Abstract:Endothelial NO synthase (eNOS) function is critically modulated by protein phosphorylation. In particular, phosphorylation of serine 1179 (S1179, bovine)/1177 (S1177, human and rat) by Akt has emerged as a central mechanism of eNOS regulation under both physiological and pathological conditions. Endoplasmic reticulum (ER) stress is a fundamental unfolded protein response occurred in various diseases. Whether and how ER stress affects eNOS phosphorylation is unknown. To address this issue, we induced ER stress … Show more
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