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AKT phosphorylates NOS3. 10 / 401
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"Since eNOS phosphorylation by AKT could be direct or indirect, eNOS inhibitor (1 mM N G -Monomethyl arginine, CalBiochem) was also used in this experiment as a control to test actual eNOS dependency (Figure xref )."

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"Previously studies have demonstrated that Akt directly phosphorylates and activates eNOS in endothelial cells xref ."

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"Since eNOS phosphorylation by AKT could be direct or indirect, eNOS inhibitor (1 mM N G -Monomethyl arginine, CalBiochem) was also used in this experiment as a control to test actual eNOS dependency."

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"NO release occurs via PI3K-Akt dependent phosphorylation of eNOS with Src-kinase playing a proximal role in these changes."

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"LA induced eNOS phosphorylation is mediated by PI 3 -kinase and Akt pathway."

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"In addition, activation of Akt upregulated eNOS phosphorylation reduced ischemic oxidative stress."

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"The inability of VEGFR2 neutralization to affect flow induced Akt phosphorylation despite attenuating eNOS phosphorylation is consistent with the findings by Jo and colleagues, who demonstrated that shear stress stimulates phosphorylation of eNOS by an Akt independent mechanism [XREF_BIBR]."

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"Because Akt and eNOS are both localized in the bladder urothelium, phosphorylation of eNOS by Akt provides an attractive mechanism for rapid increases in urinary NO production."

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"Akt can also phosphorylate and activate eNOS, leading to enhanced NO production and vasodilation ( xref ; xref )."

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"Su and colleagues demonstrated that EPO is able to activate eNOS in endothelial cells by interacting with the βcR and causing Akt-dependent phosphorylation of eNOS ( xref )."
AKT phosphorylates NOS3 on S1177. 10 / 191
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"Akt directly phosphorylates eNOS at Ser 1177 resulting in increased eNOS activity and subsequent NO production."

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"This effect was apparently due to decreased eNOS interaction with its positive protein regulator HSP90 (but not increased interaction with caveolin-1), which decreases AKT activation and AKT mediated eNOS phosphorylation on Ser 1177, and reduces constitutive NOS activity."

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"Posttranslational regulation of eNOS involves multiple mechanisms, including the phosphorylation of eNOS by Akt at Ser1177."

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"The serine/threonine kinase Akt (protein kinase B) directly phosphorylates eNOS at Ser1177 (human eNOS) and Ser1179 (bovine eNOS), which increases eNOS activity several-fold [12,13,31] ."

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"Recent studies suggest that Akt is activated by phosphorylation via activated PI3K and phosphorylates eNOS on serine 1177, thereby activating this enzyme."

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"In contrast, other groups found no change of eNOS expression in aging, but observed decreased Akt dependent phosphorylation of eNOS at Ser1177 with increasing age as a potential explanation for an impaired endothelial dysfunction in the elderly [XREF_BIBR]."

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"Compared with 18 matched control, ET in 17 stable CAD patients significantly improved endothelial function, which may be closely related to shear-stress induced phosphorylation of eNOS at Ser 1177 residue by AKT [ xref ]."
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"And Dimmeler et al. demonstrated that Akt phosphorylated the Serine 1177 site of eNOS protein and that enhanced eNOS activity; they inhibited the PI3K/Akt pathway and that led to prevention of eNOS activation [ xref ], and Fulton et al. had similar findings [ xref ]."

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"In addition, inhibition of AKT activation by LY294002 (10 muM) inhibited eNOS Ser1177 phosphorylation by TRX (XREF_FIG)."

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"Akt directly phosphorylates eNOS at Ser 1177 resulting in increased eNOS activity and subsequent NO production."
AKT phosphorylates NOS3 on S1179. 10 / 53
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"At certain conditions, such as VEGF stimulation, AKT binds with Hsp90 (327-340aa) and phosphorylates eNOS Serine 1179[ xref , xref ]."

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"It has been reported that VEGFA activated PI3K and AKT directly phosphorylates eNOS Ser1179, leading to stimulating NO production, and endothelial migration, proliferation, and capillary like structure formation."

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"Akt can directly phosphorylate eNOS on serine 1179 (based on the bovine eNOS sequence and equivalent to human eNOS-serine 1177) and activate the enzyme, leading to NO production."

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"The serine/threonine protein kinase Akt can directly phosphorylate eNOS on serine 1179 and activate the enzyme, leading to NO production ( xref )."

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"The appropriate intracellular localization and distribution of eNOS in PM and Golgi apparatus is necessary for Akt (and agonist)-dependent eNOS phosphorylation on Ser-1179 and is impaired in the cytosolic G2A eNOS (Fulton et al., xref )."

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"Akt can phosphorylate eNOS on Ser 1179, and that phosphorylation enhances the enzyme’s ability to generate NO ( xref )."

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"It was reported previously that VEGF stimulated phosphorylation of eNOS Ser 1179 by Akt activation, which was required by the formation of the eNOS and Hsp90 heterocomplex [15,16]."

No evidence text available

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"The resulting increased Akt activation leads to enhanced eNOS phosphorylation at Ser 1177 and/or Ser 1179, thereby increasing the NO synthesizing activity."

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"Phosphorylation of eNOS at Ser 1179 is stimulated by Akt kinase or protein kinase A and results in increased enzyme activity leading to an enhanced NO production, thus allowing to couple extracellular[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
AKT phosphorylates NOS3 on serine. 5 / 5
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"Akt kinase, which can phosphorylate eNOS Ser (1177), was also decreased by hypoxia, regarding both total protein content and the phosphorylated (active) form."

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"Activated Akt phosphorylates eNOS at Ser , a major activation site (Dimmeler et al., 1999; Fulton et al., 1999; Michell et al., 1999), which is enhanced by its interaction with heat shock protein 90 (Fulton et al., 2001; Fontana et al., 2002; Venema, 2002)."

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"To conclude, the mouse pulmonary endothelial beta2-AR is coupled to a G (i/o)-Src kinase-PI3K and Akt pathway to promote eNOS phosphorylation at Ser (1177) leading to a NO dependent vasorelaxation."

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"Taken together, research published results show that the stimulation of PI3K and Akt by shear stress and VEGF elicits the serine phosphorylation of eNOS, and thereby enhances enzyme activity in a Ca ++ -independent manner XREF_BIBR."

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"Insulin plays a critical role in the maintenance of physiological endothelial function through its ability to stimulate NO release via a cascade that involves activation of the PI3K-Akt signaling and downstream serine phosphorylation of eNOS."
AKT phosphorylates NOS3 on S615. 4 / 4
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No evidence text available

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"Upon stimulation, Akt and protein kinase B (PKB) phosphorylates eNOS at Ser 1177 (1179) and possibly Ser 615 (617), and consequently activates eNOS [XREF_BIBR]."

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"Upon stimulation, Akt and protein kinase B (PKB) phosphorylates eNOS at Ser 1177 (1179) and possibly Ser 615 (617), and consequently activates eNOS [XREF_BIBR]."

"The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites"
Phosphorylated AKT leads to the phosphorylation of NOS3. 4 / 4
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"However, Dimmeler et al. [XREF_BIBR] previously observed via eNOS immunoprecipitation and phosphoamino acid analysis a significant increase in Akt phosphorylation following exposure to a shear stress magnitude of 5 dyn/cm 2 (i.e., 0.5 Pa), and determined Akt phosphorylation significantly increased eNOS phosphorylation."

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"The inhibition of AKT phosphorylation by treatment with the PI3-K inhibitor LY294002 reduced eNOS phosphorylation and NO production, leading to the suppression of angiogenesis in vitro."

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"Phosphorylated Akt stimulates phosphorylation of eNOS and NO production in cultured endothelial cells and endothelial progenitor cells (EPC) [22,23,24]."

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"These results suggested that AKT phosphorylation contributed to eNOS expression and phosphorylation."
AKT phosphorylates NOS3 at position 1177. 3 / 3
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"This activation of endothelial Akt has been shown to stimulate phosphorylation of eNOS at serine residue 1177, known to be an important regulatory mechanism leading to eNOS activation."

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"We tested the hypothesis that impaired nitric oxide (NO)-mediated, endothelium dependent dilation in aged soleus muscle feed arteries (SFA) is due to an age related decline in the potential for PI3-kinase (PI3K)/protein kinase B (Akt)-dependent phosphorylation of endothelial NO synthase (eNOS) on serine residue 1177 (p-eNOS (ser1177))."

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"Akt kinase, which can phosphorylate eNOS Ser (1177), was also decreased by hypoxia, regarding both total protein content and the phosphorylated (active) form."
Modified AKT leads to the phosphorylation of NOS3. 3 / 3
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"Suppression of Akt expression by siRNA had no effect on AMPK phosphorylation but attenuated CTRP9 induced eNOS phosphorylation and NO production."

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"In line with this, silencing of Akt protein expression largely blocked 2-ME-enhanced eNOS phosphorylation (XREF_FIG)."

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"Overexpression of dominant negative Akt inhibited the eNOS phosphorylation."
Phosphorylated AKT leads to the phosphorylation of NOS3 on serine. 2 / 2
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"102 Leptin induces Akt phosphorylation 103 and phosphorylated Akt then induces phosphorylation of the eNOS serine residue, which heightens its activity."

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"Akt phosphorylation is known to induce eNOS (Ser ) phosphorylation (Fulton, 2016), and was previously described by our research group as an important stimulus for maintaining basal NO production (Van Langen et al., 2012)."
Kinase-active AKT phosphorylates NOS3 on serine. 2 / 2
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"phosphorylation of eNOS by AKT leads to increase endothelial NO release in a ligand-dependent manner corticosteroids activate PI3K and AKT"

"Although AKT can phosphorylate several proteins4, we focused on BAD, FOXO, IKKa, TSC2 and eNOS, as the consequence of AKT phosphorylation of these proteins is not redundant with the functions of the oncoproteins expressed in cells used in the cellmixing assay of tumour maintenance5 (Supplementary Fig. 1)."
Phosphorylated AKT leads to the phosphorylation of NOS3 on S1177. 1 / 1
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"It is widely accepted that activating Akt phosphorylation stimulates eNOS phosphorylation at Ser1177 and increases endothelial NO production, which is involved in the mobilization of stem and progenitor cells [XREF_BIBR]."
AKT leads to the phosphorylation of NOS3 on threonine. 1 / 1
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"Decreased expression of endothelial NO synthase (eNOS) protein, decreased phosphorylation of eNOS by the serine threonine kinase AKT, the presence of inhibitory substances (e.g., asymmetric dimethylarginine, ADMA), and hyporesponsiveness to NO underlie this endothelial dysfunction [XREF_BIBR - XREF_BIBR]."
Modified AKT leads to the phosphorylation of NOS3 on S1179. 1 / 1
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"In contrast to the decrease in insulin induced eNOS Ser1179 phosphorylation that occurred with CRP in sham transfected cells, constitutively active Akt expression rescued the promotion of eNOS phosphorylation by insulin."
AKT phosphorylates NOS3 on S617. 1 / 1
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"In vascular endothelial cells, phosphorylation of p-eNOS-S 1179 by a variety of stimuli results in higher enzymatic activity ( McCabe et al., 2000 ), and phosphorylation of eNOS-Ser 617 by Akt modul[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
Kinase-active AKT leads to the phosphorylation of NOS3 on S617. 1 / 1
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"Shear stress, via G proteins (Gs), can activate several signal transduction pathways, including the phosphoinoside 3-kinase (PI3K) and adenylate cyclase (AC) pathways, leading to eNOS activation via phosphorylation of serine residues (S617 and S1179 for Akt, and S635 and S1179 for PKA), which promote eNOS activation."