Cited by 265Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressAntioxidant Activity and Oxidative Stress

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Eosinophil Peroxidase Nitrates Protein Tyrosyl Residues

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Wu, Weijia, Chen, Yonghong, Hazen, Stanley L.·1999·Journal of Biological Chemistry

DOI 10.1074/jbc.274.36.25933

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Abstract

Eosinophil peroxidase (EPO) has been implicated in promoting oxidative tissue injury in conditions ranging from asthma and other allergic inflammatory disorders to cancer and parasitic/helminthic infections. Studies thus far on this unique peroxidase have primarily focused on its unusual substrate preference for bromide (Br(-)) and the pseudohalide thiocyanate (SCN(-)) forming potent hypohalous acids as cytotoxic oxidants. However, the ability of EPO to generate reactive nitrogen species has not yet been reported. We now demonstrate that EPO readily uses nitrite (NO(2)(-)), a major end-product of nitric oxide ((.)NO) metabolism, as substrate to generate a reactive intermediate that nitrates protein tyrosyl residues in high yield. EPO-catalyzed nitration of tyrosine occurred more readily than bromination at neutral pH, plasma levels of halides, and pathophysiologically relevant concentrations of NO(2)(-). Furthermore, EPO was significantly more effective than MPO at promoting tyrosine nitration in the presence of plasma levels of halides. Whereas recent studies suggest that MPO can also promote protein nitration through indirect oxidation of NO(2)(-) with HOCl, we found no evidence that EPO can indirectly mediate protein nitration by a similar reaction between HOBr and NO(2)(-). EPO-dependent nitration of tyrosine was modulated over a physiologically relevant range of SCN(-) concentrations and was accompanied by formation of tyrosyl radical addition products (e.g. o,o'-dityrosine, pulcherosine, trityrosine). The potential role of specific antioxidants and nucleophilic scavengers on yields of tyrosine nitration and bromination by EPO are examined. Thus, EPO may contribute to nitrotyrosine formation in inflammatory conditions characterized by recruitment and activation of eosinophils.

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A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
Markwell, M. A. K., Haas, S. M., BIEBER, L. L., & Tolbert, N. E. (1978) · Analytical Biochemistry · doi:10.1016/0003-2697(78)90586-9 · Cited by 6,460
Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75212-0 · Cited by 5,556
Trace Elements in Human and Animal Nutrition
UNDERWOOD, E. J. (1963) · Soil Science · doi:10.1097/00010694-196304000-00029 · Cited by 4,511
Eosinophilic Inflammation in Asthma
Bousquet, J., Chanez, P., Lacoste, J. Y., Barneon, G., Ghavanian, N., Enander, I., Venge, P., Ahlstedt, S., Simony-Lafontaine, J., Godard, P., et al. (1990) · New England Journal of Medicine · doi:10.1056/nejm199010113231505 · Cited by 2,499
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496
[23] Oxidative chemistry of peroxynitrite
Beckman, J. S., Chen, J., Ischiropoulos, H., & Crow, J. P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33026-3 · Cited by 973
Enthalpy of decomposition of hydrogen peroxide by catalase at 25° C (with molar extinction coefficients of H2O2 solutions in the UV)
Nelson, D. P., & Kiesow, L. A. (1972) · Analytical Biochemistry · doi:10.1016/0003-2697(72)90451-4 · Cited by 926
Oxygen metabolism and the toxic properties of phagocytes
KLEBANOFF, S. J. (1980) · Annals of Internal Medicine · doi:10.7326/0003-4819-93-3-480 · Cited by 868
3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima.
Hazen, S. L., & Heinecke, J. W. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119379 · Cited by 842
Self-citation
Eosinophilia
Rothenberg, M. E. (1998) · New England Journal of Medicine · doi:10.1056/nejm199805283382206 · Cited by 837

Show all 70 references

Research works printed but not linked: 5

Klebanoff, 1980, Ann. Intern. Med., 93, 480, 10.7326/0003-4819-93-3-480 · DOI · Paper page
Wajon, 1980, 3, 171
Nielsen, 1986, 2, 426
Linder, 1992, Nutritional Biochemistry and Metabolism, 98
Gustafsson, 1998, Eur. Respir. J., 26 (suppl.), 49

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Authors: Wu, W., Chen, Y., & Hazen, S. L.
Affiliations: Cleveland State University (US)
Corresponding author: Hazen, Stanley L.
ORCID: Wu, Weijia
Chen, Yonghong
Hazen, Stanley L.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-09
Volume: 274
Issue: 36
Pages: 25933-25944
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.36.25933
OpenAlex: W2094921988
Cited by: 265
References: 70
Citations by year: 2026: 7 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 6 · 2016: 4 · 2015: 4 · 2014: 6 · 2013: 7 · 2012: 8
FWCI: 7.75
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7707 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL61878, HL 62526, R01HL061878, R01HL062526)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Keywords: eosinophil peroxidase, nitrite, tyrosine nitration, reactive nitrogen species, eosinophils, myeloperoxidase, thiocyanate, bromide, hypohalous acids, nitrotyrosine, oxidative tissue injury, antioxidants, eosinophil activation
MeSH terms: Animals, Eosinophils, Inflammation, Kinetics, Nitric Oxide, Nitrites, Peroxidases, Tyrosine, Oxidative Stress, Eosinophil Peroxidase

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Eosinophil Peroxidase Nitrates Protein Tyrosyl Residues

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