically significant sequelae, except for some persons with diabetes mellitus who suffer severe candidal disease.
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Diagnostic Assays for Myeloperoxidase and Myeloperoxidase Deficiency

2014
Neutrophils (PMN) represent the dominant cell in the acute response to microbial infection and can contribute to some of the tissue damage that accompanies sterile inflammation. Effective antimicrobial activity in neutrophil phagosomes reflects the combined action of soluble agents in plasma with PMN-derived reactive oxygen species and granule proteins,
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Endothelium, Myeloperoxidase, Anti-Myeloperoxidase Interaction in Vasculitis

1993
Antibodies to myeloperoxidase (MPO) are found in the sera of patients with microscopic polyarteritis and idiopathic crescentic glomerulonephritis. Their pathogenicity is unknown. Studies were carried out on the binding of MPO to cultured human umbilical vein endothelial cells and the recognition of endothelium-bound MPO by antibody to MPO.
M, Vargunam   +6 more
openaire   +3 more sources

Circulating Myeloperoxidase and Anti-Myeloperoxidase Antibody in Patients with Vasculitis

Scandinavian Journal of Rheumatology, 1999
To evaluate a role of myeloperoxidase (MPO) and antibody to myeloperoxidase (anti-MPO) in vasculitis, MPO and anti-MPO were determined by enzyme-linked immunosorbent assays in sera from 43 patients with vasculitis, 40 with rheumatoid arthritis, 36 with systemic lupus erythematosus (SLE), 23 with mixed connective tissue disease, 13 with systemic ...
S, Minota   +7 more
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[20] Human myeloperoxidase and hemi-myeloperoxidase

1986
Publisher Summary This chapter describes human myeloperoxidase (MPO) and hemi-MPO. MPO is an enzyme found in the azurophilic granules of mammalian neutrophils and is also identified in human monocytes. Its function is to kill bacteria that have been phagocytosed by these cells.
Patricia C. Andrews, Norman I. Krinsky
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Partial Myeloperoxidase Deficiency

Acta Haematologica, 2009
Neutrophil myeloperoxidase (MPO) activity was analyzed by a semi-quantitative cytochemical method in 268 subjects divided into several groups. 17 subjects with significantly reduced MPO activity were found: 11 of 23 in the preleukemia group, 2/14 AMLs, 1/20 myeloproliferative syndrome, 1/7 carcinoma with bone marrow metastases, 1/33 diabetes mellitus ...
P, Cech, P, Schneider, F, Bachmann
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Role of Myeloperoxidase in Cardiology

Future Cardiology, 2010
Myeloperoxidase (MPO) is an enzyme found in myeloid cells, particularly in neutrophils, and to a lesser extent in monocytes and tissue macrophages. MPO plays an important role in the host defense against bacteria and viruses. Since MPO is also an important enzyme in the inflammatory process, and inflammation is a key component in the development and ...
Baris, Ikitimur, Bilgehan, Karadag
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Compound I of myeloperoxidase

Biochemical and Biophysical Research Communications, 1980
Summary The optical spectrum of the primary peroxide compound of myeloperoxidase (compound I) is reported. The spectrum, obtained in 1 msec after mixing native ferric myeloperoxidase with excess hydrogen peroxide, exhibits a Soret maximum at 425 nm (c = 52 mM−1 cm−1) and an increase in extinction of the ferric peroxidase at wavelengths higher than ...
J E, Harrison   +3 more
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