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The Dual Role of Myeloperoxidase in Immune Response

The heme protein myeloperoxidase (MPO) is a major constituent of neutrophils. As a key mediator of the innate immune system, neutrophils are rapidly recruited to inflammatory sites, where they recognize, phagocytose, and inactivate foreign microorganisms. In the newly formed phagosomes, MPO is invol...

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Detalles Bibliográficos
Autor principal: Arnhold, Jürgen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7663354/
https://www.ncbi.nlm.nih.gov/pubmed/33137905
http://dx.doi.org/10.3390/ijms21218057
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author Arnhold, Jürgen
author_facet Arnhold, Jürgen
author_sort Arnhold, Jürgen
collection PubMed
description The heme protein myeloperoxidase (MPO) is a major constituent of neutrophils. As a key mediator of the innate immune system, neutrophils are rapidly recruited to inflammatory sites, where they recognize, phagocytose, and inactivate foreign microorganisms. In the newly formed phagosomes, MPO is involved in the creation and maintenance of an alkaline milieu, which is optimal in combatting microbes. Myeloperoxidase is also a key component in neutrophil extracellular traps. These helpful properties are contrasted by the release of MPO and other neutrophil constituents from necrotic cells or as a result of frustrated phagocytosis. Although MPO is inactivated by the plasma protein ceruloplasmin, it can interact with negatively charged components of serum and the extracellular matrix. In cardiovascular diseases and many other disease scenarios, active MPO and MPO-modified targets are present in atherosclerotic lesions and other disease-specific locations. This implies an involvement of neutrophils, MPO, and other neutrophil products in pathogenesis mechanisms. This review critically reflects on the beneficial and harmful functions of MPO against the background of immune response.
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spelling pubmed-76633542020-11-14 The Dual Role of Myeloperoxidase in Immune Response Arnhold, Jürgen Int J Mol Sci Review The heme protein myeloperoxidase (MPO) is a major constituent of neutrophils. As a key mediator of the innate immune system, neutrophils are rapidly recruited to inflammatory sites, where they recognize, phagocytose, and inactivate foreign microorganisms. In the newly formed phagosomes, MPO is involved in the creation and maintenance of an alkaline milieu, which is optimal in combatting microbes. Myeloperoxidase is also a key component in neutrophil extracellular traps. These helpful properties are contrasted by the release of MPO and other neutrophil constituents from necrotic cells or as a result of frustrated phagocytosis. Although MPO is inactivated by the plasma protein ceruloplasmin, it can interact with negatively charged components of serum and the extracellular matrix. In cardiovascular diseases and many other disease scenarios, active MPO and MPO-modified targets are present in atherosclerotic lesions and other disease-specific locations. This implies an involvement of neutrophils, MPO, and other neutrophil products in pathogenesis mechanisms. This review critically reflects on the beneficial and harmful functions of MPO against the background of immune response. MDPI 2020-10-29 /pmc/articles/PMC7663354/ /pubmed/33137905 http://dx.doi.org/10.3390/ijms21218057 Text en © 2020 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Arnhold, Jürgen
The Dual Role of Myeloperoxidase in Immune Response
title The Dual Role of Myeloperoxidase in Immune Response
title_full The Dual Role of Myeloperoxidase in Immune Response
title_fullStr The Dual Role of Myeloperoxidase in Immune Response
title_full_unstemmed The Dual Role of Myeloperoxidase in Immune Response
title_short The Dual Role of Myeloperoxidase in Immune Response
title_sort dual role of myeloperoxidase in immune response
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7663354/
https://www.ncbi.nlm.nih.gov/pubmed/33137905
http://dx.doi.org/10.3390/ijms21218057
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