Regulation of endothelial and myocardial NO synthesis by multi-site eNOS phosphorylation (Q36535244)

14 August 2017

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title

Regulation of endothelial and myocardial NO synthesis by multi-site eNOS phosphorylation (English)

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14 August 2017

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1

Peter F Mount

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14 August 2017

Bruce E Kemp

2

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PubMed ID

16839566

14 August 2017

David A Power

series ordinal

3

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14 August 2017

12 July 2006

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Journal of Molecular and Cellular Cardiology

14 August 2017

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14 August 2017

42

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14 August 2017

2

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14 August 2017

271-279

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The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine

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Mammalian nitric oxide synthases

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Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme

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Enzymatic function of nitric oxide synthases

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AMP-activated protein kinase phosphorylation of endothelial NO synthase

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Regulation of endothelium-derived nitric oxide production by the protein kinase Akt

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Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase

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Identification of regulatory sites of phosphorylation of the bovine endothelial nitric-oxide synthase at serine 617 and serine 635.

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Regulation of endothelial nitric oxide synthase by protein kinase C.

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Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1

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Shear stress stimulates phosphorylation of endothelial nitric-oxide synthase at Ser1179 by Akt-independent mechanisms: role of protein kinase A.

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Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation

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Insulin-stimulated activation of eNOS is independent of Ca2+ but requires phosphorylation by Akt at Ser(1179).

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Acute activation and phosphorylation of endothelial nitric oxide synthase by HMG-CoA reductase inhibitors

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Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation

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The Akt kinase signals directly to endothelial nitric oxide synthase

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Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity.

7 January 2021

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Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases

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Coordinated control of endothelial nitric-oxide synthase phosphorylation by protein kinase C and the cAMP-dependent protein kinase

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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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Site-specific dephosphorylation of endothelial nitric oxide synthase by protein phosphatase 2A: evidence for crosstalk between phosphorylation sites

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Phosphorylation of threonine 497 in endothelial nitric-oxide synthase coordinates the coupling of L-arginine metabolism to efficient nitric oxide production

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Hydrogen peroxide activates endothelial nitric-oxide synthase through coordinated phosphorylation and dephosphorylation via a phosphoinositide 3-kinase-dependent signaling pathway.

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Vascular consequences of endothelial nitric oxide synthase uncoupling for the activity and expression of the soluble guanylyl cyclase and the cGMP-dependent protein kinase

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Shear stress stimulates phosphorylation of eNOS at Ser(635) by a protein kinase A-dependent mechanism

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Endothelial NO synthase phosphorylated at SER635 produces NO without requiring intracellular calcium increase

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Dephosphorylation of endothelial nitric-oxide synthase by vascular endothelial growth factor. Implications for the vascular responses to cyclosporin A.

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Nitric oxide production and regulation of endothelial nitric-oxide synthase phosphorylation by prolonged treatment with troglitazone: evidence for involvement of peroxisome proliferator-activated receptor (PPAR) gamma-dependent and PPARgamma-indepen

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Identification of flow-dependent endothelial nitric-oxide synthase phosphorylation sites by mass spectrometry and regulation of phosphorylation and nitric oxide production by the phosphatidylinositol 3-kinase inhibitor LY294002

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High-density lipoprotein and apolipoprotein AI increase endothelial NO synthase activity by protein association and multisite phosphorylation

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Hsp90 ensures the transition from the early Ca2+-dependent to the late phosphorylation-dependent activation of the endothelial nitric-oxide synthase in vascular endothelial growth factor-exposed endothelial cells

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Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release

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Synergistic activation of endothelial nitric-oxide synthase (eNOS) by HSP90 and Akt: calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex

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Heat shock protein 90 transfection reduces ischemia-reperfusion-induced myocardial dysfunction via reciprocal endothelial NO synthase serine 1177 phosphorylation and threonine 495 dephosphorylation.

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Roles of 3-phosphoinositide-dependent kinase 1 in the regulation of endothelial nitric-oxide synthase phosphorylation and function by heat shock protein 90.

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Dynamic activation of endothelial nitric oxide synthase by Hsp90.

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Post-translational mechanisms of endothelial nitric oxide synthase regulation by bradykinin

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Calmodulin-dependent endothelium-derived relaxing factor/nitric oxide synthase activity is present in the particulate and cytosolic fractions of bovine aortic endothelial cells

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Inhibitory interactions of the bradykinin B2 receptor with endothelial nitric-oxide synthase

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Functional interaction of endothelial nitric oxide synthase with a voltage-dependent anion channel.

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Role of heat shock protein 90 in bradykinin-stimulated endothelial nitric oxide release

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Rapid increase in endothelial nitric oxide production by bradykinin is mediated by protein kinase A signaling pathway

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Receptor-regulated translocation of endothelial nitric-oxide synthase

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Thrombin and histamine stimulate endothelial nitric-oxide synthase phosphorylation at Ser1177 via an AMPK mediated pathway independent of PI3K-Akt

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Regulation of the mammalian heart function by nitric oxide.

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Analysis of neuronal nitric oxide synthase isoform expression and identification of human nNOS-mu

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Expression of inducible nitric oxide synthase in human heart failure

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Increased vascular endothelial growth factor expression but impaired vascular endothelial growth factor receptor signaling in the myocardium of type 2 diabetic patients with chronic coronary heart disease.

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Adiponectin stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signaling in endothelial cells

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Leptin effect on endothelial nitric oxide is mediated through Akt-endothelial nitric oxide synthase phosphorylation pathway.

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10.1016/J.YJMCC.2006.05.023

7 January 2021

Identifiers

DOI

1 reference

14 August 2017

1 reference

PubMed ID

16839566