The DOI matches its Crossref record; 127 of the 127 references it cites were found in a registry or an index.
Molecular mechanisms underlying the activation of eNOS
Abstract
Endothelial cells situated at the interface between blood and the vessel wall play a crucial role in controlling vascular tone and homeostasis, particularly in determining the expression of pro- and anti-atherosclerotic genes. Many of these effects are mediated by changes in the generation and release of the vasodilator nitric oxide (NO) in response to hemodynamic stimuli exerted on the luminal surface of endothelial cells by the streaming blood (shear stress) and the cyclic strain of the vascular wall. The endothelial NO synthase (eNOS) is activated in response to fluid shear stress and numerous agonists via cellular events such as; increased intracellular Ca(2+), interaction with substrate and co-factors, as well as adaptor and regulatory proteins, protein phosphorylation, and through shuttling between distinct sub-cellular domains. Dysregulation of these processes leads to attenuated eNOS activity and reduced NO output which is a characteristic feature of numerous patho-physiological disorders such as diabetes and atherosclerosis. This review summarizes some of the recent findings relating to the molecular events regulating eNOS activity.
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“eNOS is constitutively expressed; a number of posttranslational modifications impact the ability of eNOS to produce NO, from changes in the NO production rates to, in some cases, the complete blockade of NO synthesis”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [296]
In the citing paper
“This kinase is activated in endothelial cells by several stimuli including angiotensin II, oxidative stress, and insulin”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [296]
Citations
Cites
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Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
Palmer, R. M. J., Ferrige, A. G., & Moncada, S. (1987) · Nature · doi:10.1038/327524a0 · Cited by 10,704 · cited 1×
“Thereafter, followed the demonstration of nitric oxide (NO) production by the endothelium and the physiological effectiveness of L-arginine analogs [86] and eventually the isolation of the first NO-generating enzyme or NO synthase (NOS) [13].”
BackgroundMassagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
Self-citationIsolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
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Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
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Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure
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A mechanosensory complex that mediates the endothelial cell response to fluid shear stress
Tzima, E., Irani-Tehrani, M., Kiosses, W. B., Dejana, E., Schultz, D., Engelhardt, B., Cao, G., DeLisser, H. M., & Schwartz, M. A. (2005) · Nature · doi:10.1038/nature03952 · Cited by 1,738
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Research works printed but not linked: 2
- Fleming I, Fisslthaler B, Dimmeler S, Kemp BE, Busse R (2001) Phosphorylation of Thr495 regulates Ca2+/calmodulin-dependent endothelial nitric oxide synthase activity. Circ Res 88:e68–e75
- Kou R, Prabhakar P, Michel T (2001) Phosphorylation of the endothelial isoform of nitric oxide synthase at serine 116: identification of a novel path for eNOS regulation by lysophosphatidic acid. Circulation 104:509
Cited by
Sorted by citations
Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409
Roles of vascular oxidative stress and nitric oxide in the pathogenesis of atherosclerosis
Förstermann, U., Xia, N., & Li, H. (2017) · Circulation Research · doi:10.1161/circresaha.116.309326 · Cited by 1,519
Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280
Coletta, C., Papapetropoulos, A., Erdelyi, K., Olah, G., Módis, K., Panopoulos, P., Asimakopoulou, A., Gerö, D., Sharina, I., Martin, E., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202916109 · Cited by 677
Nitric Oxide and Endothelial Dysfunction
Cyr, A. R., Huckaby, L. V., Shiva, S. S., & Zuckerbraun, B. S. (2020) · Critical Care Clinics · doi:10.1016/j.ccc.2019.12.009 · Cited by 712
Metadata
- Authors
- Fleming, I.
- Affiliations
- Goethe University Frankfurt (DE)
- Corresponding author
- Fleming, Ingrid
- ORCID
- Fleming, Ingrid
- Venue
- Pflügers Archiv - European Journal of Physiology
- Published
- 2009-12-13
- Volume
- 459
- Issue
- 6
- Pages
- 793-806
- ISSN
- 0031-6768 (ISSN-L)
- 1432-2013
- OpenAlex
- W2000165700
- Cited by
- 437
- References
- 125
- Citations by year
- 2026: 8 · 2025: 17 · 2024: 22 · 2023: 20 · 2022: 20 · 2021: 27 · 2020: 33 · 2019: 32 · 2018: 29 · 2017: 31 · 2016: 32 · 2015: 32 · 2014: 35 · 2013: 23 · 2012: 44
- FWCI
- 2.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Pflügers Archiv - European Journal of Physiology (publishedVersion)
- PubMed (publishedVersion)
- 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, eNOS activation, nitric oxide, endothelial cells, fluid shear stress, cyclic strain, intracellular calcium, protein phosphorylation, adaptor proteins, atherosclerosis, diabetes mellitus, vascular tone, hemodynamics
- MeSH terms
- Soluble Guanylyl Cyclase, Amino Acid Sequence, Biopterins, Calmodulin, Enzyme Activation, Guanylate Cyclase, Humans, Nitric Oxide, Phosphorylation, Protein Kinases, Signal Transduction, Receptors, Cytoplasmic and Nuclear, HSP90 Heat-Shock Proteins, Platelet Endothelial Cell Adhesion Molecule-1, Dynamins, Adaptor Proteins, Signal Transducing, Caveolin 1, Nitric Oxide Synthase Type III, Protein Tyrosine Phosphatase, Non-Receptor Type 11
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