Cited by 56Nitric Oxide and Endothelin EffectsRedox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

The interplay of nitric oxide and peroxynitrite with signal transduction pathways: Implications for disease

McAndrew, Joanne, Patel, Rakesh P., Jo, Hanjoong, Cornwell, Trudy, Lincoln, Tom, Moellering, Douglas, White, C. Roger, Matalon, Sadis +1 more·1997·Seminars in Perinatology

Abstract

Since the discovery that at least one form of endothelium derived relaxing factor is nitric oxide (NO), numerous studies have uncovered diverse roles for this free radical in a variety of physiological and pathophysiological processes. NO production, a process mediated by a family of enzymes termed NO synthases, has been detected in most cell types. Many of the effects of NO are thought to be mediated through its direct interaction with specific and defined cell signaling pathways. The nature of such interactions are highly dependent on the concentration of NO and cell type. Furthermore, specific NO derived reaction products, such as peroxynitrite, also have the potential to effect cell signal transduction events. As with NO, this can occur through diverse mechanisms and depends on concentration and cell type. It is perhaps not surprising that the reported effects of NO in different disease states are often conflicting. In this brief overview, a framework for placing these apparently disparate properties of NO will be described and will focus on the effects of NO and peroxynitrite on signaling pathways.

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Crossref · 10.1016/s0146-0005(97)80002-x

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  • Once NO has reacted with O2 ̇̄, it forms peroxynitrite and no longer participates in signaling actions that require binding to ferrous heme.

    “Once it has reacted with O2˙̄, it forms peroxynitrite and no longer participates in those signaling actions, which require binding to ferrous heme (23).”
  • The presence of free radicals such as superoxide changes the fate of NO: once reacted, it forms peroxynitrite and can no longer bind to ferrous heme.

    “The presence of free radicals such as superoxide (O2.−) [82-85] changes the fate of NO: once reacted, it forms peroxynitrite [82, 84, 85] and can no longer bind to ferrous heme [86].”

    From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [86]

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Authors
McAndrew, J., Patel, R. P., Jo, H., Cornwell, T., Lincoln, T., Moellering, D., White, C. R., Matalon, S., & Darley-Usmar, V.
Affiliations
University of Alabama at Birmingham (US)
Corresponding author
Darley-Usmar, Victor
Venue
Seminars in Perinatology
Publisher
Elsevier BV
Published
1997-10
Volume
21
Issue
5
Pages
351-366
ISSN
0146-0005 (ISSN-L)
OpenAlex
W2048272805
Cited by
56
References
128
Citations by year
2023: 1 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 1 · 2017: 1 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 2 · 2012: 1
FWCI
0.42
Type
journal article
Language
en
Open access
closed
Locations
  • Seminars in Perinatology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5p01hl048676-05)
  • National Heart, Lung, and Blood Institute (HL48676-04, R01HL051173, HL51173)
Topics
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords
nitric oxide, peroxynitrite, signal transduction, nitric oxide synthase, endothelium-derived relaxing factor, free radicals, signaling pathways, disease
MeSH terms
Animals, Humans, Nitrates, Nitric Oxide, Oxidation-Reduction, Signal Transduction, Oxidants, Nitric Oxide Synthase

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