期刊
CARDIOVASCULAR RESEARCH
卷 75, 期 2, 页码 247-260出版社
OXFORD UNIV PRESS
DOI: 10.1016/j.cardiores.2007.03.023
关键词
nitric oxide synthase; post-translational modifications; sub-cellular targeting; protein phosphorylation; protein acylation; S-nitrosylation
资金
- NHLBI NIH HHS [P01 HL048743, R01 HL046457, P01 HL048743-16, R01 HL046457-17] Funding Source: Medline
- NIGMS NIH HHS [R01 GM036259, R01 GM036259-24] Funding Source: Medline
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. (c) 2007 European Society of Cardiology. Published by Elsevier B.V. All rights reserved.
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