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Factors Determining the Selectivity of Protein Tyrosine Nitration
Open accessAbstract
Tyrosine nitration is a covalent posttranslational protein modification derived from the reaction of proteins with nitrating agents. Protein nitration appears to be a selective process since not all tyrosine residues in proteins or all proteins are nitrated in vivo. To investigate factors that may determine the biological selectivity of protein tyrosine nitration, we developed an in vitro model consisting of three proteins with similar size but different three-dimensional structure and tyrosine content. Exposure of ribonuclease A to putative in vivo nitrating agents revealed preferential nitration of tyrosine residue Y(115). Tyrosine residue Y(23) and to a lesser extent residue Y(20) were preferentially nitrated in lysozyme, whereas tyrosine Y(102) was the only residue modified by nitration in phospholipase A(2). Tyrosine Y(115) was the residue modified by nitration after exposure of ribonuclease A to different nitrating agents: chemically synthesized peroxynitrite, nitric oxide, and superoxide generated by SIN-1 or myeloperoxidase (MPO)/H(2)O(2) plus nitrite (NO(-2)) in the presence of bicarbonate/CO(2). The nature of the nitrating agent determined in part the protein that would be predominantly modified by nitration in a mixture of all three proteins. Ribonuclease A was preferentially nitrated upon exposure to MPO/H(2)O(2)/NO(-2), whereas phospholipase A(2) was the primary target for nitration upon exposure to peroxynitrite. The data also suggest that the exposure of the aromatic ring to the surface of the protein, the location of the tyrosine on a loop structure, and its association with a neighboring negative charge are some of the factors determining the selectivity of tyrosine nitration in proteins.
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“The results of different studies are contradictory, with examples of improved outcomes for NOX1 deficient mice subjected to high fat diet (854) and diabetic mouse models (380), whereas in other cases, NOX1 deletion did not seem to have an effect (875).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [875]
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Metadata
- Authors
- Souza, J. M., Daikhin, E., Yudkoff, M., Raman, C. S., & Ischiropoulos, H.
- Affiliations
- Children's Hospital of Philadelphia (US)
- Corresponding author
- Ischiropoulos, Harry
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 371
- Issue
- 2
- Pages
- 169-178
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2054336997
- Cited by
- 315
- References
- 30
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 8 · 2021: 3 · 2020: 8 · 2019: 8 · 2018: 12 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 14 · 2013: 12 · 2012: 17
- FWCI
- 5.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- University of Pennsylvania
- National Institutes of Health (1r03ag016987-01)
- National Institute on Aging (AG 13966, R01AG013966, AG 16987)
- National Heart, Lung, and Blood Institute (HL54926, R01HL054926)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- tyrosine nitration, nitration selectivity, post-translational modification, peroxynitrite, nitric oxide, superoxide, myeloperoxidase, ribonuclease A, lysozyme, phospholipase A2, tyrosine residues, nitrating agents
- MeSH terms
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Muramidase, Nitrates, Nitric Oxide, Phospholipases A, Protein Processing, Post-Translational, Ribonuclease, Pancreatic, Superoxides, Tyrosine, Protein Structure, Secondary, Sequence Analysis, Protein
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