title: Detection of oxidative damage in response to protein misfolding in the endoplasmic reticulum.
abstract: Disulfide bond formation in the endoplasmic reticulum (ER) requires the sequential transfer of electrons from thiol residues to protein disulfide isomerase and ER oxidase 1, with the final reduction of molecular oxygen to form hydrogen peroxide. Conditions that perturb correct protein folding lead to accumulation of misfolded proteins in the ER lumen, which induce ER stress and oxidative stress. Oxidative damage of cellular macromolecules is a common marker of aging and various pathological conditions including diabetes, cancer, and neurodegenerative disease. As accumulating evidence suggests a tight connection between the ER stress and oxidative stress, analysis of appropriate markers becomes particularly important. Here, we describe methods to analyze markers of oxidative damage associated with ER stress.
authors.affiliation: Center for Neuroscience, Aging, and Stem Cell Research, Sanford-Burnham Medical Research Institute, La Jolla, California, USA.
authors.forename: Guy
authors.initials: G
authors.lastname: Landau
authors.forename: Vamsi K
authors.initials: VK
authors.lastname: Kodali
authors.forename: Jyoti D
authors.initials: JD
authors.lastname: Malhotra
authors.forename: Randal J
authors.initials: RJ
authors.lastname: Kaufman
mesh_terms: D000818:Animals; D001671:Biochemistry / Q000379:methods; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D015227:Lipid Peroxidation; D008928:Mitochondria / Q000378:metabolism; D018384:Oxidative Stress; D050050:Protein Carbonylation; D056811:Unfolded Protein Response
chemical_list: D006861:Hydrogen Peroxide; D005978:Glutathione