title: Stress on redox.
abstract: Redox imbalance in the endoplasmic reticulum lumen is the most frequent cause of endoplasmic reticulum stress and consequent apoptosis. The mechanism involves the impairment of oxidative protein folding, the accumulation of unfolded/misfolded proteins in the lumen and the initiation of the unfolded protein response. The participation of several redox systems (glutathione, ascorbate, FAD, tocopherol, vitamin K) has been demonstrated in the process. Recent findings have attracted attention to the possible mechanistic role of luminal pyridine nucleotides in the endoplasmic reticulum stress. The aim of this minireview is to summarize the luminal redox systems and the redox sensing mechanisms of the endoplasmic reticulum.
authors.affiliation: Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1444 Budapest, POB 260, Hungary. banhegyi@puskin.sote.hu
authors.forename: Gábor
authors.initials: G
authors.lastname: Bánhegyi
authors.forename: Angelo
authors.initials: A
authors.lastname: Benedetti
authors.forename: Miklós
authors.initials: M
authors.lastname: Csala
authors.forename: József
authors.initials: J
authors.lastname: Mandl
mesh_terms: D000818:Animals; D001692:Biological Transport; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D051379:Mice; D018832:Molecular Chaperones / Q000378:metabolism; D010084:Oxidation-Reduction; D013312:Stress, Physiological / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism; D014815:Vitamins / Q000378:metabolism*
chemical_list: D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D013438:Sulfhydryl Compounds; D014815:Vitamins