메뉴 건너뛰기




Volumn 24, Issue 5, 2014, Pages 362-367

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

Author keywords

CCAAT enhancer binding protein; Glutathione; HNE histidine adduct

Indexed keywords

4 HYDROXYNONENAL; CASPASE 3; CASPASE 9; GLUTATHIONE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HISTIDINE; PROTEIN IRE1; PROTEIN IRE1 ALPHA; PROTEIN KINASE; PROTEIN KINASE LIKE ENDOPLASMIC RETICULUM KINASE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; 4-HYDROXY-2-NONENAL; ALDEHYDE; CASPASE;

EID: 84900812124     PISSN: 15376516     EISSN: 15376524     Source Type: Journal    
DOI: 10.3109/15376516.2014.914617     Document Type: Article
Times cited : (6)

References (37)
  • 1
    • 84859855659 scopus 로고    scopus 로고
    • 4-Hydroxynonenal induces mitochondrial-mediated apoptosis and oxidative stress in SH-SY5Y human neuronal cells
    • 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.
    • (2012) Basic Clin Pharmacol Toxicol , vol.110 , pp. 441-448
    • Abarikwu, S.O.1    Pant, A.B.2    Farombi, E.O.3
  • 2
    • 84866529392 scopus 로고    scopus 로고
    • Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase
    • 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.
    • (2012) J Biol Chem , vol.287 , pp. 33048-33060
    • Aitken, R.J.1    Whiting, S.2    De Iuliis, G.N.3
  • 3
    • 84856464242 scopus 로고    scopus 로고
    • Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart
    • 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.
    • (2012) Clin Exp Pharmacol Physiol , vol.39 , pp. 179-193
    • Anderson, E.J.1    Katunga, L.A.2    Willis, M.S.3
  • 4
    • 35848956857 scopus 로고    scopus 로고
    • Lipid peroxidation scavengers prevent the carbonylation of cytoskeletal brain proteins induced by glutathione depletion
    • DOI 10.1007/s11064-007-9377-y
    • 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. (Pubitemid 350059855)
    • (2007) Neurochemical Research , vol.32 , Issue.12 , pp. 2114-2122
    • Bizzozero, O.A.1    Reyes, S.2    Ziegler, J.3    Smerjac, S.4
  • 5
    • 84864081330 scopus 로고    scopus 로고
    • Inactivation of Bcl-2 through IkB kinase (IKK)-dependent phosphorylation mediates apoptosis upon exposure to 4-hydroxynonenal (HNE)
    • Bodur C, Kutuk O, Tezil T, Basaga H. (2012). Inactivation of Bcl-2 through IkB kinase (IKK)-dependent phosphorylation mediates apoptosis upon exposure to 4-hydroxynonenal (HNE). J Cell Physiol 227:3556-65.
    • (2012) J Cell Physiol , vol.227 , pp. 3556-3565
    • Bodur, C.1    Kutuk, O.2    Tezil, T.3    Basaga, H.4
  • 6
    • 3042596594 scopus 로고    scopus 로고
    • Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins
    • 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.
    • (2004) Mass Spectrom Rev , vol.23 , pp. 281-305
    • Carini, M.1    Aldini, G.2    Facino, R.M.3
  • 8
    • 0036852609 scopus 로고    scopus 로고
    • Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal
    • DOI 10.1021/tx025590o
    • 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. (Pubitemid 35364906)
    • (2002) Chemical Research in Toxicology , vol.15 , Issue.11 , pp. 1445-1450
    • Doorn, J.A.1    Petersen, D.R.2
  • 9
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H, Schaur RJ, Zollner H. (1991). Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11:81-128. (Pubitemid 121003917)
    • (1991) Free Radical Biology and Medicine , vol.11 , Issue.1 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 10
    • 77956569706 scopus 로고    scopus 로고
    • Chemistry and biochemistry of lipid peroxidation products
    • Guéraud F, Atalay M, Bresgen N, et al. (2010). Chemistry and biochemistry of lipid peroxidation products. Free Radic Res 44:1098-124.
    • (2010) Free Radic Res , vol.44 , pp. 1098-1124
    • Guéraud, F.1    Atalay, M.2    Bresgen, N.3
  • 11
    • 84878772042 scopus 로고    scopus 로고
    • Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response
    • 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.
    • (2013) Redox Biol , vol.1 , pp. 56-64
    • Haberzettl, P.1    Hill, B.G.2
  • 12
    • 85027920749 scopus 로고    scopus 로고
    • Apoptotic cell death in cultured cardiomyocytes following exposure to low concentrations of 4-hydroxy-2-nonenal
    • Epub ahead of print, doi: 10.1007/s12012-014-9251-5
    • 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.
    • (2014) Cardiovasc Toxicol
    • Hortigón-Vinagre, M.P.1    Henao, F.2
  • 13
    • 0037379388 scopus 로고    scopus 로고
    • Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2- nonenal: Identification of modification sites in glyceraldehyde-3- phosphate dehydrogenase
    • 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.
    • (2003) Biochemistry , vol.12 , pp. 474-480
    • Ishii, T.1    Tatsuda, E.2    Kumazawa, S.3
  • 14
    • 84881475112 scopus 로고    scopus 로고
    • The role of the unfolded protein response in diabetes mellitus
    • Iwawaki T, Oikawa D. (2013). The role of the unfolded protein response in diabetes mellitus. Semin Immunopathol 35:333-50.
    • (2013) Semin Immunopathol , vol.35 , pp. 333-350
    • Iwawaki, T.1    Oikawa, D.2
  • 15
    • 0026581414 scopus 로고
    • Islet cell metabolism is reflected by the MTT (tetrazolium) colorimetric assay
    • Janjic D, Wollheim CB. (1992). Islet cell metabolism is reflected by the MTT (tetrazolium) colorimetric assay. Diabetologia 35: 482-5.
    • (1992) Diabetologia , vol.35 , pp. 482-485
    • Janjic, D.1    Wollheim, C.B.2
  • 17
    • 59049098116 scopus 로고    scopus 로고
    • Aldose reductase decreases endoplasmic reticulum stress in ischemic hearts
    • Keith RJ, Haberzettl P, Vladykovskaya E, et al. (2009). Aldose reductase decreases endoplasmic reticulum stress in ischemic hearts. Chem Biol Interact 178:242-9.
    • (2009) Chem Biol Interact , vol.178 , pp. 242-249
    • Keith, R.J.1    Haberzettl, P.2    Vladykovskaya, E.3
  • 18
    • 84867045280 scopus 로고    scopus 로고
    • Integrating insulin secretion and ER stress in pancreatic b-cells
    • Lemaire K, Schuit F. (2012). Integrating insulin secretion and ER stress in pancreatic b-cells. Nat Cell Biol 14:979-81.
    • (2012) Nat Cell Biol , vol.14 , pp. 979-981
    • Lemaire, K.1    Schuit, F.2
  • 19
  • 20
    • 26444512720 scopus 로고    scopus 로고
    • Protein adduct formation as a molecular mechanism in neurotoxicity
    • LoPachin RM, Decaprio AP. (2005). Protein adduct formation as a molecular mechanism in neurotoxicity. Toxicol Sci 86:214-25.
    • (2005) Toxicol Sci , vol.86 , pp. 214-225
    • Lopachin, R.M.1    Decaprio, A.P.2
  • 21
    • 70349492687 scopus 로고    scopus 로고
    • Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: Nucleophilic targets and adduct formation
    • 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.
    • (2009) Chem Res Toxicol , vol.22 , pp. 1499-1508
    • Lopachin, R.M.1    Gavin, T.2    Petersen, D.R.3    Barber, D.S.4
  • 23
    • 34347218245 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced death of mouse embryonic fibroblasts requires the intrinsic pathway of apoptosis
    • DOI 10.1074/jbc.M700077200
    • 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. (Pubitemid 47100471)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14132-14139
    • Masud, A.1    Mohapatra, A.2    Lakhani, S.A.3    Ferrandino, A.4    Hakem, R.5    Flavell, R.A.6
  • 24
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state
    • DOI 10.1128/MCB.21.4.1249-1259.2001
    • 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. (Pubitemid 32114973)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.-O.3    Aw, T.-Y.4    Holbrook, N.J.5
  • 25
    • 84870166429 scopus 로고    scopus 로고
    • The unfolded protein response in secretory cell function
    • Moore KA, Hollien J. (2012). The unfolded protein response in secretory cell function. Annu Rev Genet 46:165-83.
    • (2012) Annu Rev Genet , vol.46 , pp. 165-183
    • Moore, K.A.1    Hollien, J.2
  • 26
    • 84876789350 scopus 로고    scopus 로고
    • HDL inhibit endoplasmic reticulum stress by stimulating apoE and CETP secretion from lipidloaded macrophages
    • Niculescu LS, Sanda GM, Sima AV. (2013). HDL inhibit endoplasmic reticulum stress by stimulating apoE and CETP secretion from lipidloaded macrophages. Biochem Biophys Res Commun 434:173-8.
    • (2013) Biochem Biophys Res Commun , vol.434 , pp. 173-178
    • Niculescu, L.S.1    Sanda, G.M.2    Sima, A.V.3
  • 27
    • 4444314070 scopus 로고    scopus 로고
    • Reactions of 4-hydroxynonenal with proteins and cellular targets
    • DOI 10.1016/j.freeradbiomed.2004.06.012, PII S0891584904004666
    • Petersen DR, Doorn JA. (2004). Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radic Biol Med 37:937-45. (Pubitemid 39164576)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.7 , pp. 937-945
    • Petersen, D.R.1    Doorn, J.A.2
  • 28
    • 79956155956 scopus 로고    scopus 로고
    • Structural and functional changes in human insulin induced by the lipid peroxidation byproducts 4-hydroxy-2-nonenal and 4-hydroxy-2-hexenal
    • 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.
    • (2011) Chem Res Toxicol , vol.24 , pp. 752-762
    • Pillon, N.J.1    Vella, R.E.2    Souleere, L.3
  • 29
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • DOI 10.1021/ac0617971
    • 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. (Pubitemid 46799071)
    • (2007) Analytical Chemistry , vol.79 , Issue.10 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 30
    • 84886945867 scopus 로고    scopus 로고
    • Oxidative stress and protein carbonylation in adipose tissue - Implications for insulin resistance and diabetes mellitus
    • 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.
    • (2013) J Proteomics , vol.92 , pp. 323-334
    • Ruskovska, T.1    Bernlohr, D.A.2
  • 31
    • 0043172509 scopus 로고    scopus 로고
    • Basic aspects of the biochemical reactivity of 4-hydroxynonenal
    • DOI 10.1016/S0098-2997(03)00009-8
    • Schaur RJ. (2003). Basic aspects of the biochemical reactivity of 4-hydroxynonenal. Mol Aspects Med 24:149-59. (Pubitemid 36945015)
    • (2003) Molecular Aspects of Medicine , vol.24 , Issue.4-5 , pp. 149-159
    • Schaur, R.J.1
  • 32
    • 84860427093 scopus 로고    scopus 로고
    • Short-term exposure of 4-hydroxynonenal induces mitochondria-mediated apoptosis in PC12 cells
    • 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.
    • (2012) Hum Exp Toxicol , vol.31 , pp. 336-345
    • Siddiqui, M.A.1    Kumar, V.2    Kashyap, M.P.3
  • 33
    • 84864572336 scopus 로고    scopus 로고
    • The amyloid precursor protein copper binding domain histidine residues 149 and 151 mediate APP stability and metabolism
    • 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.
    • (2012) J Biol Chem , vol.287 , pp. 26840-26853
    • Spoerri, L.1    Vella, L.J.2    Pham, C.L.3
  • 34
    • 84884877254 scopus 로고    scopus 로고
    • Lipid peroxidation triggers neurodegeneration: A redox proteomics view into the Alzheimer disease brain
    • 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.
    • (2012) Free Radic Biol Med , vol.62 , pp. 157-169
    • Sultana, R.1    Perluigi, M.2    Allan Butterfield, D.3
  • 35
    • 84859494099 scopus 로고    scopus 로고
    • Lipid peroxidation product 4-hydroxy-trans-2-nonenal causes endothelial activation by inducing endoplasmic reticulum stress
    • 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.
    • (2012) J Biol Chem , vol.287 , pp. 11398-11409
    • Vladykovskaya, E.1    Sithu, S.D.2    Haberzettl, P.3
  • 36
    • 84866954190 scopus 로고    scopus 로고
    • Oxidative and endoplasmic reticulum stresses mediate apoptosis induced by modified LDL in human retinal Müller cells
    • 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.
    • (2012) Invest Ophthalmol Vis Sci , vol.53 , pp. 4595-4604
    • Wu, M.1    Yang, S.2    Elliott, M.H.3
  • 37
    • 39149093682 scopus 로고    scopus 로고
    • Glutathione level regulates HNE-induced genotoxicity in human erythroleukemia cells
    • 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.
    • (2008) Toxicol Appl Pharmacol , vol.227 , pp. 257-264
    • Yadav, U.C.1    Ramana, K.V.2    Awasthi, Y.C.3    Srivastava, S.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.