Cited by 387Nitric Oxide and Endothelin EffectsProtein Kinase Regulation and GTPase SignalingHemoglobin structure and function

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Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation

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McCabe, Timothy J., Fulton, David, Roman, Linda J., Sessa, William C.·2000·Journal of Biological Chemistry

DOI 10.1074/jbc.275.9.6123

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Abstract

Bovine endothelial nitric oxide synthase (eNOS) is phosphorylated directly by the protein kinase Akt at serine 1179. Mutation of this residue to the negatively charged aspartate (S1179D eNOS) increases nitric oxide (NO) production constitutively, in the absence of agonist challenge. Here, we examine the potential mechanism of how aspartate at 1179 increases eNOS activity using purified proteins. Examination of NO production and cytochrome c reduction resulted in no substantial changes in the K(m)/EC(50) for L-arginine, calmodulin, and calcium, whereas there was a 2-fold increase in the rate of NO production for S1179D and a 2-4-fold increase in reductase activity (based on cytochrome c reduction). The observed increase in activity for both assays of NOS function indicates that a faster rate of electron flux through the reductase domain is likely the rate-limiting step in NO formation from eNOS. In addition, S1179D eNOS did show an increased resistance to inactivation by EGTA compared with wild type eNOS. These results suggest that a negative charge imposed at serine 1179, either by phosphorylation or by replacement with aspartate, increases eNOS catalytic activity by increasing electron flux at the reductase domain and by reducing calmodulin dissociation from activated eNOS when calcium levels are low.

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BackgroundSelf-citation
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Self-citation
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Self-citation
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“This process enhances the rate of electron flux from the reductase to the oxygenase domain of eNOS and reduces the calcium requirements for the enzyme, thus increasing NO synthesis (14).”
Background
Post-translational mechanisms of endothelial nitric oxide synthase regulation by bradykinin
Venema, R. C. (2002) · International Immunopharmacology · doi:10.1016/s1567-5769(02)00185-6 · Cited by 85
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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
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Proteasome Inhibition Down-regulates Endothelial Nitric-oxide Synthase Phosphorylation and Function
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Differences in eNOS Activity Because of Subcellular Localization Are Dictated by Phosphorylation State Rather than the Local Calcium Environment
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Self-citation
p38 Mitogen-Activated Protein Kinase Activates eNOS in Endothelial Cells by an Estrogen Receptor α-Dependent Pathway in Response to Black Tea Polyphenols
Anter, E., Chen, K., Shapira, O. M., Karas, R. H., & Keaney, J. F. (2005) · Circulation Research · doi:10.1161/01.res.0000168807.63013.56 · Cited by 78
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eNOS Gene Therapy Exacerbates Hepatic Ischemia-Reperfusion Injury in Diabetes
Elrod, J. W., Duranski, M. R., Langston, W., Greer, J. J. M., Tao, L., Dugas, T. R., Kevil, C. G., Champion, H. C., & Lefer, D. J. (2006) · Circulation Research · doi:10.1161/01.res.0000231306.03510.77 · Cited by 75
Early ischaemic preconditioning requires Akt- and PKA-mediated activation of eNOS via serine1176 phosphorylation
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“It can be visualized that these phosphorylations would displace the C-terminal a-helix away from the FMN enabling the enhanced rate of the electron flow to the haeme that has been reported with human eNOS with Ser(1177) phosphorylation.(19) This is the first direct demonstration that this eNOS modification occurs in t…”
Background
Nitric Oxide Synthase 3-Dependent Vascular Remodeling and Circulatory Dysfunction in Cirrhosis
Fernández‐Varo, G., Ros, J., Morales‐Ruiz, M., Cejudo–Martín, P., Arroyo, V., Solé, M., Rivera, F., Rodés, J., & Jiménez, W. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64331-3 · Cited by 74
“NOS3 phosphorylation increases the activation state of the enzyme at any given level of free Ca(2) , thereby enhancing NO release from cells.(19,20) Aortas of cirrhotic rats presented a clear signal corresponding to p-NOS3, which was not observed in the vessels of control rats, thus demonstrating NOS3 phosphorylation…”
Background
Nitric oxide in the regulation of the sleep-wake states
Cespuglio, R., Amrouni, D., Meiller, A., Buguet, A., & Gautier-Sauvigné, S. (2012) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2012.01.006 · Cited by 75
Improvement of Peripheral Endothelial Dysfunction by Protein Tyrosine Phosphatase Inhibitors in Heart Failure
Vercauteren, M., Rémy, E., Devaux, C., Dautréaux, B., Henry, J., Bauer, F., Mulder, P. G. H., van Huijsduijnen, R. H., Bombrun, A., Thuillez, C., et al. (2006) · Circulation · doi:10.1161/circulationaha.106.630129 · Cited by 77
Mitochondrial Superoxide Contributes to Blood Flow and Axonal Transport Deficits in the Tg2576 Mouse Model of Alzheimer's Disease
Massaad, C. A., Amin, S. K., Hu, L., Yuan, M., Klann, E., & Pautler, R. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010561 · Cited by 72
“eNOS activity is regulated mainly via phosphorylation, with two most prominent regulatory sites: threonine 495, which is inhibitory [45] and serine 1177, which is permissive [46].”
Background
HSP90 and Akt modulate Ang-1-induced angiogenesis via NO in coronary artery endothelium
Chen, J., Lawrence, M. L., Cunningham, G. R., Christman, B. W., & Meyrick, B. O. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00728.2003 · Cited by 69
“Phosphorylation of eNOS correlates directly with electron flow through the eNOS enzyme, increases in eNOS activity, and NO production by endothelial cells (30).”
Background
Protein kinase N2 mediates flow-induced endothelial NOS activation and vascular tone regulation
Jin, Y., Chennupati, R., Li, R., Liang, G., Wang, S., Iring, A., Graumann, J., Wettschureck, N., & Offermanns, S. (2021) · Journal of Clinical Investigation · doi:10.1172/jci145734 · Cited by 70
“serine 1177 reduces this autoinhibition (58-60).”
Oleanolic acid induces relaxation and calcium‐independent release of endothelium‐derived nitric oxide
Rodríguez‐Rodríguez, R., Stankevıčıus, E., Herrera, M. D., Østergaard, L., Andersen, M. R., Ruíz-Gutiérrez, V., & Simonsen, U. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.289 · Cited by 67
“, 2001), even at resting levels of calcium (Montagnani et al., 2001; McCabe et al., 2000).”
Background
Functional implications of vascular endothelium in regulation of endothelial nitric oxide synthesis to control blood pressure and cardiac functions
Kumar, G., Dey, S. K., & Kundu, S. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118377 · Cited by 71
Deficient eNOS Phosphorylation Is a Mechanism for Diabetic Vascular Dysfunction Contributing to Increased Stroke Size
Li, Q., Atochin, D. N., Kashiwagi, S., Earle, J., Wang, A., Mandeville, E. T., Hayakawa, K., d’Uscio, L. V., Lo, E. H., Katušić, Z. S., et al. (2013) · Stroke · doi:10.1161/strokeaha.113.002073 · Cited by 65
“This site is phosphorylated by Akt kinase,(2,3) AMP kinase,(6) and protein kinase A,(7) resulting in a conformational change, enhancing electron flux through the reductase domain, and increasing NO production.(8) eNOSderived NO plays known protective roles in cerebral ischemia, including maintenance of cerebral blood…”
BackgroundSelf-citation
Role of Endothelial Nitric Oxide Synthase in the Regulation of SREBP Activation by Oxidized Phospholipids
Gharavi, N. M., Baker, N. A., Mouillesseaux, K. P., Yeung, W., Honda, H. M., Hsieh, X., Yeh, M. W., Smart, E. J., & Berliner, J. A. (2006) · Circulation Research · doi:10.1161/01.res.0000215343.89308.93 · Cited by 65
Phosphorylated Endothelial Nitric Oxide Synthase Mediates Vascular Endothelial Growth Factor-Induced Penile Erection1
Musicki, B., Palese, M., Crone, J. K., & Burnett, A. L. “. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.103.021113 · Cited by 65
“This posttranslational modification accelerates electron flux through the enzyme, reducing the enzyme’s calcium requirement and causing increased and prolonged production of NO [22].”
Background
Electronic cigarette exposure causes vascular endothelial dysfunction due to NADPH oxidase activation and eNOS uncoupling
El‐Mahdy, M. A., Ewees, M. G., Eid, M. S., Mahgoup, E. M., Khaleel, S. A., & Zweier, J. L. (2022) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00460.2021 · Cited by 69
Inhibition of heat shock protein 90 (hsp90) in proliferating endothelial cells uncouples endothelial nitric oxide synthase activity
Ou, J., Ou, Z., Ackerman, A. W., Oldham, K. T., & Pritchard, K. A. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01299-6 · Cited by 63
Signalling mechanisms in the cardiovascular protective effects of estrogen: With a focus on rapid/membrane signalling.
Niță, A.-R., Knock, G. A., & Heads, R. J. (2021) · Current Research in Physiology · doi:10.1016/j.crphys.2021.03.003 · Cited by 65
Coordinated regulation of endothelial nitric oxide synthase activity by phosphorylation and subcellular localization
Boo, Y. C., Kim, H. J., Song, H. W., Fulton, D. J., Sessa, W. C., & Jo, H. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.03.024 · Cited by 62
Self-citation
Role of Heat Shock Protein 90 and Endothelial Nitric Oxide Synthase during Early Anesthetic and Ischemic Preconditioning
Amour, J., Brzezinska, A. K., Weihrauch, D., Billstrom, A. R., Zielonka, J., Krolikowski, J. G., Bienengraeber, M. W., Warltier, D. C., Pratt, P. F., & Kersten, J. R. (2009) · Anesthesiology · doi:10.1097/aln.0b013e3181942cb4 · Cited by 62
“tion is proportional to the extent of eNOS phosphorylation.(8) Certain pathophysiological stimuli, such as”
Background
Angiostatin
Koshida, R., Ou, J., Matsunaga, T., Chilian, W. M., Oldham, K. T., Ackerman, A. W., & Pritchard, K. A. (2003) · Circulation · doi:10.1161/01.cir.0000057551.88851.09 · Cited by 62
Role of endothelial [Ca2+]iin activation of eNOS in pressurized arterioles by agonists and wall shear stress
Ungvari, Z. I., Sun, D., Huang, A., Kaley, G., & Koller, Á. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.2.h606 · Cited by 62
“Recently, it has been shown that in cultured endothelial cells, eNOS can be phosphorylated and stimulated by tyrosine kinases that can be activated by shear stress (1, 4, 9, 10, 13, 26, 28, 36).”
BackgroundInfluential
Rapid, Estrogen Receptor–Mediated Signaling: Why Is the Endothelium So Special?
Kim, K. H., & Bender, J. R. (2005) · Science s STKE · doi:10.1126/stke.2882005pe28 · Cited by 61
Intensive exercise induces changes of endothelial nitric oxide synthase pattern in human erythrocytes
Suhr, F., Porten, S., Hertrich, T., Brixius, K., Schmidt, A., Platen, P., & Bloch, W. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.10.004 · Cited by 61
A connecting hinge represses the activity of endothelial nitric oxide synthase
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Phospholamban S-nitrosylation modulates Starling response in fish heart
Garofalo, F., Parisella, M. L., Amelio, D., Tota, B., & Imbrogno, S. (2009) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2009.1189 · Cited by 59
“This mechanism, which involves membrane caveolae (regarding their occurrence in fish heart, see Di Maio & Block 2008) and cytoskeleton (Casadei & Sears 2003), causes a sustained increase in enzyme activity, probably by reducing the dissociation of calmodulin from activated eNOS (McCabe et al. 2000), thus enhancing NO…”
Background
Neurovascular protection by adropin in experimental ischemic stroke through an endothelial nitric oxide synthase-dependent mechanism
Yang, C., Lavayen, B. P., Liu, L., Sanz, B. D., DeMars, K. M., Larochelle, J., Pompilus, M., Febo, M., Sun, Y., Kuo, Y.-M., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102197 · Cited by 61
“Other studies have shown that eNOS is protective in ischemic stroke [52–55], and eNOS phosphorylation at Ser1176 (based on mouse eNOS sequence and equivalent to human eNOS at Ser1177 or bovine eNOS at Ser1179) is a key post-translational modification indispensable for its enzymatic activity [43].”
Background
Low-Level Lead Exposure Increases Systolic Arterial Pressure and Endothelium-Derived Vasodilator Factors in Rat Aortas
Fiorim, J., Ribeiro, E. H., Silveira, E. A., Padilha, A. S., Vescovi, M. V. A., de Jesus, H. C., Stefanon, I., Salaíces, M., & Vassallo, D. V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017117 · Cited by 59
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Simonsen, U., Rodríguez‐Rodríguez, R., Dalsgaard, T., Buus, N. H., & Stankevıčıus, E. (2009) · Pharmacological Reports · doi:10.1016/s1734-1140(09)70012-x · Cited by 59
“, insulin) [60] even at resting levels of calcium [55, 60].”
Background
Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells
Tzima, E., Reader, J. S., Irani-Tehrani, M., Ewalt, K. L., Schwartz, M. A., & SCHIMMEL, P. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436330100 · Cited by 59
Preserved endothelium-dependent dilatation of the coronary microvasculature at the early phase of diabetes mellitus despite the increased oxidative stress and depressed cardiac mechanical function ex vivo
Mourmoura, E., Vial, G., Laillet, B., Rigaudière, J., Hininger‐Favier, I., Dubouchaud, H., Morio, B., & Demaison, L. (2013) · Cardiovascular Diabetology · doi:10.1186/1475-2840-12-49 · Cited by 57
“We also evaluated indirectly the NO production through measurements of the expression and phosphorylation of the cardiac and aortic eNOS, since the phosphorylation of the enzyme at this site has been shown to increase NO production [58], and that of the iNOS levels, since it has been shown that under diabetic conditio…”
Method
Promotion of nitric oxide production: mechanisms, strategies, and possibilities
Gonzalez, M., Clayton, S., Wauson, E., Christian, D., & Tran, Q. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1545044 · Cited by 62
Effects of Combined Phosphorylation at Ser-617 and Ser-1179 in Endothelial Nitric-oxide Synthase on EC50(Ca2+) Values for Calmodulin Binding and Enzyme Activation
Tran, Q., Leonard, J., Black, D. J., Nadeau, O. W., Boulatnikov, I. G., & Persechini, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806205200 · Cited by 55
Nitric oxide signalling in salivary glands
Looms, D., Tritsaris, K., Pedersen, A. M. L., Nauntofte, B., & Dissing, S. (2002) · Journal of Oral Pathology and Medicine · doi:10.1034/j.1600-0714.2002.00047.x · Cited by 54
Phosphorylation inactivation of endothelial nitric oxide synthesis in pulmonary arterial hypertension
Ghosh, S., Gupta, M. K., Xu, W., Mavrakis, D. A., Janocha, A. J., COMHAIR, S. A. A., Haque, M. M., Stuehr, D. J., Yu, J., POLGAR, P. R., et al. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00092.2016 · Cited by 57
“Activation of eNOS requires dimerization of the enzyme along with cofactors including tetrahydrobiopterin and calmodulin (51), but the dominant control of eNOS activity occurs via phosphorylation of specific residues within the enzyme (6, 18, 27, 39, 40).”
Background
S1P and eNOS regulation
IGARASHI, J. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.06.008 · Cited by 53
(−)-Epicatechin induces calcium and translocation independent eNOS activation in arterial endothelial cells
Ramírez‐Sánchez, I., Maya-Ramos, L., Ceballos, G. M., & Villarreal, F. J. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00406.2010 · Cited by 52
“The phosphorylation of eNOS-Ser-1177, Ser-633, and Ser-615 (human sequence) is associated with increases in enzymatic activity (23, 13), whereas the phosphorylation at Thr-495 decreases its activity (6, 15).”
Background
Endothelial Nitric Oxide Synthase Dimerization Is Regulated by Heat Shock Protein 90 Rather than by Phosphorylation
Chen, W., Xiao, H., Rizzo, A. N., Zhang, W., Mai, Y., & Ye, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105479 · Cited by 52
“Additionally, Ser1179 phosphorylation results in electron transfer efficiency in eNOS reductase domain [41].”
Background
Endothelial Cell Autonomous Role of Akt1
Lee, M. Y., Gámez-Méndez, A. M., Zhang, J., Zhuang, Z., Vinyard, D. J., Kraehling, J. R., Velázquez, H., Brudvig, G. W., Kyriakides, T. R., Simons, M., et al. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.310748 · Cited by 50
Self-citation
Functional characterization of Glu298Asp mutant human endothelial nitric oxide synthase purified from a yeast expression system
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cAMP signal transduction induces eNOS activation by promoting PKB phosphorylation
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Differences in a Conformational Equilibrium Distinguish Catalysis by the Endothelial and Neuronal Nitric-oxide Synthase Flavoproteins
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Authors: McCabe, T. J., Fulton, D., Roman, L. J., & Sessa, W. C.
Affiliations: Yale University (US)
The University of Texas at San Antonio Health Science Center (US)
Corresponding author: Sessa, William C.
ORCID: McCabe, Timothy J.
Fulton, David
Sessa, William C.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2000-03
Volume: 275
Issue: 9
Pages: 6123-6128
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.275.9.6123
OpenAlex: W2090688283
Cited by: 387
References: 32
Citations by year: 2025: 6 · 2024: 3 · 2023: 5 · 2022: 11 · 2021: 13 · 2020: 18 · 2019: 4 · 2018: 11 · 2017: 8 · 2016: 9 · 2015: 16 · 2014: 18 · 2013: 14 · 2012: 21
FWCI: 14.94
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7526 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: American Heart Association
National Institutes of Health (HL61371, HL64793)
National Heart, Lung, and Blood Institute (HL-61371, HL-64793, R01HL064793, HL 57665, R01HL057665)
National Institute of General Medical Sciences (R01GM052419)
Topics: Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords: endothelial nitric oxide synthase, eNOS phosphorylation, Akt, nitric oxide production, electron flux, reductase domain, calcium-independent activation, cytochrome c reduction, L-arginine
MeSH terms: Animals, Calcium, Calmodulin, Cattle, Egtazic Acid, Electrons, Enzyme Activation, Kinetics, Mutation, NADH Dehydrogenase, NADP, Nitric Oxide, Phosphorylation, Proto-Oncogene Proteins, Protein Serine-Threonine Kinases, Nitric Oxide Synthase, Dimerization, Proto-Oncogene Proteins c-akt, Nitric Oxide Synthase Type III, Static Electricity

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Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation

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