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 response 、 Glutathione 、 Protein Carbonylation 、 Endoplasmic reticulum 、 Oxidative stress 、 Mitochondrion 、 Cell biology 、 Protein disulfide-isomerase 、 Chemistry 、 Protein 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