Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation
Open accessAbstract
Initiation of lipid peroxidation and the formation of bioactive eicosanoids are pivotal processes in inflammation and atherosclerosis. Currently, lipoxygenases, cyclooxygenases, and cytochrome P450 monooxygenases are considered the primary enzymatic participants in these events. Myeloperoxidase (MPO), a heme protein secreted by activated leukocytes, generates reactive intermediates that promote lipid peroxidation in vitro. For example, MPO catalyzes oxidation of tyrosine and nitrite to form tyrosyl radical and nitrogen dioxide ((.)NO(2)), respectively, reactive intermediates capable of initiating oxidation of lipids in plasma. Neither the ability of MPO to initiate lipid peroxidation in vivo nor its role in generating bioactive eicosanoids during inflammation has been reported. Using a model of inflammation (peritonitis) with MPO knockout mice (MPO(-/-)), we examined the role for MPO in the formation of bioactive lipid oxidation products and promoting oxidant stress in vivo. Electrospray ionization tandem mass spectrometry was used to simultaneously quantify individual molecular species of hydroxy- and hydroperoxy-eicosatetraenoic acids (H(P)ETEs), F(2)-isoprostanes, hydroxy- and hydroperoxy-octadecadienoic acids (H(P)ODEs), and their precursors, arachidonic acid and linoleic acid. Peritonitis-triggered formation of F(2)-isoprostanes, a marker of oxidant stress in vivo, was reduced by 85% in the MPO(-/-) mice. Similarly, formation of all molecular species of H(P)ETEs and H(P)ODEs monitored were significantly reduced (by at least 50%) in the MPO(-/-) group during inflammation. Parallel analyses of peritoneal lavage proteins for protein dityrosine and nitrotyrosine, molecular markers for oxidative modification by tyrosyl radical and (.)NO(2), respectively, revealed marked reductions in the content of nitrotyrosine, but not dityrosine, in MPO(-/-) samples. Thus, MPO serves as a major enzymatic catalyst of lipid peroxidation at sites of inflammation. Moreover, MPO-dependent formation of (.)NO-derived oxidants, and not tyrosyl radical, appears to serve as a preferred pathway for initiating lipid peroxidation and promoting oxidant stress in vivo.
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Amyloid peptide-mediated oxidative stress, the activation of microglia associated with Aβ peptide deposition, and excessive production of microglial-derived cytokines such as IL-1β and TNF-α support progressive inflammatory episodes in AD.
“Amyloid peptide-mediated oxidative stress, the activation of microglia associated with Aβ peptide deposition, and excessive production of microglial-derived cytokines such as IL-1β and TNF-α support progressive inflammatory episodes in AD (McGeer and McGeer, 2003; Zhang et al., 2002; Kim et al., 2003; Hong et al., 2003).”
From Docosanoids and elovanoids from omega-3 fatty acids are pro-homeostatic modulators of inflammatory responses, cell damage and neuroprotection (2018) · cites this paper as Zhang et al., 2002
Myeloperoxidase in inter-cellular spaces of the brain is a highly effective enzymatic catalyst for the initiation of lipid peroxidation, and brain cells are richly endowed with polyunsaturated fatty acyl phospholipids.
“Myeloperoxidase in inter-cellular spaces of the brain is a highly effective enzymatic catalyst for the initiation of lipid peroxidation (Zhang et al., 2002), and brain cells are richly endowed with a major target of that process, polyunsaturated fatty acyl phospholipids (Bazan, 1990; Bazan and Allan, 1998).”
From Docosanoids and elovanoids from omega-3 fatty acids are pro-homeostatic modulators of inflammatory responses, cell damage and neuroprotection (2018) · cites this paper as Zhang et al., 2002
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- Authors
- Zhang, R., Brennan, M.-L., Shen, Z., MacPherson, J. C., Schmitt, D., Molenda, C. E., & Hazen, S. L.
- Affiliations
- Cleveland Clinic (US)
- Cleveland State University (US)
- Corresponding author
- Hazen, Stanley L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-11
- Volume
- 277
- Issue
- 48
- Pages
- 46116-46122
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2043446682
- Cited by
- 432
- References
- 65
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- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL61878, HL 62526, R01HL061878, HL 70621, R01HL062526, R01HL070621)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- myeloperoxidase, lipid peroxidation, inflammation, oxidative stress, eicosanoids, F2-isoprostanes, tyrosyl radical, nitrite, nitrotyrosine, dityrosine, peritonitis
- MeSH terms
- Catalysis, Lipoxygenase, Peroxidase, Prostaglandin-Endoperoxide Synthases, Lipid Peroxidation, Oxidative Stress
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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