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Life history of eNOS: Partners and pathways
Open accessAbstract
The complex regulation of eNOS (endothelial nitric oxide synthase) in cardiovascular physiology occurs at multiple stages. eNOS mRNA levels are controlled both at the transcriptional and post-transcriptional phases, and epigenetic mechanisms appear to modulate tissue-specific eNOS expression. The eNOS enzyme reversibly associates with a diverse family of protein partners that regulate eNOS sub-cellular localization, catalytic function, and biological activity. eNOS enzyme activity and sub-cellular localization are intimately controlled by post-translational modifications including phosphorylation, nitrosylation, and acylation. The multiple extra-cellular stimuli affecting eNOS function coordinate their efforts through these key modifications to dynamically control eNOS and NO bioactivity in the vessel wall. This review will focus on the biochemical partners and perturbations of the eNOS protein as this vital enzyme undergoes modulation by diverse signal transduction pathways in the vascular endothelium.
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“NOS3 (commonly called endothelial NOS or eNOS) is expressed to highest relative abundance in the vascular endothelium, but has also been found in neurons, epithelial cells, and cardiomyocytes [66] as well as adipocytes [67, 68] and hepatocytes [69-71].”
From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [66]
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“eNOS (NOS3) generates the lowest levels of NO and was originally discovered in the vascular endothelium but is also found in neurons, epithelial cells, and cardiac myocytes (28).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [28]
In the citing paper
“At the extreme of this spectrum, it is known that for inducible NOS to kill microbes, parasites, or cancer cells, high levels of NO are needed to destroy FeS centers and respiratory proteins in the target organism (28, 31, 32, 46).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [28]
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Metadata
- Authors
- DUDZINSKI, D., & MICHEL, T.
- Affiliations
- Harvard University (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- MICHEL, T
- Venue
- Cardiovascular Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-07-15
- Volume
- 75
- Issue
- 2
- Pages
- 247-260
- ISSN
- 0008-6363 (ISSN-L)
- PMC
- PMC2682334
- OpenAlex
- W2129195977
- Cited by
- 400
- References
- 143
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 9 · 2023: 11 · 2022: 15 · 2021: 13 · 2020: 5 · 2019: 10 · 2018: 19 · 2017: 19 · 2016: 23 · 2015: 17 · 2014: 40 · 2013: 30 · 2012: 42
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cardiovascular Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL046457, P01HL048743)
- National Institute of General Medical Sciences (R01GM036259)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Health and Disease Prevention
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Keywords
- endothelial nitric oxide synthase, nitric oxide, post-translational modification, phosphorylation, nitrosylation, acylation, subcellular localization, epigenetic regulation, transcriptional regulation, post-transcriptional regulation, signal transduction, vascular endothelium, cardiovascular physiology
- MeSH terms
- Acetylation, Animals, Endothelium, Vascular, Humans, Nitric Oxide, Phosphorylation, Protein Processing, Post-Translational, Signal Transduction, Nitrosation, Nitric Oxide Synthase Type III
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