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Cited by 30Redox biology and oxidative stressNitric Oxide and Endothelin EffectsNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Mitochondria and regulated tyrosine nitration

Koeck, T., Stuehr, D.J., Aulak, K.S.·2005·Biochemical Society Transactions
DOI 10.1042/bst0331399
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Abstract

The conditions of the cellular microenvironment in complex multicellular organisms fluctuate, enforcing permanent adaptation of cells at multiple regulatory levels. Covalent post-translational modifications of proteins provide the short-term response tools for cellular adjustment and growing evidence supports the possibility that protein tyrosine nitration is part of this cellular toolkit and not just a marker for oxidative damage. We have demonstrated that protein tyrosine nitration fulfils the major criteria for signalling and suggest that the normally highly regulated process may lead to disease upon excessive or inappropriate nitration.

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Crossref · 10.1042/bst0331399

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53 of 53 references verified0 citation errors · 0 not checkable

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  • The nitroproteome appears to be quite specific.

    “Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”

    From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [51]

  • Pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism.

    “Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”

    From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [51]

  • Increased nitration of specific tyrosine residues can impact signaling, including in mitochondria depending on O2 tension.

    “Increases in nitration of specific tyrosine residues can impact signaling, for example in mitochondria with dependence on fluctuations in O2 tension [285].”

    From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [285]

  • Peroxynitrite and reactive species derived from it are important in inflammatory responses and can modulate cell signaling, in part by promoting oxidation or nitration of biomolecules.

    “Peroxynitrite and reactive species derived from it (e.g., nitrogen dioxide) are important in inflammatory responses [85] and can modulate cell signaling [87-90], in part by promoting the oxidation or nitration of a broad range of biomolecules [62].”

    From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [89]

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Authors
Koeck, T., Stuehr, D. J., & Aulak, K. S.
Affiliations
Cleveland Clinic (US)
ORCID
Aulak, K.S.
Venue
Biochemical Society Transactions
Publisher
Portland Press Ltd.
Published
2005-10-26
Volume
33
Issue
6
Pages
1399-1403
ISSN
  • 0300-5127 (ISSN-L)
  • 1470-8752
DOI
10.1042/bst0331399
OpenAlex
W1972406007
Cited by
30
References
53
Citations by year
2021: 1 · 2020: 1 · 2016: 4 · 2015: 1 · 2014: 3 · 2012: 2
FWCI
1.51
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical Society Transactions (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Heart, Lung, and Blood Institute (HL076491, P01HL076491)
  • National Cancer Institute (CA53919)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords
tyrosine nitration, mitochondria, post-translational modification, oxidative stress, cellular adaptation, disease
MeSH terms
Animals, Energy Metabolism, Homeostasis, Mitochondria, Nitric Oxide, Nitrogen, Protein Processing, Post-Translational, Tyrosine, Signal Transduction, Oxidative Stress

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