The DOI matches its Crossref record; 45 of the 46 references it cites were found in a registry or an index.
AMP-Activated Protein Kinase Functionally Phosphorylates Endothelial Nitric Oxide Synthase Ser633
Open accessAbstract
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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“Increasing evidence suggests that AMPK is essential in maintaining NO bioavailability.”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [163]
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“AMPK is activated and in turn acts as a direct activator of eNOS by phosphorylating its Ser1177 residue [163].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [163]
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Metadata
- 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)
- Venue
- Circulation Research
- Published
- 2009-02-27
- Volume
- 104
- Issue
- 4
- Pages
- 496-505
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- 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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