| | Oxidative folding in the endoplasmic reticulum: Towards a multiple oxidant hypothesis?Edited by Miguel De la Rosa Received 28 April 2010; received in revised form 20 May 2010; accepted 22 May 2010. published online 31 May 2010. Abstract Oxidative protein folding in the luminal compartment of the endoplasmic reticulum is thought to be mediated by a proteinaceous electron relay system composed by PDI and ER oxidoreductin 1 (Ero1), transferring electrons from the cysteinyl residues of substrate proteins to oxygen. However, recent observations revealed that Ero1 isoforms are dispensable. Endoplasmic reticulum is known as a generator and accumulator of low molecular weight oxidants; some of them have already been shown to promote oxidative folding. On the basis of these observations a new theory of oxidative folding is proposed where the oxidative power is provided by the stochastic contribution of prooxidants. Abbreviations: ER, endoplasmic reticulum, Ero1, ER oxidoreductin 1, PDI, protein disulfide isomerase, QSOX, quiescin sulfhydryl oxidase, ROS, reactive oxygen species, UPR, unfolded protein response, VKOR, vitamin K epoxide reductase a Università Vita-Salute, Division of Genetics and Cell Biology, San Raffaele Scientific Institute, Milano, Italy b Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, Siena, Italy c Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1444 Budapest, Hungary  Corresponding author at: Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1444 Budapest, P.O. Box 260, Hungary. Fax: +36 1 2662615.
PII: S0014-5793(10)00459-X doi:10.1016/j.febslet.2010.05.055 © 2010 Federation of European Biochemical Societies | |
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ABSTRACT
