Redox status related activation of endoplasmic reticulum stress and apoptosis caused by 4-hydroxynonenal exposure in INS-1 cells

References

• Abarikwu SO, Pant AB, Farombi EO. (2012). 4-Hydroxynonenal induces mitochondrial-mediated apoptosis and oxidative stress in SH-SY5Y human neuronal cells. Basic Clin Pharmacol Toxicol 110:441–8
   PubMedGoogle Scholar
• Aitken RJ, Whiting S, De Iuliis GN, et al. (2012). Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase. J Biol Chem 287:33048–60
   PubMed Web of Science ®Google Scholar
• Anderson EJ, Katunga LA, Willis MS. (2012). Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart. Clin Exp Pharmacol Physiol 39:179–93
   PubMed Web of Science ®Google Scholar
• Bizzozero OA, Reyes S, Ziegler J, Smerjac S. (2007). Lipid peroxidation scavengers prevent the carbonylation of cytoskeletal brain proteins induced by glutathione depletion. Neurochem Res 32:2114–22
   PubMed Web of Science ®Google Scholar
• Bodur C, Kutuk O, Tezil T, Basaga H. (2012). Inactivation of Bcl-2 through IκB kinase (IKK)-dependent phosphorylation mediates apoptosis upon exposure to 4-hydroxynonenal (HNE). J Cell Physiol 227:3556–65
   Google Scholar
• Carini M, Aldini G, Facino RM. (2004). Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins. Mass Spectrom Rev 23:281–305
   PubMed Web of Science ®Google Scholar
• Choudhary S, Xiao T, Srivastava S, et al. (2005). Toxicity and detoxification of lipid-derived aldehydes in cultured retinal pigmented epithelial cells. Toxicol Appl Pharmacol 204:122–34
   PubMed Web of Science ®Google Scholar
• Doorn JA, Petersen DR. (2002). Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal. Chem Res Toxicol 15:1445–50
   PubMed Web of Science ®Google Scholar
• Esterbauer H, Schaur RJ, Zollner H. (1991). Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11:81–128
   PubMed Web of Science ®Google Scholar
• Guéraud F, Atalay M, Bresgen N, et al. (2010). Chemistry and biochemistry of lipid peroxidation products. Free Radic Res 44:1098–124
   PubMed Web of Science ®Google Scholar
• Haberzettl P, Hill BG. (2013). Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response. Redox Biol 1:56–64
   PubMed Web of Science ®Google Scholar
• Hortigón-Vinagre MP, Henao F. (2014). Apoptotic cell death in cultured cardiomyocytes following exposure to low concentrations of 4-hydroxy-2-nonenal. Cardiovasc Toxicol. [Epub ahead of print]. doi: 10.1007/s12012-014-9251-5
   Google Scholar
• Ishii T, Tatsuda E, Kumazawa S, et al. (2003). Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 12:474–80
   Google Scholar
• Iwawaki T, Oikawa D. (2013). The role of the unfolded protein response in diabetes mellitus. Semin Immunopathol 35:333--50
   Google Scholar
• Janjic D, Wollheim CB. (1992). Islet cell metabolism is reflected by the MTT (tetrazolium) colorimetric assay. Diabetologia 35:482–5
   PubMed Web of Science ®Google Scholar
• Jimbo A, Fujita E, Kouroku Y, et al. (2003). ER stress induces caspase-8 activation, stimulating cytochrome c release and caspase-9 activation. Exp Cell Res 283:156–66
   PubMed Web of Science ®Google Scholar
• Keith RJ, Haberzettl P, Vladykovskaya E, et al. (2009). Aldose reductase decreases endoplasmic reticulum stress in ischemic hearts. Chem Biol Interact 178:242–9
   PubMed Web of Science ®Google Scholar
• Lemaire K, Schuit F. (2012). Integrating insulin secretion and ER stress in pancreatic β-cells. Nat Cell Biol 14:979–81
   Google Scholar
• Logue SE, Cleary P, Saveljeva S, Samali A. (2013). New directions in ER stress-induced cell death. Apoptosis 18:537–46
   PubMed Web of Science ®Google Scholar
• LoPachin RM, Decaprio AP. (2005). Protein adduct formation as a molecular mechanism in neurotoxicity. Toxicol Sci 86:214–25
   PubMed Web of Science ®Google Scholar
• LoPachin RM, Gavin T, Petersen DR, Barber DS. (2009). Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: nucleophilic targets and adduct formation. Chem Res Toxicol 22:1499–508
   PubMed Web of Science ®Google Scholar
• Marciniak SJ, Yun CY, Oyadomari S, et al. (2004). CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev 18:3066–77
   PubMed Web of Science ®Google Scholar
• Masud A, Mohapatra A, Lakhani SA, et al. (2007). Endoplasmic reticulum stress-induced death of mouse embryonic fibroblasts requires the intrinsic pathway of apoptosis. J Biol Chem 282:14132–9
   PubMed Web of Science ®Google Scholar
• McCullough KD, Martindale JL, Klotz LO, et al. (2001). Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 21:1249–59
   PubMed Web of Science ®Google Scholar
• Moore KA, Hollien J. (2012). The unfolded protein response in secretory cell function. Annu Rev Genet 46:165–83
   PubMed Web of Science ®Google Scholar
• Niculescu LS, Sanda GM, Sima AV. (2013). HDL inhibit endoplasmic reticulum stress by stimulating apoE and CETP secretion from lipid-loaded macrophages. Biochem Biophys Res Commun 434:173–8
   Google Scholar
• Petersen DR, Doorn JA. (2004). Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radic Biol Med 37:937–45
   PubMed Web of Science ®Google Scholar
• Pillon NJ, Vella RE, Souleere L, et al. (2011). Structural and functional changes in human insulin induced by the lipid peroxidation byproducts 4-hydroxy-2-nonenal and 4-hydroxy-2-hexenal. Chem Res Toxicol 24:752–62
   PubMed Web of Science ®Google Scholar
• Roe MR, Xie H, Bandhakavi S, Griffin TJ. (2007). Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Anal Chem 79:3747–56
   PubMed Web of Science ®Google Scholar
• Ruskovska T, Bernlohr DA. (2013). Oxidative stress and protein carbonylation in adipose tissue – implications for insulin resistance and diabetes mellitus. J Proteomics 92:323–34
   PubMed Web of Science ®Google Scholar
• Schaur RJ. (2003). Basic aspects of the biochemical reactivity of 4-hydroxynonenal. Mol Aspects Med 24:149–59
   PubMedGoogle Scholar
• Siddiqui MA, Kumar V, Kashyap MP, et al. (2012). Short-term exposure of 4-hydroxynonenal induces mitochondria-mediated apoptosis in PC12 cells. Hum Exp Toxicol 31:336–45
   Google Scholar
• Spoerri L, Vella LJ, Pham CL, et al. (2012). The amyloid precursor protein copper binding domain histidine residues 149 and 151 mediate APP stability and metabolism. J Biol Chem 287:26840–53
   Google Scholar
• Sultana R, Perluigi M, Allan Butterfield D. (2012). Lipid peroxidation triggers neurodegeneration: a redox proteomics view into the Alzheimer disease brain. Free Radic Biol Med 62:157–69
   PubMed Web of Science ®Google Scholar
• Vladykovskaya E, Sithu SD, Haberzettl P, et al. (2012). Lipid peroxidation product 4-hydroxy-trans-2-nonenal causes endothelial activation by inducing endoplasmic reticulum stress. J Biol Chem 287:11398–409
   PubMed Web of Science ®Google Scholar
• Wu M, Yang S, Elliott MH, et al. (2012). Oxidative and endoplasmic reticulum stresses mediate apoptosis induced by modified LDL in human retinal Müller cells. Invest Ophthalmol Vis Sci 53:4595–604
   PubMed Web of Science ®Google Scholar
• Yadav UC, Ramana KV, Awasthi YC, Srivastava SK. (2008). Glutathione level regulates HNE-induced genotoxicity in human erythroleukemia cells. Toxicol Appl Pharmacol 227:257–64
   PubMed Web of Science ®Google Scholar