Regulation of eNOS Enzyme Activity by Posttranslational Modification

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

Journal Name: Current Pharmaceutical Design

Volume 20 , Issue 22 , 2014

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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.

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Article Details

VOLUME: 20
ISSUE: 22
Year: 2014
Page: [3503 - 3513]
Pages: 11
DOI: 10.2174/13816128113196660745
Price: $58

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