Generic placeholder image

Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Regulation of eNOS Enzyme Activity by Posttranslational Modification

Author(s): Elke H. Heiss and Verena M. Dirsch

Volume 20, Issue 22, 2014

Page: [3503 - 3513] Pages: 11

DOI: 10.2174/13816128113196660745

Price: $65

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.

Keywords: Endothelial NO synthase, regulation of enzyme activity, posttranslational modification.


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy