Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation

Tavender, T.J. and Bulleid, N.J. (2010) Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation. Journal of Cell Science, 123(15), pp. 2672-2679. (doi:10.1242/jcs.067843)

Full text not currently available from Enlighten.

Publisher's URL: http://dx.doi.org/10.1242/jcs.067843

Abstract

Disulphide formation within the endoplasmic reticulum (ER) requires the activity of the ER oxidase Ero1, and as a consequence, generates hydrogen peroxide. The production of hydrogen peroxide is thought to lead to oxidative stress that ultimately results in apoptosis. Here, we show that mammalian peroxiredoxin IV (PrxIV) metabolises hydrogen peroxide produced by Ero1. We demonstrate that the presence of PrxIV within the ER provides a cytoprotective effect against stresses known to enhance Ero1 activity and perturb ER redox balance. Increased Ero1 activity and production of hydrogen peroxide led to preferential hyperoxidation of PrxIV relative to peroxiredoxins in other cellular compartments. The hyperoxidation was increased by the upregulation of Ero1 and by the expression of a hyperactive Ero1. These findings provide the first evidence for an enzymatic mechanism that facilitates peroxide removal from the ER, and show that the oxidation status of PrxIV acts as a marker for ER oxidative stress.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Tavender, Dr Timothy and Bulleid, Professor Neil
Authors: Tavender, T.J., and Bulleid, N.J.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Journal of Cell Science
ISSN:0021-9533

University Staff: Request a correction | Enlighten Editors: Update this record