Neil Bulleid

Institute:Institute of Molecular Cell and Systems Biology, University of Glasgow, UK
Title:Regulating the Level of Intra-cellular Hydrogen Peroxide: the Role of Peroxiredoxin 4
Abstract:["Hydrogen peroxide can act as a signalling molecule affecting the cell cycle as well as contributing towards the oxidative stress response. The primary target of this molecule is oxidation sensitive cysteine residues in proteins such as protein tyrosine phosphatases. The cell has robust mechanisms to remove hydrogen peroxide that need to be regulated for hydrogen peroxide to react with and modify protein thiols. In particular the family of peroxiredoxins are capable of the rapid removal of even trace amounts of this molecule. It has been suggested that the inactivation of peroxiredoxins by hyperoxidation may allow hydrogen peroxide levels to increase in cells and thereby modify critical thiol groups in proteins. We have been studying how the hydrogen peroxide produced during disulfide formation in the endoplasmic reticulum is metabolised and have shown that ER-resident peroxiredoxin 4 can not only remove hydrogen peroxide but also can contribute to de novo disulfide formation. Our recent results indicate that peroxiredoxin 4 is a robust enzyme that is protected from over modification by the lack of an efficient recycling system in the ER."]
Host:Ineke Braakman