Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase.

作者: Célio X.C. Santos , Leonardo Y. Tanaka , João Wosniak , Francisco R.M. Laurindo

DOI: 10.1089/ARS.2009.2625

关键词: Unfolded protein responseProtein foldingCell biologyEndoplasmic reticulumMitochondrial electron transportBiologyProtein disulfide-isomeraseNADPH oxidaseEnzymeOxidative stress

摘要: Abstract Cellular mechanisms governing redox homeostasis likely involve their integration with other stresses. Endoplasmic reticulum (ER) stress triggers complex adaptive or proapoptotic signaling defined as the unfolded protein response (UPR), involved in several pathophysiological processes. Since folding is highly redox-dependent, convergence between ER and oxidative has attracted interest. Evidence suggests that ROS production are not only coincidental to stress, but integral UPR components, being triggered by distinct types of stressors contributing support proapoptotic, well proadaptive signaling. Thus, generation can be upstream downstream targets may display a UPR-specific plus nonspecific component. Enzymatic during include: (a) Multiple thiol–disulfide exchanges involving oxidoreductases including flavooxidase Ero1 disulfide isomerase (PDI); (b) Mitochondrial ele...

参考文章(134)
Francisco R.M. Laurindo, Denise C. Fernandes, Célio X.C. Santos, Assessment of superoxide production and NADPH oxidase activity by HPLC analysis of dihydroethidium oxidation products. Methods in Enzymology. ,vol. 441, pp. 237- 260 ,(2008) , 10.1016/S0076-6879(08)01213-5
P. Maattanen, G. Kozlov, K. Gehring, D.Y. Thomas, ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations. Biochemistry and Cell Biology. ,vol. 84, pp. 881- 889 ,(2006) , 10.1139/O06-186
John W. Cuozzo, Chris A. Kaiser, Competition between glutathione and protein thiols for disulphide-bond formation. Nature Cell Biology. ,vol. 1, pp. 130- 135 ,(1999) , 10.1038/11047
Agnes Görlach, Peter Klappa, Dr. Thomas Kietzmann, The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxidants & Redox Signaling. ,vol. 8, pp. 1391- 1418 ,(2006) , 10.1089/ARS.2006.8.1391
Shinji Tanaka, Takashi Uehara, Yasuyuki Nomura, Up-regulation of Protein-disulfide Isomerase in Response to Hypoxia/Brain Ischemia and Its Protective Effect against Apoptotic Cell Death Journal of Biological Chemistry. ,vol. 275, pp. 10388- 10393 ,(2000) , 10.1074/JBC.275.14.10388
V. E. KAGAN, Y. Y. TYURINA, Recycling and Redox Cycling of Phenolic Antioxidants Annals of the New York Academy of Sciences. ,vol. 854, pp. 425- 434 ,(1998) , 10.1111/J.1749-6632.1998.TB09921.X
Kendra D. Martyn, Linda M. Frederick, Katharina von Loehneysen, Mary C. Dinauer, Ulla G. Knaus, Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases Cellular Signalling. ,vol. 18, pp. 69- 82 ,(2006) , 10.1016/J.CELLSIG.2005.03.023
Kajorn Kitiphongspattana, Tarannum A. Khan, Katrin Ishii-Schrade, Michael W. Roe, Louis H. Philipson, H. Rex Gaskins, Protective role for nitric oxide during the endoplasmic reticulum stress response in pancreatic β-cells American Journal of Physiology-endocrinology and Metabolism. ,vol. 292, ,(2007) , 10.1152/AJPENDO.00620.2006
Weiming Xu, Lizhi Liu, Ian G. Charles, Salvador Moncada, Nitric oxide induces coupling of mitochondrial signalling with the endoplasmic reticulum stress response. Nature Cell Biology. ,vol. 6, pp. 1129- 1134 ,(2004) , 10.1038/NCB1188
James C A Bardwell, The dance of disulfide formation Nature Structural & Molecular Biology. ,vol. 11, pp. 582- 583 ,(2004) , 10.1038/NSMB0704-582