| Literature DB >> 24180389 |
Elke H Heiss, Verena M Dirsch1.
Abstract
The regulation of endothelial NO synthase (eNOS) employs multiple different cellular control mechanisms impinging on level and activity of the enzyme. This review aims at summarizing the current knowledge on the posttranslational modifications of eNOS, including acylation, nitrosylation, phosphorylation, acetylation, glycosylation and glutathionylation. Sites, mediators and impact on enzyme localization and activity of the single modifications will be discussed. Moreover, interdependence, cooperativity and competition between the different posttranslational modifications will be elaborated with special emphasis on the susceptibility of eNOS to metabolic cues.Entities:
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Year: 2014 PMID: 24180389 PMCID: PMC4401012 DOI: 10.2174/13816128113196660745
Source DB: PubMed Journal: Curr Pharm Des ISSN: 1381-6128 Impact factor: 3.116