eNOS at a glance

Sessa, William C.

doi:10.1242/jcs.01165

Cited by 561Nitric Oxide and Endothelin EffectsAngiogenesis and VEGF in CancerCardiovascular Health and Disease Prevention

eNOS at a glance

Sessa, William C.·2004·Journal of Cell Science

DOI 10.1242/jcs.01165

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Abstract

Endothelium-derived nitric oxide (NO) is a critical regulator of cardiovascular homeostasis. Endothelial nitric oxide synthase (eNOS or NOS3)-derived NO is an endogenous vasodilatory gas that continually regulates the diameter of blood vessels and maintains an anti-proliferative and anti-apoptotic

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eNOS location in the cell and activity are controlled by Ca2+ and calmodulin.
“Its location in the cell and activity are controlled by Ca2+ and calmodulin, as well as post-translational modifications such as phosphorylation and myristoylation (29, 30).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [30]
eNOS location and activity are controlled by post-translational modifications such as phosphorylation and myristoylation.
“Its location in the cell and activity are controlled by Ca2+ and calmodulin, as well as post-translational modifications such as phosphorylation and myristoylation (29, 30).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [30]
NOS3 produces relatively low quantities of NO, and its activity is controlled by calcium/calmodulin, post-translational modifications, and physical forces such as shear stress.
“It produces relatively low quantities of NO, and its activity is controlled by Ca2+ and calmodulin, post-translational modifications [72, 73], and physical forces such as shear stress [74, 75].”
From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [73]

Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
Fulton, D. J., Gratton, J., McCabe, T. J. D., Fontana, J. T., Fujio, Y., Walsh, K., Franke, T. F., Papapetropoulos, A., & Sessa, W. C. (1999) · Nature · doi:10.1038/21218 · Cited by 2,612 · see citing works
Self-citation
The JAK/STAT signaling pathway
Rawlings, J. S., Rosler, K. M., & Harrison, D. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.00963 · Cited by 1,858 · see citing works
Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
Simoncini, T., Hafezi‐Moghadam, A., Brazil, D. P., Ley, K. F., Chin, W. W., & Liao, J. K. (2000) · Nature · doi:10.1038/35035131 · Cited by 1,437 · see citing works
Nitric Oxide Synthases: Properties and Catalytic Mechanism
Griffith, O. W., & Stuehr, D. J. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.003423 · Cited by 1,311 · see citing works
Untitled work
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261 · see citing works
AMP‐activated protein kinase phosphorylation of endothelial NO synthase
Chen, Z.-P., Mitchelhill, K. I., Michell, B. J., Stapleton, D., Rodríguez‐Crespo, I., Witters, L. A., Power, D. A., de Montellano, P. R. O., & Kemp, B. E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01705-0 · Cited by 835 · see citing works
Phosphorylation of Thr <sup>495</sup> Regulates Ca <sup>2+</sup> /Calmodulin-Dependent Endothelial Nitric Oxide Synthase Activity
Fleming, I., Fisslthaler, B., Dimmeler, S., Kemp, B. E., & Busse, R. (2001) · Circulation Research · doi:10.1161/hh1101.092677 · Cited by 770 · cited 1× · see citing works
“…stress triggering the breakdown of ATP will stimulate AMP kinase (AMPK) to phosphorylate eNOS on S1179 (Chen et al., 1999; Dimmeler et al., 1998; Fleming et al., 2001; Fulton et al., 1999; Harris et al., 2001; Haynes et al., 2000; Igarashi and Michel, 2001; Lin et al., 2003; Michell et al.,…”
Background
Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling.
García‐Cardeña, G., Oh, P., Liu, J., Schnitzer, J. E., & Sessa, W. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6448 · Cited by 679 · see citing works
Self-citation
Membrane Estrogen Receptor Engagement Activates Endothelial Nitric Oxide Synthase via the PI3-Kinase–Akt Pathway in Human Endothelial Cells
Haynes, M. P., Sinha, D., Russell, K. S., Collinge, M., Fulton, D. J., Morales‐Ruiz, M., Sessa, W. C., & Bender, J. R. (2000) · Circulation Research · doi:10.1161/01.res.87.8.677 · Cited by 576 · see citing works
Self-citation
Post-Translational Control of Endothelial Nitric Oxide Synthase: Why Isn't Calcium/Calmodulin Enough?
Fulton, D. J., Gratton, J., & Sessa, W. C. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)29198-9 · Cited by 495 · see citing works
Self-citation
Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation
McCabe, T. J., Fulton, D., Roman, L. J., & Sessa, W. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6123 · Cited by 387 · cited 1× · see citing works
“…of T497, S617 and S635 in ACE-1 and S1179 in ACE-II, it is likely that phosphorylation removes the steric hindrance imparted by these non-catalytic inserts and permits better fidelity of electron flux from the reductase domain to NO generation in the oxygenase domain (McCabe et al., 2000).”
BackgroundSelf-citation
Flow-dependent regulation of endothelial nitric oxide synthase: role of protein kinases
Boo, Y. C., & Jo, H. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00122.2003 · Cited by 384 · see citing works
Reciprocal Phosphorylation and Regulation of Endothelial Nitric-oxide Synthase in Response to Bradykinin Stimulation
Harris, M. B., Ju, H., Venema, V. J., Liang, H., Zou, R., Michell, B. J., Chen, Z.-P., Kemp, B. E., & Venema, R. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100229200 · Cited by 363 · see citing works
Sphingosine 1-Phosphate Activates Akt, Nitric Oxide Production, and Chemotaxis through a GiProtein/Phosphoinositide 3-Kinase Pathway in Endothelial Cells
Morales‐Ruiz, M., Lee, M.-J., Zöllner, S. K., Gratton, J., Scotland, R. S., Shiojima, I., Walsh, K., Hla, T., & Sessa, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009993200 · Cited by 276 · see citing works
Self-citation
Cyclic GMP-Dependent Protein Kinases and the Cardiovascular System
Feil, R., Lohmann, S. M., de Jonge, H. R., Walter, U., & Hofmann, F. B. (2003) · Circulation Research · doi:10.1161/01.res.0000100390.68771.cc · Cited by 271 · see citing works
An Autoinhibitory Control Element Defines Calcium-regulated Isoforms of Nitric Oxide Synthase
Salerno, J. C., Harris, D. E., Irizarry, K., Patel, B., Morales, A. J., Smith, S. M., Pavel Martasek, E., Roman, L. J., Masters, B. S. S., Jones, C. L., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29769 · Cited by 248 · see citing works
Phosphorylation of Threonine 497 in Endothelial Nitric-oxide Synthase Coordinates the Coupling of l-Arginine Metabolism to Efficient Nitric Oxide Production
Lin, M. I., Fulton, D. J., Babbitt, R. W., Fleming, I., Busse, R., Pritchard, K. A., & Sessa, W. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302836200 · Cited by 236 · see citing works
Self-citation
Identification of Regulatory Sites of Phosphorylation of the Bovine Endothelial Nitric-oxide Synthase at Serine 617 and Serine 635
Michell, B. J., Harris, M. B., Chen, Z.-P., Ju, H., Venema, V. J., Blackstone, M. A., Huang, W., Venema, R. C., & Kemp, B. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205144200 · Cited by 212 · cited 1× · see citing works
“…AMP kinase (AMPK) to phosphorylate eNOS on S1179 (Chen et al., 1999; Dimmeler et al., 1998; Fleming et al., 2001; Fulton et al., 1999; Harris et al., 2001; Haynes et al., 2000; Igarashi and Michel, 2001; Lin et al., 2003; Michell et al., 2002; Morales-Ruiz et al., 2001; Simoncini et al., 2000).”
Background
The First 35 Amino Acids and Fatty Acylation Sites Determine the Molecular Targeting of Endothelial Nitric Oxide Synthase into the Golgi Region of Cells: A Green Fluorescent Protein Study
Liu, J., Hughes, T. E., & Sessa, W. C. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.7.1525 · Cited by 191 · see citing works
Self-citation
Calcium-dependent membrane association sensitizes soluble guanylyl cyclase to nitric oxide
Zabel, U., Kleinschnitz, C., Oh, P., Nedvetsky, P. I., Smolenski, A., Müller, H., Kronich, P., Kügler, P., Walter, U., Schnitzer, J. E., et al. (2002) · Nature Cell Biology · doi:10.1038/ncb775 · Cited by 151 · see citing works
Sphingosine 1-Phosphate and Isoform-specific Activation of Phosphoinositide 3-Kinase β
Igarashi, J., & Michel, T. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105628200 · Cited by 133 · see citing works
Biosynthesis and Palmitoylation of Endothelial Nitric Oxide Synthase: Mutagenesis of Palmitoylation Sites, Cysteines-15 and/or -26, Argues against Depalmitoylation-Induced Translocation of the Enzyme
Liu, J., García‐Cardeña, G., & Sessa, W. C. (1995) · Biochemistry · doi:10.1021/bi00038a029 · Cited by 131 · see citing works
Self-citation
Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins
Miranda, K. M., Nims, R. W., Thomas, D. D., Espey, M. G., Citrin, D. E., Bartberger, M. D., Paolocci, N., Fukuto, J. M., Feelisch, M., & Wink, D. A. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00498-1 · Cited by 120 · see citing works
Chaperone-dependent Regulation of Endothelial Nitric-oxide Synthase Intracellular Trafficking by the Co-chaperone/Ubiquitin Ligase CHIP
Jiang, J., Cyr, D., Babbitt, R. W., Sessa, W. C., & Patterson, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304738200 · Cited by 110 · see citing works
Self-citation
Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase.
Liu, J., & Sessa, W. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32626-1 · Cited by 96 · see citing works
Self-citation
Disabling a C-terminal Autoinhibitory Control Element in Endothelial Nitric-oxide Synthase by Phosphorylation Provides a Molecular Explanation for Activation of Vascular NO Synthesis by Diverse Physiological Stimuli
Lane, P. B., & Gross, S. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200258200 · Cited by 80 · see citing works
There's NO binding like NOS binding: Protein–protein interactions in NO/cGMP signaling
Nedvetsky, P. I., Sessa, W. C., & Schmidt, H. H. H. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262701999 · Cited by 75 · see citing works
Self-citation

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Evolving functions of endothelial cells in inflammation
Pober, J. S., & Sessa, W. C. (2007) · Nature Reviews Immunology · doi:10.1038/nri2171 · Cited by 2,022 · see citing works
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What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology
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Sansbury, B. E., & Hill, B. G. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.016 · Cited by 274 · see citing works
“It produces relatively low quantities of NO, and its activity is controlled by Ca2þ and calmodulin, posttranslational modifications [72,73], and physical forces such as shear stress [74,75].”
Background
AMP-activated protein kinase functionally phosphorylates endothelial nitric oxide synthase Ser633
Chen, Z., Peng, I.-C., Sun, W., Su, M.-I., Hsu, P.-H., Fu, Y., Zhu, Y., DeFea, K., Pan, S., Tsai, M.-D., et al. (2009) · Circulation Research · doi:10.1161/circresaha.108.187567 · Cited by 264 · see citing works
Endothelial nitric oxide (NO) and its pathophysiologic regulation
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Flow shear stress regulates endothelial barrier function and expression of angiogenic factors in a 3D microfluidic tumor vascular model
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AMP-activated protein kinase is involved in endothelial NO synthase activation in response to shear stress
Zhang, Y., Lee, T.-S., Kolb, E. M., Sun, K., Lu, X., Sladek, F. M., Kassab, G. S., Garland, T., & Shyy, J. Y.-J. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000221230.08596.98 · Cited by 212 · see citing works
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Authors: Sessa, W. C.
Affiliations: Yale University (US)
Corresponding author: Sessa, William C.
ORCID: Sessa, William C.
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2004-05-15
Volume: 117
Issue: 12
Pages: 2427-2429
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.01165
OpenAlex: W2018344800
Cited by: 561
References: 27
Citations by year: 2026: 2 · 2025: 11 · 2024: 15 · 2023: 23 · 2022: 23 · 2021: 20 · 2020: 21 · 2019: 22 · 2018: 19 · 2017: 31 · 2016: 21 · 2015: 21 · 2014: 37 · 2013: 35 · 2012: 33
FWCI: 15.43
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Topics: Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Health and Disease Prevention
Keywords: endothelial nitric oxide synthase, nitric oxide, endothelium, cardiovascular homeostasis, vasodilation, vessel diameter, antiproliferative activity, anti-apoptotic effects
MeSH terms: Animals, Endothelium, Vascular, Enzyme Activation, Humans, Models, Biological, Signal Transduction, Nitric Oxide Synthase, Endothelial Cells

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eNOS at a glance

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