Aug 5, 2003

Reduction of the endoplasmic reticulum accompanies the oxidative damage of diabetes mellitus

BioFactors
Gábor NardaiP Csermely

Abstract

The endoplasmic reticulum (ER), similary to other subcompartments of the eukaryotic cell possesses a relatively oxidizing environment. The special milieu of ER lumen is important for many ER-specific processes (redox protein folding, glycoprotein synthesis, quality control of secreted proteins, antigen presentation, etc.). Despite of the vital importance of redox regulation in the ER, we have a surprisingly fragmented knowledge about the mechanisms responsible for the ER redox balance. Moreover, new observations on disulfide bridge synthesis and on glutathione functions urge us to revise our recent theories based on many indirect and in vitro results. We have also very little information about the effects of different pathological conditions on the thiol metabolism and redox folding in the ER. Examining the role of molecular chaperones in the cellular pathology of diabetes mellitus we found that the ER redox environment shifted to a more reducing state, which was followed by changes of the thiol metabolism and structural-functional changes of the protein machinery involved in the redox folding process in diabetes. The possible consequences of these unexpected changes are also discussed.

Mentioned in this Paper

Oxidative Stress
Sulfhydryl Compounds
Oxidation-Reduction
Protein Folding, Globular
Cell Surface Proteins
Diabetes Mellitus
Protein Disulfide Isomerase
Endoplasmic Reticulum
Disulfides

About this Paper

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