Jump to ContentJump to Main Navigation

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year

VolumeIssuePage

Issues

Modifications of Glyceraldehyde-3-Phosphate Dehydrogenase Induced by Increasing Concentrations of Peroxynitrite: Early Recognition by 20S Proteasome

D.P. Buchczyk / T. Grune / H. Sies / L.-O. Klotz

Citation Information: Biological Chemistry. Volume 384, Issue 2, Pages 237–241, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2003.026, June 2005

Publication History

Published Online:
2005-06-01

Abstract

Peroxynitrite, a potent oxidizing and nitrating species, induces covalent modifications of biomolecules in a number of pathological conditions. In previous studies with S. cerevisiae, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was identified as being especially susceptible to nitration by peroxynitrite. The activity of this enzyme was strongly inhibited by low doses of peroxynitrite in yeast and in cultured rat astrocytes. Here, the sequence of modifications of isolated mammalian GAPDH induced by increasing concentrations of peroxynitrite is demonstrated to be as follows: (i) oxidation, leading to inactivation and to enhanced susceptibility of GAPDH for proteasomal degradation, (ii) oligomer formation, and (iii) nitration. In our study the susceptibility for degradation by isolated 20S proteasome was by far the most sensitive parameter for peroxynitrite-induced damage to GAPDH, implying that this might also occur under pathological conditions where peroxynitrite is generated at low concentrations in vivo.

Comments (0)

Please log in or register to comment.
Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.