Detection of oxidative damage in response to protein misfolding in the endoplasmic reticulum.

作者: Guy Landau , Vamsi K. Kodali , Jyoti D. Malhotra , Randal J. Kaufman

DOI: 10.1016/B978-0-12-405883-5.00014-4

关键词: Unfolded protein responseGlutathioneProtein CarbonylationEndoplasmic reticulumOxidative stressMitochondrionCell biologyProtein disulfide-isomeraseChemistryProtein folding

摘要: Disulfide bond formation in the endoplasmic reticulum (ER) requires sequential transfer of electrons from thiol residues to protein disulfide isomerase and ER oxidase 1, with final reduction molecular oxygen form hydrogen peroxide. Conditions that perturb correct folding lead accumulation misfolded proteins lumen, which induce stress oxidative stress. Oxidative damage cellular macromolecules is a common marker aging various pathological conditions including diabetes, cancer, neurodegenerative disease. As accumulating evidence suggests tight connection between stress, analysis appropriate markers becomes particularly important. Here, we describe methods analyze associated

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