Cited by 264Nitric Oxide and Endothelin EffectsMetabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase Signaling

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AMP-Activated Protein Kinase Functionally Phosphorylates Endothelial Nitric Oxide Synthase Ser633

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Chen, Zhen, Peng, I-Chen, Sun, Wei, Su, Mei-I, Hsu, Pang-Hung, Fu, Yi, Zhu, Yi, DeFea, Kathryn, Pan, Songqin, Tsai, Ming-Daw, Shyy, John Y-J.·2009·Circulation Research

DOI 10.1161/circresaha.108.187567PMC PMC2761102

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Abstract

Endothelial nitric oxide synthase (eNOS) plays a central role in maintaining cardiovascular homeostasis by controlling NO bioavailability. The activity of eNOS in vascular endothelial cells (ECs) largely depends on posttranslational modifications, including phosphorylation. Because the activity of AMP-activated protein kinase (AMPK) in ECs can be increased by multiple cardiovascular events, we studied the phosphorylation of eNOS Ser633 by AMPK and examined its functional relevance in the mouse models. Shear stress, atorvastatin, and adiponectin all increased AMPK Thr172 and eNOS Ser633 phosphorylations, which were abolished if AMPK was pharmacologically inhibited or genetically ablated. The constitutively active form of AMPK or an AMPK agonist caused a sustained Ser633 phosphorylation. Expression of gain-/loss-of-function eNOS mutants revealed that Ser633 phosphorylation is important for NO production. The aorta of AMPKalpha2(-/-) mice showed attenuated atorvastatin-induced eNOS phosphorylation. Nano-liquid chromatography/tandem mass spectrometry (LC/MS/MS) confirmed that eNOS Ser633 was able to compete with Ser1177 or acetyl-coenzyme A carboxylase Ser79 for AMPKalpha phosphorylation. Nano-LC/MS/MS confirmed that eNOS purified from AICAR-treated ECs was phosphorylated at both Ser633 and Ser1177. Our results indicate that AMPK phosphorylation of eNOS Ser633 is a functional signaling event for NO bioavailability in ECs.

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Background
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BackgroundInfluential
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BackgroundResult
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Background
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Background
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Background
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Thiopental Inhibits Global Protein Synthesis by Repression of Eukaryotic Elongation Factor 2 and Protects from Hypoxic Neuronal Cell Death
Schwer, C. I., Lehane, C., Guelzow, T., Zenker, S., Strosing, K. M., Spassov, S. G., Erxleben, A., Heimrich, B., Buerkle, H., & Humar, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077258 · Cited by 26
“Additionally, AMPK has been associated with induction of eNOS [32], an enzyme that promotes vasodilatation, increases regional blood flow in ischemic brain tissue, and reduces infarct volume [33].”
Background
Reduced Endothelium-Dependent Relaxation to Anandamide in Mesenteric Arteries from Young Obese Zucker Rats
Lobato, N. S., Filgueira, F. P., Prakash, R., Giachini, F. R. C., Ergul, A., de Carvalho, M. H. C., Webb, R. C., Tostes, R. C., & Fortes, Z. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063449 · Cited by 26
“Recent studies indicate that cannabinoid compounds activate the AMPK pathway in tissues that control energy homeostasis [56].”
Background
Fasting as Medicine: Mitochondrial and Endothelial Rejuvenation in Vascular Aging
Milan, M., Troyano‐Rodriguez, E., Ihuoma, J., Negri, S., Rudraboina, R., Kosmider, A., Awasthi, S., Balasubramanian, P., Conley, S. M., Yabluchanskiy, A., et al. (2026) · Aging Cell · doi:10.1111/acel.70372 · Cited by 25
“Activation of AMPK enhances endothelial NO bioavailability (Chen et al. 2009), stimulates mitochondrial biogenesis, promotes autophagy and mitophagy (Rodriguez et al. 2021), and reduces oxidative stress (Jansen et al. 2021).”
The Role of Sirtuin-1 (SIRT1) in the Physiology and Pathophysiology of the Human Placenta
Wątroba, M., Szewczyk, G., & Szukiewicz, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216210 · Cited by 29
“SIRT1 may directly deacetylate eNOs, or stimulate eNOs activity indirectly by affecting FoxO proteins and AMPK-dependent signaling pathways [156], which can participate in PE pathogenesis.”
Background
Comparison of cardioprotective efficacy resulting from a combination of atorvastatin and ischaemic post‐conditioning in diabetic and non‐diabetic rats
Fan, Y., Yang, S., Zhang, X.-K., Cao, Y., & Huang, Y. (2012) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12014 · Cited by 25
Morinda citrifolia ( Noni ) fruit juice promotes vascular endothelium function in hypertension via glucagon‐like peptide‐1 receptor‐CaMKKβ‐AMPK‐eNOS pathway
Yoshitomi, H., Zhou, J., Nishigaki, T., Li, W., Liu, T., Wu, L., & Gao, M. (2020) · Phytotherapy Research · doi:10.1002/ptr.6685 · Cited by 24
“AMPK, which is activated leading to the phospharalytion and activation of eNOS, has been reported to enhance NO production and vasodilatory effect in vascular endothelial cells (Chen et al., 2009; Kanazawa, Yamaguchi, Yano, Yamauchi, & Sugimoto, 2008; Li et al., 2008).”
Background
Effects and Mechanisms of Five Psoralea Prenylflavonoids on Aging-Related Diseases
Zhou, Y., Zhu, L., Yuan, Y., Ling, S., & Xu, J. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2128513 · Cited by 24
“Our multiple results indicate (Figure 4) that AMPK-mediated cardiovascular protection of bavachalcone can include regulating mitochondrial biogenesis [65], delaying cell senescence [66], activating eNOS, MnSOD and PGC-1α activity and expression [67, 68], and promoting EPC differentiation [69], which presents consisten…”
Result
NmFGF1-Regulated Glucolipid Metabolism and Angiogenesis Improves Functional Recovery in a Mouse Model of Diabetic Stroke and Acts via the AMPK Signaling Pathway
Zhao, Y., Ye, S., Lin, J., Liang, F., Chen, J., HU, J. L., Chen, K., Fang, Y., Chen, X., Xiong, Y., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.680351 · Cited by 24
Type 2 Diabetes and Vascular Endothelial Dysfunction
Torimoto, K., Okada, Y., & Tanaka, Y. (2018) · Journal of UOEH · doi:10.7888/juoeh.40.65 · Cited by 24
AMPK activation promotes gastroprotection through mutual interaction with the gaseous mediators H 2 S, NO, and CO
de Araújo, S., de Oliveira, A. P., Sousa, F. B. M., de Souza, L. K. M., Pacheco, G., Filgueiras, M. D. C., Nicolau, L. A. D., Brito, G. A. D. C., Cerqueira, G. S., Silva, R. O., et al. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.05.008 · Cited by 23
EDF-1 contributes to the regulation of nitric oxide release in VEGF-treated human endothelial cells
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Disrupted eNOS activity and expression account for vasodilator dysfunction in different stage of sepsis
Hu, S., Pi, Q., Xu, X., Yan, J., Guo, Y., Tan, W., He, A., Cheng, Z., Luo, S., & Xia, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118606 · Cited by 22
Chronic activation of AMP‐activated protein kinase prevents 20‐hydroxyeicosatetraenoic acid‐induced endothelial dysfunction
Ward, N. C., Chen, K., Li, C., Croft, K. D., & Keaney, J. F. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05509.x · Cited by 22
“The serine-1177 residue is typically seen as an activation site that is required for normal eNOS function.(13) There were no changes observed at serine-633; however, phosphorylation of threonine-495 increased over time.”
Background
Regulation of cardiac miR-208a, an inducer of obesity, by rapamycin and nebivolol
Gul, R., Mahmood, A., Luck, C., Lum‐Naihe, K., Alfadda, A. A., Speth, R. C., & Pulakat, L. (2015) · Obesity · doi:10.1002/oby.21227 · Cited by 22
“In addition to being a b1-AR blocker, Neb is known to act as an agonist of b3-AR and also to activate endothelial nitric oxide synthase (eNOS) and AMP kinase (27-31).”
Panax Notoginseng Protects against Diabetes‐Associated Endothelial Dysfunction: Comparison between Ethanolic Extract and Total Saponin
Zhang, X., Zhou, C., Miao, L., Tan, Y., Zhou, Y., Cheong, M. S., Huang, Y., Wang, Y., Yu, H., & Cheang, W. S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4722797 · Cited by 21
“AMPK activation stimulates eNOS and increases NO bioavailability [23].”
Background
RAMP2-AS1 Regulates Endothelial Homeostasis and Aging
Lai, C., Chen, A. T., Burns, A. B., Sriram, K., Luo, Y., Tang, X., Branciamore, S., O’Meally, D., Chang, S.-L., Huang, P., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.635307 · Cited by 20
AMP-Activated Protein Kinase Inhibits Homocysteine-Induced Dysfunction and Apoptosis in Endothelial Progenitor Cells
Jia, F., Wu, C., Chen, Z., & Lü, G. (2011) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-010-6277-1 · Cited by 20
“AMPK could phosphorylate eNOS Ser633 to regulate NO bioavailability [ 16 ], and mediate some cardiovascular protective effects of drugs such as atorvastatin through eNOS activation [17].”
Background
Sildenafil Alleviates Murine Experimental Autoimmune Encephalomyelitis by Triggering Autophagy in the Spinal Cord
Duarte-Silva, E. P., Araújo, S. M. D. R., de Oliveira, W. H., Lós, D. B., Bonfanti, A. P., Peron, G., Thomaz, L. D. L., Verinaud, L. M. C., & Peixoto, C. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.671511 · Cited by 18
“It is worthy to mention that activated AMPK phosphorylates and activates eNOS, leading to NO production, which in turn activates AMPK (41, 43).”
Background
Advances in endothelial shear stress proteomics
Firasat, S., Hecker, M., Binder, L., & Asif, A. R. (2014) · Expert Review of Proteomics · doi:10.1586/14789450.2014.933673 · Cited by 21
“eNOS activity is regulated by phosphorylation/ dephosphorylation of serine (Ser) and threonine residues by protein kinases/phosphatases [56,57].”
Background
Role of Ca2+ in the Control of H2O2-Modulated Phosphorylation Pathways Leading to eNOS Activation in Cardiac Myocytes
Sartoretto, J. L., Kalwa, H., Shiroto, T., Sartoretto, S., Pluth, M. D., Lippard, S. J., & Michel, T. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044627 · Cited by 19
“We and others have previously reported that AMPK regulates eNOS in endothelial cells [21,22].”
AMP-Activated Protein Kinase
Hardie, D. G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00073-5 · Cited by 19
Shear Stress-Induced AMP-Activated Protein Kinase Modulation in Endothelial Cells: Its Role in Metabolic Adaptions and Cardiovascular Disease
Hauger, P. C., & Hordijk, P. L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116047 · Cited by 21
“Further investigations revealed that shear stress-activated AMPK phosphorylates eNOS at Ser633 and Ser1177 [45,71].”
Background
Omics‐based approaches to understand mechanosensitive endothelial biology and atherosclerosis
Simmons, R. D., Kumar, S., Thabet, S., Sur, S., & Jo, H. (2016) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1344 · Cited by 18
“Furthermore, AMPK can directly phosphorylate eNOS at Ser633 in response to shear stress, statins, and adiponectin and is crucial for NO bioavailability.(213) AMPK not only regulates eNOS directly but also regulates the key mechanosensitive transcription factor KLF2 which also regulates eNOS.”
Background
Randomised clinical study: acute effects of metformin versus placebo on portal pressure in patients with cirrhosis and portal hypertension
Rittig, N. F., Aagaard, N. K., Villadsen, G. E., Sandahl, T. D., Jessen, N., Grønbæk, H., & George, J. (2021) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.16460 · Cited by 17
Inhibition of sphingomyelinase attenuates diet – Induced increases in aortic stiffness
Habibi, J., DeMarco, V. G., Hulse, J. L., Hayden, M. R., Whaley‐Connell, A. T., Hill, M. A., Sowers, J. R., & Jia, G. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.03.006 · Cited by 17
Diminazene aceturate uses different pathways to induce relaxation in healthy and atherogenic blood vessels
Gadanec, L. K., Qaradakhi, T., McSweeney, K. R., Matsoukas, J., Apostolopoulos, V., Burrell, L. M., & Zulli, A. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115397 · Cited by 16
Regulation of Overnutrition-Induced Cardiac Inflammatory Mechanisms by nebivolol
Gul, R., DeMarco, V. G., Sowers, J. R., Whaley‐Connell, A. T., & Pulakat, L. (2012) · Cardiorenal Medicine · doi:10.1159/000339565 · Cited by 16
Molecular modeling and simulation of the human eNOS reductase domain, an enzyme involved in the release of vascular nitric oxide
Devika, N. T., Amresh, P., Hassan, M. I., & Ali, B. M. J. (2014) · Journal of Molecular Modeling · doi:10.1007/s00894-014-2470-7 · Cited by 16
“Experimental observations reported in the literature suggest that S633 functions as a stimulatory phosphorylation site which is stimulated in response to shear stress [43].”
Background
Methotrexate and Cardiovascular Protection: Current Evidence and Future Directions
Mangoni, A. A., Zinellu, A., Sotgia, S., Carru, C., & Erre, G. L. (2017) · Clinical Medicine Insights Therapeutics · doi:10.1177/1179559x17741289 · Cited by 18
N-cadherin coordinates AMP kinase-mediated lung vascular repair
Jian, M., Liu, Y., Li, Q., Wolkowicz, P. E., ALEXEYEV, M. F., Zmijewski, J. W., & Creighton, J. R. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00227.2015 · Cited by 15
Pathological basis of cardiac arrhythmias: vicious cycle of immune-metabolic dysregulation
Wang, S. C., Meng, D., Yang, H.-P., Wang, X., Jia, S., Wang, Y., & Wang, P. (2017) · Cardiovascular Disorders and Medicine · doi:10.15761/cdm.1000158 · Cited by 15
“This proposal is supported by the studies on vascular endothelial cells in mice [30] and human umbilical vein endothelial cells [31].”
Result
Carotid Disease and Ageing: A Literature Review on the Pathogenesis of Vascular Senescence in Older Subjects
Sertedaki, E., Veroutis, D., Zagouri, F., Galyfos, G. C., Filis, K., Papalambros, A., Aggeli, K. D., Tsioli, P., Charalambous, G., Zografos, G., et al. (2020) · Current Gerontology and Geriatrics Research · doi:10.1155/2020/8601762 · Cited by 15
Liver X Receptor Agonist Alleviated High Glucose‐Induced Endothelial Progenitor Cell Dysfunction via Inhibition of Reactive Oxygen Species and Activation of AMP‐Activated Protein Kinase
Li, X., Song, Y., Han, Y., Wang, D., & Zhu, Y. (2012) · Microcirculation · doi:10.1111/j.1549-8719.2012.00186.x · Cited by 14
“We and other groups previously reported that AMPK-eNOS activation could improve EPC differentiation [2,6,10].”
Background
Methotrexate and Vasculoprotection: Mechanistic Insights and Potential Therapeutic Applications in Old Age
Mangoni, A. A., Tommasi, S., Zinellu, A., Sotgia, S., Bassu, S., Piga, M., Erre, G. L., & Carru, C. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191112091700 · Cited by 14
Apelin prevents diabetes-induced poor collateral vessel formation and blood flow reperfusion in ischemic limb
Robillard, S., Trân, K., Lachance, M.-S., Brazeau, T., Boisvert, E., Lizotte, F., Auger‐Messier, M., Boudreault, P., Marsault, É., & Geraldes, P. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1191891 · Cited by 13
“Interestingly, the administration of Pyr-apelin-13 in diabetic mice increased both Ser1177 phosphorylation of eNOS by 3.7-fold (P = 0.0010; reported to GAPDH) or 4.3-fold (P = 0.0224; reported to total eNOS) (Figures 5A,F,G) and Ser633 by 2.5-fold (P = 0.0168; reported to GAPDH) or 2.1-fold (P = 0.0058; reported to to…”
BackgroundInfluential
Kidney-specific genetic deletion of both AMPK α-subunits causes salt and water wasting
Lazo‐Fernandez, Y., Baile, G., Meade, P., Torcal, P., Martínez-Gimeno, L., Ibañez, C. R., Bernal, M. L., Viollet, B., & Gimenez-Lopez, I. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00169.2016 · Cited by 15
“In addition, AMPK stimulates vasorelaxation through endothelium-dependent hyperpolarization (19) and the activation of endothelial nitric oxide (NO) synthase (13, 14, 55).”
Background
Adiponectin promotes the migration of circulating angiogenic cells through p38-mediated induction of the CXCR4 receptor
Adams, V., Heiker, J. T., Höllriegel, R., Beck, E. B., Woitek, F. J., Erbs, S., Blüher, M., Stümvoll, M., Beck‐Sickinger, A. G., Schuler, G. C., et al. (2012) · International Journal of Cardiology · doi:10.1016/j.ijcard.2012.05.056 · Cited by 13
“With respect to the underlying signaling pathways, the involvement of AMP-activated protein kinase (AMPK) in the phosphorylation of eNOS either at position Ser or Ser is proven in the literature [34–36].”
Background
Sex-Specific Antioxidant and Anti-Inflammatory Protective Effects of AMPK in Cardiovascular Diseases
Strohm, L., Mihaliková, D., Czarnowski, A., Schwaibold, Z., Daiber, A., & Stamm, P. (2025) · Antioxidants · doi:10.3390/antiox14050615 · Cited by 12
“Physiological, pharmacological, and hormonal stimuli, including shear stress, statins, or adiponectin, can directly activate AMPK, leading to eNOS phosphorylation at Ser633/635 and increased NO production [59–62].”
Empagliflozin mitigates methotrexate-induced nephrotoxicity in male albino rats: insights on the crosstalk of AMPK/Nrf2 signaling pathway
Mishriki, A., Khalifa, A. K., Ibrahim, D. A., Hashem, G., Rashed, L. A., Abdelrahmen, S. S., & Mahmoud, H. (2024) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-024-00669-3 · Cited by 12
“It also regulates endothelial function through boosting endothelial nitric oxide synthase (eNOS) [42, 43].”
Background
Vascular adenosine monophosphate‐activated protein kinase: Enhancer, brake or both?
Chen, H., Vanhoutte, P. M., & Leung, S. W. S. (2019) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13357 · Cited by 14

Authors: Chen, Z., Peng, I.-C., Sun, W., Su, M.-I., Hsu, P.-H., Fu, Y., Zhu, Y., DeFea, K., Pan, S., Tsai, M.-D., & Shyy, J. Y.-J.
Affiliations: University of California, Riverside (US)
ORCID: Chen, Zhen
Peng, I-Chen
Sun, Wei
Hsu, Pang-Hung
Zhu, Yi
DeFea, Kathryn
Tsai, Ming-Daw
Venue: Circulation Research
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2009-02-27
Volume: 104
Issue: 4
Pages: 496-505
ISSN: 0009-7330 (ISSN-L)
1524-4571
DOI: 10.1161/circresaha.108.187567
PMC: PMC2761102
OpenAlex: W1966733021
Cited by: 264
References: 46
Citations by year: 2026: 8 · 2025: 6 · 2024: 8 · 2023: 6 · 2022: 10 · 2021: 17 · 2020: 19 · 2019: 12 · 2018: 13 · 2017: 13 · 2016: 14 · 2015: 22 · 2014: 27 · 2013: 15 · 2012: 26
FWCI: 16.35
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Circulation Research (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Heart, Lung, and Blood Institute (HL-77448, R01HL089940, R01HL077448, HL89940)
National Institute of General Medical Sciences (R01GM066151)
Topics: Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: AMPK, endothelial nitric oxide synthase, eNOS Ser1177 phosphorylation, nitric oxide bioavailability, shear stress, atorvastatin, adiponectin, AMPKα2, vascular endothelial cells, post-translational modification, AICAR
MeSH terms: Atorvastatin, Acetyl-CoA Carboxylase, Aminoimidazole Carboxamide, Animals, Cattle, Cells, Cultured, Chromatography, Liquid, Enzyme Activation, Heptanoic Acids, Humans, Mice, Inbred C57BL, Mutation, Nitric Oxide, Phosphorylation, Protein Processing, Post-Translational, Pyrazoles, Pyrimidines, Pyrroles, Ribonucleotides, Serine, Stress, Mechanical, Time Factors, Transfection, Signal Transduction, Mice, Knockout, Hydroxymethylglutaryl-CoA Reductase Inhibitors, RNA Interference, RNA, Small Interfering, Nanotechnology, Endothelial Cells, Protein Kinase Inhibitors, Mice, Adiponectin, Nitric Oxide Synthase Type III, Tandem Mass Spectrometry, AMP-Activated Protein Kinases

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AMP-Activated Protein Kinase Functionally Phosphorylates Endothelial Nitric Oxide Synthase Ser633

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