The Dual Role of Myeloperoxidase in Immune Response
Abstract
:1. Immune Response and Tissue Destruction
2. Short Overview about Myeloperoxidase Properties
2.1. Selected Structural Properties
2.2. Heme States and Redox Properties of Myeloperoxidase
2.3. Reaction Cycles of Myeloperoxidase
3. Neutrophils and Myeloperoxidase at Inflammatory Sites
3.1. Recruitment of PMNs to Inflamed Sites
3.2. Important Components of Azurophilic and Specific Granules of Neutrophils
3.3. Conditions of Phagosomal Digestion
3.4. Potential Role of Myeloperoxidase in Phagosomes
3.5. Redundancy in Deactivation and Killing Pathways and MPO Deficiency
3.6. Cell Death of Neutrophils and Formation of Extracellular Traps
3.7. Frustrated Phagocytosis
3.8. Degradation of Ingested Material by Macrophages
4. Involvement of Myeloperoxidase in Disease Progression
4.1. The Fate of Myeloperoxidase at Inflammatory Sites
4.2. Important Binding Sites for Myeloperoxidase
4.3. The Protective Role of Ceruloplasmin
4.4. Myeloperoxidase in Atherosclerotic Plaques
4.5. Myeloperoxidase and Cardiovascular Diseases
4.6. Vasculitis Induced by Antineutrophil Cytoplasmic Antibodies
4.7. Involvement of Myeloperoxidase in Other Disease Scenarios
5. Chronicity of Inflammatory States
5.1. Chronic Inflammatory Processes
5.2. Protection of Surrounding Media Against Damaging Agents
5.3. Immunosuppression
5.4. Sepsis
6. Conclusions
Funding
Conflicts of Interest
References
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Heme State of MPO | Short Denomination | Formal Oxidation State Versus Resting MPO |
---|---|---|
resting MPO | Por−Fe3+ a | |
Compound I | •+Por−Fe4+=O | +2 |
Compound II | Por−Fe4+−OH | +1 |
Compound III | Por−Fe3+−O2•− | 0 |
Redox Couple | E’° (at pH 7) | Number of Transferred Electrons | References |
---|---|---|---|
Compound I/resting MPO | 1.16 V | 2 | [24] |
Compound I/Compound II | 1.35 V | 1 | [25] |
Compound II/resting MPO | 0.97 V | 1 | [25] |
Potentially Damaging Agents | Antagonizing Principle | References |
---|---|---|
Myeloperoxidase | Ceruloplasmin | [182,183] |
Proteases from PMNs, mast cells and others | Anti-proteinases such as α1-antiproteinase, α1-antichymotrypsin, secretory leukocyte protease inhibitor, elafin, α2-macroglobulin | [90] |
Superoxide anion radicals | Superoxide dismutases, cytochrome c, ceruloplasmin | [187,257,258,259] |
Hydrogen peroxide | Glutathione peroxidases, peroxiredoxins, catalase | [260,261,262] |
Free metal ions | Ceruloplasmin, chelators, lactoferrin, ferritin | [88,184,263,264] |
Free hemoglobin, free myoglobin | Haptoglobin | [265] |
Free heme | Hemopexin | [265] |
Lipid-based oxidants | Lipid-soluble antioxidants such as tocopherols, carotenoids, ubiquinol | [266,267] |
Water-based oxidants | Ascorbic acid, urate | [268,269] |
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Arnhold, J. The Dual Role of Myeloperoxidase in Immune Response. Int. J. Mol. Sci. 2020, 21, 8057. https://doi.org/10.3390/ijms21218057
Arnhold J. The Dual Role of Myeloperoxidase in Immune Response. International Journal of Molecular Sciences. 2020; 21(21):8057. https://doi.org/10.3390/ijms21218057
Chicago/Turabian StyleArnhold, Jürgen. 2020. "The Dual Role of Myeloperoxidase in Immune Response" International Journal of Molecular Sciences 21, no. 21: 8057. https://doi.org/10.3390/ijms21218057