We are analyzing https://link.springer.com/article/10.1007/s003900050270.

Title:
Neutrophil myeloperoxidase revisited: it's role in health and disease | Intensivmedizin und Notfallmedizin
Description:
Human myeloperoxidase (MPO; EC 1.11.1.7) is a specific heme (Fe3+) peroxidase, present in high concentrations in the azurophilic granules of neutrophils. Its amino acid and genomic sequences have been elucidated, and recombinant MPO is produced from genetically engineered mammalian cells. This peroxidase has the unique activity of chlorination, generating hypochlorous acid (HOCl) from hydrogen peroxide and chloride anion, but also chlorine and monoatomic chlorine. By interacting with other enzymes of neutrophils and reacting with the products of neutrophil activation, MPO also produces other reactive oxygen species (singlet oxygen, hydroxyl radical, nitrosyl and nitryl chloride, etc.). In phagolysosomes, MPO acts together with NADPH oxidase and proteases for the destruction of the ingested organisms, by binding to the microorganism walls and producing locally HOCl, which is particularly active against the polysaccharidic capsules. MPO activity influences the transduction of the cellular signal (activation of NF-κB, chlorination of tyrosyl residues on essential enzymes, etc.) and modulates the functions of cells: it decreases the killer activity of NT lymphocytes and, after internalization, it enhances the microbial activity of macrophages. MPO is taken up by endothelial cells. MPO deficiency is the most common neutrophilic lysosomal enzyme deficiency, but usually without apparent increased susceptibility to infection or altered inflammatory response. MPO has been recognized to be responsible for the oxidation and chlorination of low density lipoproteins, contributing to the early stage of atherosclerosis. In disease with excessive and uncontrolled inflammatory reaction, MPO can be released in the extracellular milieu where it becomes cytotoxic for neighboring cells (oxidant stress) and oxidizes tissues and proteins (thiol oxidation, oxidation and chlorination of lipids and amino acids, etc.). Out of the neutrophil, the activity of MPO would be quickly inhibited by proteins; however, active MPO has been measured in broncho-alveolar lavage fluids from patients with acute lung injury. This specific enzyme, thus, presents a double role of essential host protection when acting into the phagocytes and of host damage when released in the extracellular milieu.
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Keywords {🔍}

mpo, chlorination, article, myeloperoxidase, privacy, cookies, activity, oxidation, information, publish, search, neutrophil, disease, hocl, milieu, cells, essential, content, data, journal, research, role, download, debydupont, deby, lamy, peroxidase, neutrophils, enzymes, products, oxygen, discover, optional, personal, parties, protection, policy, find, track, intensivmedizin, notfallmedizin, revisited, health, cite, pdf, explore, spezifische, neutrophilen, chlor, produziert,

Topics {✒️}

neutrophil myeloperoxidase revisited broncho-alveolar lavage fluids aktivierung von nf-κb nadph oxidase nitrosyl und nitrylchlorid… indem es sich privacy choices/manage cookies mpo activity influences phagozyten wirksam ist producing locally hocl search search article deby-dupont mpo deficiency european economic area reactive oxygen species apparent increased susceptibility altered inflammatory response low density lipoproteins uncontrolled inflammatory reaction acute lung injury related subjects conditions privacy policy generating hypochlorous acid accepting optional cookies recombinant mpo mpo acts extracellular milieu wenn es nt lymphocytes essential enzymes essential host protection journal finder publish neutrophil activation active mpo article cite thiol oxidation phagocytes nf-κb neutrophil mpo privacy policy personal data das hydroxylradikal specific enzyme books a data protection optional cookies manage preferences enzymes singlet oxygen

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Neutrophil myeloperoxidase revisited: it's role in health and disease
         description: Human myeloperoxidase (MPO; EC 1.11.1.7) is a specific heme (Fe3+) peroxidase, present in high concentrations in the azurophilic granules of neutrophils. Its amino acid and genomic sequences have been elucidated, and recombinant MPO is produced from genetically engineered mammalian cells. This peroxidase has the unique activity of chlorination, generating hypochlorous acid (HOCl) from hydrogen peroxide and chloride anion, but also chlorine and monoatomic chlorine. By interacting with other enzymes of neutrophils and reacting with the products of neutrophil activation, MPO also produces other reactive oxygen species (singlet oxygen, hydroxyl radical, nitrosyl and nitryl chloride, etc.). In phagolysosomes, MPO acts together with NADPH oxidase and proteases for the destruction of the ingested organisms, by binding to the microorganism walls and producing locally HOCl, which is particularly active against the polysaccharidic capsules. MPO activity influences the transduction of the cellular signal (activation of NF-κB, chlorination of tyrosyl residues on essential enzymes, etc.) and modulates the functions of cells: it decreases the killer activity of NT lymphocytes and, after internalization, it enhances the microbial activity of macrophages. MPO is taken up by endothelial cells. MPO deficiency is the most common neutrophilic lysosomal enzyme deficiency, but usually without apparent increased susceptibility to infection or altered inflammatory response. MPO has been recognized to be responsible for the oxidation and chlorination of low density lipoproteins, contributing to the early stage of atherosclerosis. In disease with excessive and uncontrolled inflammatory reaction, MPO can be released in the extracellular milieu where it becomes cytotoxic for neighboring cells (oxidant stress) and oxidizes tissues and proteins (thiol oxidation, oxidation and chlorination of lipids and amino acids, etc.). Out of the neutrophil, the activity of MPO would be quickly inhibited by proteins; however, active MPO has been measured in broncho-alveolar lavage fluids from patients with acute lung injury. This specific enzyme, thus, presents a double role of essential host protection when acting into the phagocytes and of host damage when released in the extracellular milieu.
         datePublished:
         dateModified:
         pageStart:500
         pageEnd:513
         sameAs:https://doi.org/10.1007/s003900050270
         keywords:
            Schlüsselwörter Myeloperoxidase
            Oxidation
            Entzündung
            Key words Myeloperoxidase
            Inflammation
            Internal Medicine
            Intensive / Critical Care Medicine
            Emergency Medicine
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         author:
               name:G. Deby-Dupont
               affiliation:
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                     address:
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ScholarlyArticle:
      headline:Neutrophil myeloperoxidase revisited: it's role in health and disease
      description: Human myeloperoxidase (MPO; EC 1.11.1.7) is a specific heme (Fe3+) peroxidase, present in high concentrations in the azurophilic granules of neutrophils. Its amino acid and genomic sequences have been elucidated, and recombinant MPO is produced from genetically engineered mammalian cells. This peroxidase has the unique activity of chlorination, generating hypochlorous acid (HOCl) from hydrogen peroxide and chloride anion, but also chlorine and monoatomic chlorine. By interacting with other enzymes of neutrophils and reacting with the products of neutrophil activation, MPO also produces other reactive oxygen species (singlet oxygen, hydroxyl radical, nitrosyl and nitryl chloride, etc.). In phagolysosomes, MPO acts together with NADPH oxidase and proteases for the destruction of the ingested organisms, by binding to the microorganism walls and producing locally HOCl, which is particularly active against the polysaccharidic capsules. MPO activity influences the transduction of the cellular signal (activation of NF-κB, chlorination of tyrosyl residues on essential enzymes, etc.) and modulates the functions of cells: it decreases the killer activity of NT lymphocytes and, after internalization, it enhances the microbial activity of macrophages. MPO is taken up by endothelial cells. MPO deficiency is the most common neutrophilic lysosomal enzyme deficiency, but usually without apparent increased susceptibility to infection or altered inflammatory response. MPO has been recognized to be responsible for the oxidation and chlorination of low density lipoproteins, contributing to the early stage of atherosclerosis. In disease with excessive and uncontrolled inflammatory reaction, MPO can be released in the extracellular milieu where it becomes cytotoxic for neighboring cells (oxidant stress) and oxidizes tissues and proteins (thiol oxidation, oxidation and chlorination of lipids and amino acids, etc.). Out of the neutrophil, the activity of MPO would be quickly inhibited by proteins; however, active MPO has been measured in broncho-alveolar lavage fluids from patients with acute lung injury. This specific enzyme, thus, presents a double role of essential host protection when acting into the phagocytes and of host damage when released in the extracellular milieu.
      datePublished:
      dateModified:
      pageStart:500
      pageEnd:513
      sameAs:https://doi.org/10.1007/s003900050270
      keywords:
         Schlüsselwörter Myeloperoxidase
         Oxidation
         Entzündung
         Key words Myeloperoxidase
         Inflammation
         Internal Medicine
         Intensive / Critical Care Medicine
         Emergency Medicine
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      isPartOf:
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         issn:
            0175-3851
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         type:
            Periodical
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         name:Steinkopff Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
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      author:
            name:G. Deby-Dupont
            affiliation:
                  name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected]
                  address:
                     name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
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                     name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
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                     name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
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      name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected]
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         name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
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      affiliation:
            name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected]
            address:
               name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
               type:PostalAddress
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      affiliation:
            name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected]
            address:
               name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
               type:PostalAddress
            type:Organization
      name:M. Lamy
      affiliation:
            name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected]
            address:
               name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
               type:PostalAddress
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      name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX
      name:Centre for the Biochemistry of Oxygen Institut de Chimie, B6a Domaine Universitaire du Sart Tilman B-4000 Liège e-mail: [email protected], , XX

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