Copyright © 2007, European Society of Cardiology
Life history of eNOS: Partners and pathways
aDepartment of Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, MA, United States
bDepartment of Medicine, Cardiovascular Division, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA, 02115, United States
* Corresponding author. Tel.: +1 617 732 7376; fax: +1 617 732 5132. tmichel{at}rics.bwh.harvard.edu
The complex regulation of eNOS (endothelial nitric oxide synthase) in cardiovascular physiology occurs at multiple stages. eNOS mRNA levels are controlled both at the transcriptional and post-transcriptional phases, and epigenetic mechanisms appear to modulate tissue-specific eNOS expression. The eNOS enzyme reversibly associates with a diverse family of protein partners that regulate eNOS sub-cellular localization, catalytic function, and biological activity. eNOS enzyme activity and sub-cellular localization are intimately controlled by post-translational modifications including phosphorylation, nitrosylation, and acylation. The multiple extra-cellular stimuli affecting eNOS function coordinate their efforts through these key modifications to dynamically control eNOS and NO bioactivity in the vessel wall. This review will focus on the biochemical partners and perturbations of the eNOS protein as this vital enzyme undergoes modulation by diverse signal transduction pathways in the vascular endothelium.
KEYWORDS Nitric oxide synthase; Post-translational modifications; Sub-cellular targeting; Protein phosphorylation; Protein acylation; S-nitrosylation
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