Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051611 | FEBS Letters | 2007 | 7 Pages |
Abstract
The effect of tyrosine nitration on mammalian GS activity and stability was studied in vitro. Peroxynitrite at a concentration of 5 μmol/l produced tyrosine nitration and inactivation of GS, whereas 50 μmol/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 μmol/l). Further, a putative “denitrase” activity restored the activity of peroxynitrite (5 μmol/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.
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Authors
Boris Görg, Natalia Qvartskhava, Peter Voss, Tilman Grune, Dieter Häussinger, Freimut Schliess,