Reversible Inhibition of Mammalian Glutamine Synthetase by Tyrosine Nitration.
From: Clinic for Gastroenterology, Hepatology and Infectiology, Heinrich-Heine-University Düsseldorf, Moorenstrasse 5, D-40225 Dusseldorf, Germany.
FEBS letters
- Publish Date: Jan 2007
- ISSN: 0014-5793
- Volume: 581
- Issue: 1
- Pages: 84-90
- Medium: Print
- Language: English
- Citation (JAMA): Görg Boris, Qvartskhava Natalia, Voss Peter, et al. Reversible Inhibition of Mammalian Glutamine Synthetase by Tyrosine Nitration.. FEBS Lett. Jan 2007;581:84-90
Abstract
The effect of tyrosine nitration on mammalian GS activity and stability was studied in vitro. Peroxynitrite at a concentration of 5 micro mol/l produced tyrosine nitration and inactivation of GS, whereas 50 micro mol/l peroxynitrite additionally increased S-nitrosylation and carbonylation and degradation of GS by the 20S proteasome. (-)Epicatechin completely prevented both, tyrosine nitration and inactivation of GS by peroxynitrite (5 micro mol/l). Further, a putative “denitrase” activity restored the activity of peroxynitrite (5 micro mol/l)-treated GS. The data point to a potential regulation of GS activity by a reversible tyrosine nitration. High levels of oxidative stress may irreversibly damage and predispose the enzyme to proteasomal degradation.
Mesh Headings (Keywords): Animals, Enzyme Activation, Glutamate-Ammonia Ligase, Nitrates, Oxidative Stress, Peroxynitrous Acid, Proteasome Endopeptidase Complex, Protein Processing, Post-Translational, Sheep, Tyrosine
Check for Full Text / PubMed Unique Identifier (PMID): 17174954
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