IndraLab
Statements
sparser
"The protein kinase Akt phosphorylates eNOS at serine 1177 in vivo , whereas other kinases such as members of the family AGC (protein kinase A, protein kinase G, protein kinase C) as well as AMP-activated kinase (AMPK) can phosphorylate eNOS at the same site in vitro and perhaps in vivo xref ."
reach
"It has been reported that eNOS phosphorylation by PI3K and Akt pathway is required for efficient NO production [XREF_BIBR, XREF_BIBR], after phosphorylated at Ser 473 by PI3K, Akt in turn phosphorylates eNOS at Ser 1177 and thereby increases eNOS activity, and finally enhances NO production."
reach
"It attenuated phosphorylation of IRS-1 at S307 and effectively ameliorated the tyrosine phosphorylation of IRS-1, which activated PI3K, subsequently activated PI3K phosphorylates and activated downstream target Akt which directly phosphorylated eNOS at Ser1177, leading to increased production of NO(Hwang et al., 2011)."
reach
"Although it is recognized that eNOS phosphorylation at Ser 1177 by the PI3K-Akt pathway plays a central role in the response to shear stress [XREF_BIBR, XREF_BIBR, XREF_BIBR], the contribution of eNOS translocation and the requirement of Ca 2+ in this physiological regulation are controversial."
reach
"With increasing disease severity, more malondialdehyde is bound to HDL particles and subsequent activation of protein kinase-betaII (PKC-betaII) results in pronounced phosphorylation of eNOS at its inhibitory site Thr 495 whereas the eNOS activating phosphorylation at Ser 1177, mediated by PI3K and Akt, is reduced."
sparser
"Further, we showed that preserved vascular redox state during aging decreases age-related hypertension by the following mechanisms: (i) maintenance of NO-mediated relaxing responses, (ii) preservation of functional NO release, (iii) activated AKT-dependent eNOS Ser1177 phosphorylation, (iv) decreased eNOS-dependent generation of O 2 •− in arteries of Trx-Tg mice because of preservation of eNOS function during aging, (v) abrogation of eNOS glutathionylation in the TAS of Trx-Tg mice, and (vi) decreased arterial stiffness with improved vascular flow."
"Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase a on serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no."
reach
"XREF_BIBR, XREF_BIBR Interestingly, whereas we now show that in response to CRP, Src activation leads to eNOS antagonism, the stimulation of eNOS by numerous agonists including HDL, estrogen and shear stress also entails Src activation, which preceeds PI3 kinase and Akt activation that promotes eNOS Ser1177 phosphorylation."
sparser
"Previous research showed that protein kinase B (AKT) and AMP‐activated protein kinase (AMPK) could phosphorylate eNOS at the Ser1177 site in response to various stimuli. xref , xref In our study, p‐eNOS (Ser1177) expression dramatically increased with zingerone treatment after AB surgery in vivo and after PE challenge in vitro, thus leading to increased production of NO."
sparser
"Reduced eNOS mRNA and protein expression, decreased phosphorylation of eNOS at Ser-1177 by serine-threonine protein kinase Akt, increased dissociation of functional eNOS dimers into nonfunctional monomers, and reduced NOS activity have been noticed in CC of rat or mouse models of T2DM, all of which would lead to decreased NO production. xref xref xref xref xref xref xref Consistent with previous reports, we also found an impaired Akt-eNOS pathway in CC of T2DM rats, including reduced eNOS expression at both transcription and protein level, decreased phosphorylation of Akt at Thr308 and phosphorylation of eNOS at Ser-1177, as well as subsequent reduced total NOS activity and NO production."
reach
"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))."
reach
"Furthermore, over-expression of dominant negative Akt [Akt (DN)] significantly reduced LA induced eNOS phosphorylation (XREF_FIG), whereas an AMPK inhibitor, dorsomorphin, reduced LA induced phosphorylation of AMPKalpha but not eNOS (XREF_FIG), strongly supporting that LA induced eNOS phosphorylation at Ser1177 is mediated by Akt."
reach
"In our palmitate induced model of oxidative stress, we demonstrated diminished NO production via reduced Akt dependent phosphorylation of eNOS at Ser 1177, which supports the findings of previous reports; however, the damaging effect of palmitate was attenuated when HUVECs were coincubated with EMPs."
reach
"Activation of VEGFR2 in endothelial cells (by VEGF binding) results in the Akt dependent phosphorylation of eNOS at Ser 1177 XREF_BIBR, XREF_BIBR, while VEGF treatment of BAECs resulted in the phosphorylation of eNOS at Ser 617 and Ser 635 (equivalent to human Ser 615 and Ser 633) XREF_BIBR."
sparser
"The PI3K/Akt/eNOS pathway plays an important role in the regulation of NO production and it has been shown that activated Akt phosphorylates eNOS at Ser1177, stimulates eNOS activity and induces NO release. xref , xref Furthermore, the activity of eNOS is influenced not only by the phosphorylation of eNOS‐Ser1177 but also by the phosphorylation of eNOS‐Thr495 and thus we also assessed the phosphorylation eNOS‐Thr495."
sparser
"It has been reported that eNOS phosphorylation by PI3K/Akt pathway is required for efficient NO production [ xref , xref ], after phosphorylated at Ser-473 by PI3K, Akt in turn phosphorylates eNOS at Ser-1177 and thereby increases eNOS activity, and finally enhances NO production."
reach
"This uncoupling effect is mediated primarily by Akt dependent phosphorylation of eNOS at serine 1177 [XREF_BIBR, XREF_BIBR], which alters the kinetics of electron transfer within the enzyme, leading to increased production of superoxide, particularly at low levels of calcium [XREF_BIBR]."