Protein S -Nitrosylation and Cardioprotection
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Abstract : Nitric oxide (NO) plays an important role in the regulation of cardiovascular function. In addition to the classic NO activation of the cGMP-dependent pathway, NO can also regulate cell function through protein S -nitrosylation, a redox dependent, thiol-based, reversible posttranslational protein modification that involves attachment of an NO moiety to a nucleophilic protein sulfhydryl group. There are emerging data suggesting that S -nitrosylation of proteins plays an important role in cardioprotection. Protein S -nitrosylation not only leads to changes in protein structure and function but also prevents these thiol(s) from further irreversible oxidative/nitrosative modification. A better understanding of the mechanism regulating protein S -nitrosylation and its role in cardioprotection will provide us new therapeutic opportunities and targets for interventions in cardiovascular diseases.
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NOXs are multiprotein enzyme complexes that catalyze the electron transfer to molecular oxygen to form ROS, more commonly superoxide, but also hydrogen peroxide.
“NOXs are multiprotein enzyme complexes that catalyze the electron transfer to molecular oxygen to form ROS, more commonly superoxide, but also hydrogen peroxide (79, 252, 383, 546, 912).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [912]
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References 157 · Cited by 205
- Authors
- Sun, J., & Murphy, E.
- Affiliations
- National Institutes of Health (US)
- Venue
- Circulation Research
- Published
- 2010-02-05
- Volume
- 106
- Issue
- 2
- Pages
- 285-296
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC3137884
- OpenAlex
- W1992254322
- Cited by
- 205
- References
- 157
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 7 · 2023: 5 · 2022: 5 · 2021: 11 · 2020: 7 · 2019: 11 · 2018: 10 · 2017: 12 · 2016: 17 · 2015: 22 · 2014: 14 · 2013: 22 · 2012: 16
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (ZIAHL002065, ZIAHL002066)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Keywords
- S-nitrosylation, nitric oxide, cardioprotection, post-translational modification, thiol modification, redox regulation, cardiovascular disease, S-nitrosothiols
- MeSH terms
- Animals, Calcium, Humans, Models, Biological, Myocardium, Nitric Oxide, Oxidation-Reduction, Protein Processing, Post-Translational, Sulfhydryl Compounds, S-Nitrosothiols
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