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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 389, Issue 3

Issues

Regulation of proteasome-mediated protein degradation during oxidative stress and aging

Nicolle Breusing
  • 1Institute of Biological Chemistry and Nutrition, University of Hohenheim, Garbenstraße 28, D-70593 Stuttgart, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Tilman Grune
  • 2Institute of Biological Chemistry and Nutrition, University of Hohenheim, Garbenstraße 28, D-70593 Stuttgart, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-03-03 | DOI: https://doi.org/10.1515/BC.2008.029

Abstract

Protein degradation is a physiological process required to maintain cellular functions. There are distinct proteolytic systems for different physiological tasks under changing environmental and pathophysiological conditions. The proteasome is responsible for the removal of oxidatively damaged proteins in the cytosol and nucleus. It has been demonstrated that proteasomal degradation increases due to mild oxidation, whereas at higher oxidant levels proteasomal degradation decreases. Moreover, the proteasome itself is affected by oxidative stress to varying degrees. The ATP-stimulated 26S proteasome is sensitive to oxidative stress, whereas the 20S form seems to be resistant. Non-degradable protein aggregates and cross-linked proteins are able to bind to the proteasome, which makes the degradation of other misfolded and damaged proteins less efficient. Consequently, inhibition of the proteasome has dramatic effects on cellular aging processes and cell viability. It seems likely that during oxidative stress cells are able to keep the nuclear protein pool free of damage, while cytosolic proteins may accumulate. This is because of the high proteasome content in the nucleus, which protects the nucleus from the formation and accumulation of non-degradable proteins. In this review we highlight the regulation of the proteasome during oxidative stress and aging.

Keywords: aging; oxidative stress; proteasome; protein degradation; protein oxidation

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Corresponding author


Published Online: 2008-03-03

Published in Print: 2008-03-01


Citation Information: Biological Chemistry, Volume 389, Issue 3, Pages 203–209, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2008.029.

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