Life history of eNOS: partners and pathways

DUDZINSKI, D; MICHEL, T

doi:10.1016/j.cardiores.2007.03.023

Cited by 400Nitric Oxide and Endothelin EffectsCardiovascular Health and Disease PreventionAngiogenesis and VEGF in Cancer

Life history of eNOS: partners and pathways

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DUDZINSKI, D, MICHEL, T·2007·Cardiovascular Research

DOI 10.1016/j.cardiores.2007.03.023PMC PMC2682334

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Abstract

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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eNOS (NOS3) generates the lowest levels of NO.
“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]
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.
“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]
NOS3 is expressed at highest relative abundance in vascular endothelium, but is also found in neurons, epithelial cells, cardiomyocytes, adipocytes, and hepatocytes.
“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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Functional Relevance of Golgi- and Plasma Membrane-Localized Endothelial NO Synthase in Reconstituted Endothelial Cells
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NOSIP and Its Interacting Protein, eNOS, in the Rat Trachea and Lung
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Erythropoietin Receptors Associate with a Ubiquitin Ligase, p33RUL, and Require Its Activity for Erythropoietin-induced Proliferation
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Statin-Mediated Inhibition of Rho
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FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN
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Dudzinski DM, Michel T. The vascular biology of nitric oxide and nitric oxide synthases. In: Colman RW, George JN, Goldhaber SZ, Marder VJ, Clowes AW, editors. Hemostasis and thrombosis: basic principles and clinical practice. 5th ed. Philadelphia: Lippincott Williams & Wilkins; 2005. p. 653-66.
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Toporsian M, Gros R, Kabir MG, Vera S, Govindaraju K, Eidelman DH, et al. A role for endoglin in coupling eNOS activity and regulating vascular tone revealed in hereditary hemorrhagic telangi- ectasia. Circ Res 2005;96:684-92.

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“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].”
Background
Voluntary wheel running restores endothelial function in conduit arteries of old mice: direct evidence for reduced oxidative stress, increased superoxide dismutase activity and down‐regulation of NADPH oxidase
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Authors: DUDZINSKI, D., & MICHEL, T.
Affiliations: Harvard University (US)
Brigham and Women's Hospital (US)
Corresponding author: MICHEL, T
ORCID: DUDZINSKI, D
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)
DOI: 10.1016/j.cardiores.2007.03.023
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 › 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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