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AKT phosphorylates NOS3 on serine. 15 / 16
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"The impaired eNOS activities in cirrhosis are caused by decreased protein expression and by decreased posttranslational modifications such as eNOS phosphorylation by the serine-threonine kinase PKB/Ak[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As the eNOS upstream effectors, Akt or ERK1/2 can phosphorylate eNOS at Ser thus resulting in NO release [59]."
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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."
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"As we know, NO production involves a rapid, PI3-kinase-dependent activation of Akt and consequent serine phosphorylation of eNOS ( Haynes et al. 2000 )."
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"Phosphorylation of serine residue (Ser1177) of eNOS by Akt is associated with increased enzyme activity ( Dimmeler et al., 1999; Fulton et al., 1999 )."
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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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"Importantly, Akt can directly phosphorylate eNOS at a serine phosphorylation site, resulting in the enhancement of eNOS enzymatic activity and altered sensitivity of the enzyme to Ca (14)."
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"In endothelial cells, two ways of eNOS activation are known: a dissociation of the enzyme from the cellular membrane into the cytosol (i.e., translocation) ( Michel et al., 1997 ) and an Akt kinase-de[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The presence of a similar signalling pathway could be hypothesized even in endothelial cells.In summary, we have found a new insulin-sensitizing action of glimepiride on cultured human endothelial cel[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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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"E2 replacement in ovariectomized fructose-fed rats caused a reversion of the diet effect on eNOS serine phosphorylation, possibly mediated by Akt ( Koricanac et al., 2011 ), but mostly had no effect o[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We previously observed that exposure of HAEC to OA promoted signaling by the PI3K/Akt pathway to increase eNOS phosphorylation at Ser , relative to PA, linoleic acid, and stearic acid [25]."
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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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"Phosphorylation of serine residue (Ser1177) of eNOS by Akt is associated with increased enzyme activity ( Dimmeler et al., 1999; Fulton et al., 1999 )."
20713148
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"Phosphorylation of serine residue (Ser1177) of eNOS by Akt is associated with increased enzyme activity ( Dimmeler et al., 1999; Fulton et al., 1999 )."
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