On the role of 4-hydroxynonenal in health and disease

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1852, Issue 5, 2015, Pages 826-838

  Csala, Miklós ^a   Kardon, Tamás ^a   Legeza, Balázs ^b   Lizák, Beáta ^a   Mandl, József ^a   Margittai, Éva ^a   Puskás, Ferenc ^c   Száraz, Péter ^d   Szelényi, Péter ^a   Bánhegyi, Gábor ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF TORONTO   (Canada)

Author keywords

4 Hydroxynonenal; Electrophilic stress; Lipid peroxidation; Nrf2; Proteostasis

Indexed keywords

4 HYDROXYNONENAL; KELCH LIKE ECH ASSOCIATED PROTEIN 1; TRANSCRIPTION FACTOR NRF2; 4-HYDROXY-2-NONENAL; ALDEHYDE;

ALZHEIMER DISEASE; ANTIPROLIFERATIVE ACTIVITY; APOPTOSIS; AUTOPHAGY; BIOTRANSFORMATION; CARDIOVASCULAR DISEASE; CELL CYCLE; CELL PROLIFERATION; DEGENERATIVE DISEASE; ENDOPLASMIC RETICULUM STRESS; HEAT SHOCK RESPONSE; HUMAN; HUNTINGTON CHOREA; LIPID PEROXIDATION; MYOCARDIAL DISEASE; NEOPLASM; PARKINSON DISEASE; PATHOGENESIS; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN HOMEOSTASIS; REVIEW; SIGNAL TRANSDUCTION; SYNTHESIS; UNFOLDED PROTEIN RESPONSE; CELL FUNCTION; CHEMICAL STRUCTURE; CHEMISTRY; DISEASES; METABOLISM; PHYSIOLOGY;

ALDEHYDES; CARDIOVASCULAR DISEASES; CELL PHYSIOLOGICAL PHENOMENA; DISEASE; HUMANS; MOLECULAR STRUCTURE; NEOPLASMS; NEURODEGENERATIVE DISEASES; SIGNAL TRANSDUCTION;

EID: 84922371393     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2015.01.015     Document Type: Review

References (199)

1. Schauenstein E., Esterbauer H., Jaag G., Taufer M. Über die Wirkungen von Aldehyden auf gesunde und maligne Zellen, 1. Mitt.: Hydroxy-octenal, ein neuer Fettaldehyd. Monatsh. Chem. 1964, 95:180-183.
2. Benedetti A., Comporti M., Esterbauer H. Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochim. Biophys. Acta 1980, 620:281-296.
3. Niki E., Yoshida Y., Saito Y., Noguchi N. Lipid peroxidation: mechanisms, inhibition, and biological effects. Biochem. Biophys. Res. Commun. 2005, 338:668-676.
4. Gueraud F., Atalay M., Bresgen N., Cipak A., Eckl P.M., Huc L., Jouanin I., Siems W., Uchida K. Chemistry and biochemistry of lipid peroxidation products. Free Radic. Res. 2010, 44:1098-1124.
5. Spickett C.M. The lipid peroxidation product 4-hydroxy-2-nonenal: advances in chemistry and analysis. Redox Biol. 2013, 1:145-152.
6. Esterbauer H., Schaur R.J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 1991, 11:81-128.
7. Guillen M.D., Goicoechea E. Toxic oxygenated alpha, beta-unsaturated aldehydes and their study in foods: a review. Crit. Rev. Food Sci. Nutr. 2008, 48:119-136.
8. Zheng R., Dragomir A.C., Mishin V., Richardson J.R., Heck D.E., Laskin D.L., Laskin J.D. Differential metabolism of 4-hydroxynonenal in liver, lung and brain of mice and rats. Toxicol. Appl. Pharmacol. 2014, 279:43-52.
9. Hartley D.P., Ruth J.A., Petersen D.R. The hepatocellular metabolism of 4-hydroxynonenal by alcohol dehydrogenase, aldehyde dehydrogenase, and glutathione S-transferase. Arch. Biochem. Biophys. 1995, 316:197-205.
10. Srivastava S., Dixit B.L., Cai J., Sharma S., Hurst H.E., Bhatnagar A., Srivastava S.K. Metabolism of lipid peroxidation product, 4-hydroxynonenal (HNE) in rat erythrocytes: role of aldose reductase. Free Radic. Biol. Med. 2000, 29:642-651.
11. Amunom I., Stephens L.J., Tamasi V., Cai J., Pierce W.M., Conklin D.J., Bhatnagar A., Srivastava S., Martin M.V., Guengerich F.P., Prough R.A. Cytochromes P450 catalyze oxidation of alpha, beta-unsaturated aldehydes. Arch. Biochem. Biophys. 2007, 464:187-196.
12. Amunom I., Dieter L.J., Tamasi V., Cai J., Conklin D.J., Srivastava S., Martin M.V., Guengerich F.P., Prough R.A. Cytochromes P450 catalyze the reduction of alpha, beta-unsaturated aldehydes. Chem. Res. Toxicol. 2011, 24:1223-1230.
13. Gueraud F., Alary J., Costet P., Debrauwer L., Dolo L., Pineau T., Paris A. In vivo involvement of cytochrome P450 4A family in the oxidative metabolism of the lipid peroxidation product trans-4-hydroxy-2-nonenal, using PPARalpha-deficient mice. J. Lipid Res. 1999, 40:152-159.
14. Jin Z., Berthiaume J.M., Li Q., Henry F., Huang Z., Sadhukhan S., Gao P., Tochtrop G.P., Puchowicz M.A., Zhang G.F. Catabolism of (2E)-4-hydroxy-2-nonenal via omega- and omega-1-oxidation stimulated by ketogenic diet. J. Biol. Chem. 2014, 289:32327-32338.
15. Srivastava S., Chandra A., Bhatnagar A., Srivastava S.K., Ansari N.H. Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase. Biochem. Biophys. Res. Commun. 1995, 217:741-746.
16. Ramana K.V., Bhatnagar A., Srivastava S., Yadav U.C., Awasthi S., Awasthi Y.C., Srivastava S.K. Mitogenic responses of vascular smooth muscle cells to lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE): role of aldose reductase-catalyzed reduction of the HNE-glutathione conjugates in regulating cell growth. J. Biol. Chem. 2006, 281:17652-17660.
17. Frohnert B.I., Long E.K., Hahn W.S., Bernlohr D.A. Glutathionylated lipid aldehydes are products of adipocyte oxidative stress and activators of macrophage inflammation. Diabetes 2014, 63:89-100.
18. Frohnert B.I., Bernlohr D.A. Glutathionylated products of lipid peroxidation: a novel mechanism of adipocyte to macrophage signaling. Adipocyte 2014, 3:224-229.
19. Ramana K.V., Willis M.S., White M.D., Horton J.W., DiMaio J.M., Srivastava D., Bhatnagar A., Srivastava S.K. Endotoxin-induced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition. Circulation 2006, 114:1838-1846.
20. Alary J., Gueraud F., Cravedi J.P. Fate of 4-hydroxynonenal in vivo: disposition and metabolic pathways. Mol. Asp. Med. 2003, 24:177-187.
21. Baradat M., Jouanin I., Dalleau S., Tache S., Gieules M., Debrauwer L., Canlet C., Huc L., Dupuy J., Pierre F.H., Gueraud F. 4-Hydroxy-2(E)-nonenal metabolism differs in Apc(+/+) cells and in Apc(Min/+) cells: it may explain colon cancer promotion by heme iron. Chem. Res. Toxicol. 2011, 24:1984-1993.
22. Renes J., de Vries E.E., Hooiveld G.J., Krikken I., Jansen P.L., Muller M. Multidrug resistance protein MRP1 protects against the toxicity of the major lipid peroxidation product 4-hydroxynonenal. Biochem. J. 2000, 350(Pt 2):555-561.
23. Reichard J.F., Doorn J.A., Simon F., Taylor M.S., Petersen D.R. Characterization of multidrug resistance-associated protein 2 in the hepatocellular disposition of 4-hydroxynonenal. Arch. Biochem. Biophys. 2003, 411:243-250.
24. Singhal S.S., Sehrawat A., Mehta A., Sahu M., Awasthi S. Functional reconstitution of RLIP76 catalyzing ATP-dependent transport of glutathione-conjugates. Int. J. Oncol. 2009, 34:191-199.
25. Singhal S.S., Yadav S., Roth C., Singhal J. RLIP76: a novel glutathione-conjugate and multi-drug transporter. Biochem. Pharmacol. 2009, 77:761-769.
26. Uchida K. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog. Lipid Res. 2003, 42:318-343.
27. Chung F.L., Nath R.G., Ocando J., Nishikawa A., Zhang L. Deoxyguanosine adducts of t-4-hydroxy-2-nonenal are endogenous DNA lesions in rodents and humans: detection and potential sources. Cancer Res. 2000, 60:1507-1511.
28. Sodum R.S., Chung F.L. 1, N2-ethenodeoxyguanosine as a potential marker for DNA adduct formation by trans-4-hydroxy-2-nonenal. Cancer Res. 1988, 48:320-323.
29. Nair J., Barbin A., Velic I., Bartsch H. Etheno DNA-base adducts from endogenous reactive species. Mutat. Res. 1999, 424:59-69.
30. Marnett L.J., Plastaras J.P. Endogenous DNA damage and mutation. Trends Genet. 2001, 17:214-221.
31. Winczura A., Zdzalik D., Tudek B. Damage of DNA and proteins by major lipid peroxidation products in genome stability. Free Radic. Res. 2012, 46:442-459.
32. Schaur R.J. Basic aspects of the biochemical reactivity of 4-hydroxynonenal. Mol. Asp. Med. 2003, 24:149-159.
33. Jacobs A.T., Marnett L.J. Systems analysis of protein modification and cellular responses induced by electrophile stress. Acc. Chem. Res. 2010, 43:673-683.
34. Higdon A.N., Landar A., Barnes S., Darley-Usmar V.M. The electrophile responsive proteome: integrating proteomics and lipidomics with cellular function. Antioxid. Redox Signal. 2012, 17:1580-1589.
35. Ayala A., Munoz M.F., Arguelles S. Lipid peroxidation: production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxidative Med. Cell. Longev. 2014, 2014:360438.
36. Levonen A.L., Hill B.G., Kansanen E., Zhang J., Darley-Usmar V.M. Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics. Free Radic. Biol. Med. 2014, 71:196-207.
37. Kobayashi M., Li L., Iwamoto N., Nakajima-Takagi Y., Kaneko H., Nakayama Y., Eguchi M., Wada Y., Kumagai Y., Yamamoto M. The antioxidant defense system Keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds. Mol. Cell. Biol. 2009, 29:493-502.
38. McMahon M., Lamont D.J., Beattie K.A., Hayes J.D. Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:18838-18843.
39. Gorrini C., Harris I.S., Mak T.W. Modulation of oxidative stress as an anticancer strategy. Nat. Rev. Drug Discov. 2013, 12:931-947.
40. Chowdhry S., Zhang Y., McMahon M., Sutherland C., Cuadrado A., Hayes J.D. Nrf2 is controlled by two distinct beta-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity. Oncogene 2013, 32:3765-3781.
41. Papp D., Lenti K., Modos D., Fazekas D., Dul Z., Turei D., Foldvari-Nagy L., Nussinov R., Csermely P., Korcsmaros T. The NRF2-related interactome and regulome contain multifunctional proteins and fine-tuned autoregulatory loops. FEBS Lett. 2012, 586:1795-1802.
42. Turei D., Papp D., Fazekas D., Foldvari-Nagy L., Modos D., Lenti K., Csermely P., Korcsmaros T. NRF2-ome: an integrated web resource to discover protein interaction and regulatory networks of NRF2. Oxidative Med. Cell. Longev. 2013, 2013:737591.
43. Jones D.P. Redefining oxidative stress. Antioxid. Redox Signal. 2006, 8:1865-1879.
44. Banhegyi G., Margittai E., Szarka A., Mandl J., Csala M. Crosstalk and barriers between the electron carriers of the endoplasmic reticulum. Antioxid. Redox Signal. 2012, 16:772-780.
45. Benedetti A., Esterbauer H., Ferrali M., Fulceri R., Comporti M. Evidence for aldehydes bound to liver microsomal protein following CCl4 or BrCCl3 poisoning. Biochim. Biophys. Acta 1982, 711:345-356.
46. Benedetti A., Fulceri R., Ferrali M., Ciccoli L., Esterbauer H., Comporti M. Detection of carbonyl functions in phospholipids of liver microsomes in CCl4- and BrCCl3-poisoned rats. Biochim. Biophys. Acta 1982, 712:628-638.
47. Ferrali M., Fulceri R., Benedetti A., Comporti M. Effects of carbonyl compounds (4-hydroxyalkenals) originating from the peroxidation of liver microsomal lipids on various microsomal enzyme activities of the liver. Res. Commun. Chem. Pathol. Pharmacol. 1980, 30:99-112.
48. Haberzettl P., Hill B.G. Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response. Redox Biol. 2013, 1:56-64.
49. Carbone D.L., Doorn J.A., Kiebler Z., Petersen D.R. Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase. Chem. Res. Toxicol. 2005, 18:1324-1331.
50. Galligan J.J., Fritz K.S., Backos D.S., Shearn C.T., Smathers R.L., Jiang H., MacLean K.N., Reigan P.R., Petersen D.R. Oxidative stress-mediated aldehyde adduction of GRP78 in a mouse model of alcoholic liver disease: functional independence of ATPase activity and chaperone function. Free Radic. Biol. Med. 2014, 73:411-420.
51. Vladykovskaya E., Sithu S.D., Haberzettl P., Wickramasinghe N.S., Merchant M.L., Hill B.G., McCracken J., Agarwal A., Dougherty S., Gordon S.A., Schuschke D.A., Barski O.A., O'Toole T., D'Souza S.E., Bhatnagar A., Srivastava S. Lipid peroxidation product 4-hydroxy-trans-2-nonenal causes endothelial activation by inducing endoplasmic reticulum stress. J. Biol. Chem. 2012, 287:11398-11409.
52. Lin M.H., Yen J.H., Weng C.Y., Wang L., Ha C.L., Wu M.J. Lipid peroxidation end product 4-hydroxy-trans-2-nonenal triggers unfolded protein response and heme oxygenase-1 expression in PC12 cells: roles of ROS and MAPK pathways. Toxicology 2014, 315:24-37.
53. Cullinan S.B., Zhang D., Hannink M., Arvisais E., Kaufman R.J., Diehl J.A. Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol. Cell. Biol. 2003, 23:7198-7209.
54. Del Vecchio C.A., Feng Y., Sokol E.S., Tillman E.J., Sanduja S., Reinhardt F., Gupta P.B. De-differentiation confers multidrug resistance via noncanonical PERK-Nrf2 signaling. PLoS Biol. 2014, 12:e1001945.
55. Vila A., Tallman K.A., Jacobs A.T., Liebler D.C., Porter N.A., Marnett L.J. Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives. Chem. Res. Toxicol. 2008, 21:432-444.
56. Wang Y., Gibney P.A., West J.D., Morano K.A. The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds. Mol. Biol. Cell 2012, 23:3290-3298.
57. Jacobs A.T., Marnett L.J. Heat shock factor 1 attenuates 4-Hydroxynonenal-mediated apoptosis: critical role for heat shock protein 70 induction and stabilization of Bcl-XL. J. Biol. Chem. 2007, 282:33412-33420.
58. Kaarniranta K., Ryhanen T., Karjalainen H.M., Lammi M.J., Suuronen T., Huhtala A., Kontkanen M., Terasvirta M., Uusitalo H., Salminen A. Geldanamycin increases 4-hydroxynonenal (HNE)-induced cell death in human retinal pigment epithelial cells. Neurosci. Lett. 2005, 382:185-190.
59. Calamini B., Silva M.C., Madoux F., Hutt D.M., Khanna S., Chalfant M.A., Saldanha S.A., Hodder P., Tait B.D., Garza D., Balch W.E., Morimoto R.I. Small-molecule proteostasis regulators for protein conformational diseases. Nat. Chem. Biol. 2012, 8:185-196.
60. West J.D., Wang Y., Morano K.A. Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise. Chem. Res. Toxicol. 2012, 25:2036-2053.
61. Komatsu M., Kurokawa H., Waguri S., Taguchi K., Kobayashi A., Ichimura Y., Sou Y.S., Ueno I., Sakamoto A., Tong K.I., Kim M., Nishito Y., Iemura S., Natsume T., Ueno T., Kominami E., Motohashi H., Tanaka K., Yamamoto M. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat. Cell Biol. 2010, 12:213-223.
62. Jain A., Lamark T., Sjottem E., Larsen K.B., Awuh J.A., Overvatn A., McMahon M., Hayes J.D., Johansen T. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J. Biol. Chem. 2010, 285:22576-22591.
63. Kageyama S., Sou Y.S., Uemura T., Kametaka S., Saito T., Ishimura R., Kouno T., Bedford L., Mayer R.J., Lee M.S., Yamamoto M., Waguri S., Tanaka K., Komatsu M. Proteasome dysfunction activates autophagy and the keap1-nrf2 pathway. J. Biol. Chem. 2014, 289:24944-24955.
64. Pickering A.M., Linder R.A., Zhang H., Forman H.J., Davies K.J. Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress. J. Biol. Chem. 2012, 287:10021-10031.
65. Chapple S.J., Cheng X., Mann G.E. Effects of 4-hydroxynonenal on vascular endothelial and smooth muscle cell redox signaling and function in health and disease. Redox Biol. 2013, 1:319-331.
66. Arguelles S., Machado A., Ayala A. Adduct formation of 4-hydroxynonenal and malondialdehyde with elongation factor-2 in vitro and in vivo. Free Radic. Biol. Med. 2009, 47:324-330.
67. Chaudhary P., Sharma R., Sharma A., Vatsyayan R., Yadav S., Singhal S.S., Rauniyar N., Prokai L., Awasthi S., Awasthi Y.C. Mechanisms of 4-hydroxy-2-nonenal induced pro- and anti-apoptotic signaling. Biochemistry 2010, 49:6263-6275.
68. Dice J.F. Chaperone-mediated autophagy. Autophagy 2007, 3:295-299.
69. Klionsky D.J., Ohsumi Y. Vacuolar import of proteins and organelles from the cytoplasm. Annu. Rev. Cell Dev. Biol. 1999, 15:1-32.
70. Wong P.M., Puente C., Ganley I.G., Jiang X. The ULK1 complex: sensing nutrient signals for autophagy activation. Autophagy 2013, 9:124-137.
71. Mandl J., Meszaros T., Banhegyi G., Hunyady L., Csala M. Endoplasmic reticulum: nutrient sensor in physiology and pathology. Trends Endocrinol. Metab. 2009, 20:194-201.
72. Bergamini E., Cavallini G., Donati A., Gori Z. The role of autophagy in aging: its essential part in the anti-aging mechanism of caloric restriction. Ann. N. Y. Acad. Sci. 2007, 1114:69-78.
73. Knuppertz L., Hamann A., Pampaloni F., Stelzer E., Osiewacz H.D. Identification of autophagy as a longevity-assurance mechanism in the aging model Podospora anserina. Autophagy 2014, 10:822-834.
74. Zhang C., Cuervo A.M. Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat. Med. 2008, 14:959-965.
75. Giordano S., Darley-Usmar V., Zhang J. Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease. Redox Biol. 2014, 2:82-90.
76. Tang B., Cai J., Sun L., Li Y., Qu J., Snider B.J., Wu S. Proteasome inhibitors activate autophagy involving inhibition of PI3K-Akt-mTOR pathway as an anti-oxidation defense in human RPE cells. PLoS One 2014, 9:e103364.
77. Hill B.G., Haberzettl P., Ahmed Y., Srivastava S., Bhatnagar A. Unsaturated lipid peroxidation-derived aldehydes activate autophagy in vascular smooth-muscle cells. Biochem. J. 2008, 410:525-534.
78. Csala M., Banhegyi G., Benedetti A. Endoplasmic reticulum: a metabolic compartment. FEBS Lett. 2006, 580:2160-2165.
79. Mandl J., Meszaros T., Banhegyi G., Csala M. Minireview: endoplasmic reticulum stress: control in protein, lipid, and signal homeostasis. Mol. Endocrinol. 2013, 27:384-393.
80. Dodson M., Liang Q., Johnson M.S., Redmann M., Fineberg N., Darley-Usmar V.M., Zhang J. Inhibition of glycolysis attenuates 4-hydroxynonenal-dependent autophagy and exacerbates apoptosis in differentiated SH-SY5Y neuroblastoma cells. Autophagy 2013, 9:1996-2008.
81. Ma H., Guo R., Yu L., Zhang Y., Ren J. Aldehyde dehydrogenase 2 (ALDH2) rescues myocardial ischaemia/reperfusion injury: role of autophagy paradox and toxic aldehyde. Eur. Heart J. 2011, 32:1025-1038.
82. Sun A., Cheng Y., Zhang Y., Zhang Q., Wang S., Tian S., Zou Y., Hu K., Ren J., Ge J. Aldehyde dehydrogenase 2 ameliorates doxorubicin-induced myocardial dysfunction through detoxification of 4-HNE and suppression of autophagy. J. Mol. Cell. Cardiol. 2014, 71:92-104.
83. Schutt F., Bergmann M., Holz F.G., Kopitz J. Proteins modified by malondialdehyde, 4-hydroxynonenal, or advanced glycation end products in lipofuscin of human retinal pigment epithelium. Invest. Ophthalmol. Vis. Sci. 2003, 44:3663-3668.
84. Krohne T.U., Kaemmerer E., Holz F.G., Kopitz J. Lipid peroxidation products reduce lysosomal protease activities in human retinal pigment epithelial cells via two different mechanisms of action. Exp. Eye Res. 2010, 90:261-266.
85. Krohne T.U., Stratmann N.K., Kopitz J., Holz F.G. Effects of lipid peroxidation products on lipofuscinogenesis and autophagy in human retinal pigment epithelial cells. Exp. Eye Res. 2010, 90:465-471.
86. Zetterberg A., Larsson O., Wiman K.G. What is the restriction point?. Curr. Opin. Cell Biol. 1995, 7:835-842.
87. Golias C.H., Charalabopoulos A., Charalabopoulos K. Cell proliferation and cell cycle control: a mini review. Int. J. Clin. Pract. 2004, 58:1134-1141.
88. Yang A., McKeon F. P63 and P73: P53 mimics, menaces and more. Nat. Rev. Mol. Cell Biol. 2000, 1:199-207.
89. Cox L.S. Multiple pathways control cell growth and transformation: overlapping and independent activities of p53 and p21Cip1/WAF1/Sdi1. J. Pathol. 1997, 183:134-140.
90. Dianzani M.U. Lipid peroxidation and cancer. Crit. Rev. Oncol. Hematol. 1993, 15:125-147.
91. Canuto R.A., Muzio G., Bassi A.M., Maggiora M., Leonarduzzi G., Lindahl R., Dianzani M.U., Ferro M. Enrichment with arachidonic acid increases the sensitivity of hepatoma cells to the cytotoxic effects of oxidative stress. Free Radic. Biol. Med. 1995, 18:287-293.
92. Muzio G., Salvo R.A., Trombetta A., Autelli R., Maggiora M., Terreno M., Dianzani M.U., Canuto R.A. Dose-dependent inhibition of cell proliferation induced by lipid peroxidation products in rat hepatoma cells after enrichment with arachidonic acid. Lipids 1999, 34:705-711.
93. Barrera G., Pizzimenti S., Laurora S., Briatore F., Toaldo C., Dianzani M.U. 4-Hydroxynonenal and cell cycle. Biofactors 2005, 24:151-157.
94. Barrera G., Brossa O., Fazio V.M., Farace M.G., Paradisi L., Gravela E., Dianzani M.U. Effects of 4-hydroxynonenal, a product of lipid peroxidation, on cell proliferation and ornithine decarboxylase activity. Free Radic. Res. Commun. 1991, 14:81-89.
95. Barrera G., Pizzimenti S., Muraca R., Barbiero G., Bonelli G., Baccino F.M., Fazio V.M., Dianzani M.U. Effect of 4-hydroxynonenal on cell cycle progression and expression of differentiation-associated antigens in HL-60 cells. Free Radic. Biol. Med. 1996, 20:455-462.
96. Barrera G., Muraca R., Pizzimenti S., Serra A., Rosso C., Saglio G., Farace M.G., Fazio V.M., Dianzani M.U. Inhibition of c-myc expression induced by 4-hydroxynonenal, a product of lipid peroxidation, in the HL-60 human leukemic cell line. Biochem. Biophys. Res. Commun. 1994, 203:553-561.
97. Barrera G., Pizzimenti S., Serra A., Ferretti C., Fazio V.M., Saglio G., Dianzani M.U. 4-Hydroxynonenal specifically inhibits c-myb but does not affect c-fos expressions in HL-60 cells. Biochem. Biophys. Res. Commun. 1996, 227:589-593.
98. Fazio V.M., Barrera G., Martinotti S., Farace M.G., Giglioni B., Frati L., Manzari V., Dianzani M.U. 4-Hydroxynonenal, a product of cellular lipid peroxidation, which modulates c-myc and globin gene expression in K562 erythroleukemic cells. Cancer Res. 1992, 52:4866-4871.
99. Pizzimenti S., Barrera G., Dianzani M.U., Brusselbach S. Inhibition of D1, D2, and A-cyclin expression in HL-60 cells by the lipid peroxydation product 4-hydroxynonenal. Free Radic. Biol. Med. 1999, 26:1578-1586.
100. Barrera G., Pizzimenti S., Laurora S., Moroni E., Giglioni B., Dianzani M.U. 4-Hydroxynonenal affects pRb/E2F pathway in HL-60 human leukemic cells. Biochem. Biophys. Res. Commun. 2002, 295:267-275.
101. Wolf D., Rotter V. Major deletions in the gene encoding the p53 tumor antigen cause lack of p53 expression in HL-60 cells. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:790-794.
102. Sharma R., Brown D., Awasthi S., Yang Y., Sharma A., Patrick B., Saini M.K., Singh S.P., Zimniak P., Singh S.V., Awasthi Y.C. Transfection with 4-hydroxynonenal-metabolizing glutathione S-transferase isozymes leads to phenotypic transformation and immortalization of adherent cells. Eur. J. Biochem. 2004, 271:1690-1701.
103. Patrick B., Li J., Jeyabal P.V., Reddy P.M., Yang Y., Sharma R., Sinha M., Luxon B., Zimniak P., Awasthi S., Awasthi Y.C. Depletion of 4-hydroxynonenal in hGSTA4-transfected HLE B-3 cells results in profound changes in gene expression. Biochem. Biophys. Res. Commun. 2005, 334:425-432.
104. Laurora S., Tamagno E., Briatore F., Bardini P., Pizzimenti S., Toaldo C., Reffo P., Costelli P., Dianzani M.U., Danni O., Barrera G. 4-Hydroxynonenal modulation of p53 family gene expression in the SK-N-BE neuroblastoma cell line. Free Radic. Biol. Med. 2005, 38:215-225.
105. Parola M., Robino G., Marra F., Pinzani M., Bellomo G., Leonarduzzi G., Chiarugi P., Camandola S., Poli G., Waeg G., Gentilini P., Dianzani M.U. HNE interacts directly with JNK isoforms in human hepatic stellate cells. J. Clin. Invest. 1998, 102:1942-1950.
106. Robino G., Parola M., Marra F., Caligiuri A., De Franco R.M., Zamara E., Bellomo G., Gentilini P., Pinzani M., Dianzani M.U. Interaction between 4-hydroxy-2,3-alkenals and the platelet-derived growth factor-beta receptor. Reduced tyrosine phosphorylation and downstream signaling in hepatic stellate cells. J. Biol. Chem. 2000, 275:40561-40567.
107. Ruef J., Rao G.N., Li F., Bode C., Patterson C., Bhatnagar A., Runge M.S. Induction of rat aortic smooth muscle cell growth by the lipid peroxidation product 4-hydroxy-2-nonenal. Circulation 1998, 97:1071-1078.
108. Pappa A., Brown D., Koutalos Y., DeGregori J., White C., Vasiliou V. Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells. J. Biol. Chem. 2005, 280:27998-28006.
109. Lee T.J., Lee J.T., Moon S.K., Kim C.H., Park J.W., Kwon T.K. Age-related differential growth rate and response to 4-hydroxynonenal in mouse aortic smooth muscle cells. Int. J. Mol. Med. 2006, 17:29-35.
110. Guicciardi M.E., Gores G.J. Life and death by death receptors. FASEB J. 2009, 23:1625-1637.
111. Moldoveanu T., Follis A.V., Kriwacki R.W., Green D.R. Many players in BCL-2 family affairs. Trends Biochem. Sci. 2014, 39:101-111.
112. Dalleau S., Baradat M., Gueraud F., Huc L. Cell death and diseases related to oxidative stress: 4-hydroxynonenal (HNE) in the balance. Cell Death Differ. 2013, 20:1615-1630.
113. Hampton M.B., Orrenius S. Redox regulation of apoptotic cell death. Biofactors 1998, 8:1-5.
114. Liu W., Kato M., Akhand A.A., Hayakawa A., Suzuki H., Miyata T., Kurokawa K., Hotta Y., Ishikawa N., Nakashima I. 4-Hydroxynonenal induces a cellular redox status-related activation of the caspase cascade for apoptotic cell death. J. Cell Sci. 2000, 113(Pt 4):635-641.
115. Raza H., John A. 4-Hydroxynonenal induces mitochondrial oxidative stress, apoptosis and expression of glutathione S-transferase A4-4 and cytochrome P450 2E1 in PC12 cells. Toxicol. Appl. Pharmacol. 2006, 216:309-318.
116. Vaillancourt F., Fahmi H., Shi Q., Lavigne P., Ranger P., Fernandes J.C., Benderdour M. 4-Hydroxynonenal induces apoptosis in human osteoarthritic chondrocytes: the protective role of glutathione-S-transferase. Arthritis Res. Ther. 2008, 10:R107.
117. Nakajima A., Yamada K., Zou L.B., Yan Y., Mizuno M., Nabeshima T. Interleukin-6 protects PC12 cells from 4-hydroxynonenal-induced cytotoxicity by increasing intracellular glutathione levels. Free Radic. Biol. Med. 2002, 32:1324-1332.
118. Kutuk O., Basaga H. Apoptosis signalling by 4-hydroxynonenal: a role for JNK-c-Jun/AP-1 pathway. Redox Rep. 2007, 12:30-34.
119. Csala M., Kereszturi E., Mandl J., Banhegyi G. The endoplasmic reticulum as the extracellular space inside the cell: role in protein folding and glycosylation. Antioxid. Redox Signal. 2012, 16:1100-1108.
120. Csala M., Margittai E., Banhegyi G. Redox control of endoplasmic reticulum function. Antioxid. Redox Signal. 2010, 13:77-108.
121. Cumaoglu A., Aricioglu A., Karasu C. Redox status related activation of endoplasmic reticulum stress and apoptosis caused by 4-hydroxynonenal exposure in INS-1 cells. Toxicol. Mech. Methods 2014, 24:362-367.
122. Liao J., Sun A., Xie Y., Isse T., Kawamoto T., Zou Y., Ge J. Aldehyde dehydrogenase-2 deficiency aggravates cardiac dysfunction elicited by endoplasmic reticulum stress induction. Mol. Med. 2012, 18:785-793.
123. Liu W., Akhand A.A., Takeda K., Kawamoto Y., Itoigawa M., Kato M., Suzuki H., Ishikawa N., Nakashima I. Protein phosphatase 2A-linked and -unlinked caspase-dependent pathways for downregulation of Akt kinase triggered by 4-hydroxynonenal. Cell Death Differ. 2003, 10:772-781.
124. Ji G.R., Yu N.C., Xue X., Li Z.G. 4-Hydroxy-2-nonenal induces apoptosis by inhibiting AKT signaling in human osteosarcoma cells. ScientificWorldJournal 2014, 2014:873525.
125. Haynes R.L., Brune B., Townsend A.J. Apoptosis in RAW 264.7 cells exposed to 4-hydroxy-2-nonenal: dependence on cytochrome C release but not p53 accumulation. Free Radic. Biol. Med. 2001, 30:884-894.
126. Shoeb M., Ansari N.H., Srivastava S.K., Ramana K.V. 4-Hydroxynonenal in the pathogenesis and progression of human diseases. Curr. Med. Chem. 2014, 21:230-237.
127. Duncker D.J., Bache R.J. Regulation of coronary blood flow during exercise. Physiol. Rev. 2008, 88:1009-1086.
128. Dedkova E.N., Blatter L.A. Measuring mitochondrial function in intact cardiac myocytes. J. Mol. Cell. Cardiol. 2012, 52:48-61.
129. Barth E., Stammler G., Speiser B., Schaper J. Ultrastructural quantitation of mitochondria and myofilaments in cardiac muscle from 10 different animal species including man. J. Mol. Cell. Cardiol. 1992, 24:669-681.
130. Mali V.R., Palaniyandi S.S. Regulation and therapeutic strategies of 4-hydroxy-2-nonenal metabolism in heart disease. Free Radic. Res. 2014, 48:251-263.
131. Roede J.R., Jones D.P. Reactive species and mitochondrial dysfunction: mechanistic significance of 4-hydroxynonenal. Environ. Mol. Mutagen. 2010, 51:380-390.
132. Nakamura K., K no K., Nakamura Y., Kakishita M., Ohta K., Nagase S., Yamamoto M., Miyaji K., Saito H., Morita H., Emori T., Matsubara H., Toyokuni S., Ohe T. Carvedilol decreases elevated oxidative stress in human failing myocardium. Circulation 2002, 105:2867-2871.
133. Mak S., Lehotay D.C., Yazdanpanah M., Azevedo E.R., Liu P.P., Newton G.E. Unsaturated aldehydes including 4-OH-nonenal are elevated in patients with congestive heart failure. J. Card. Fail. 2000, 6:108-114.
134. Asselin C., Ducharme A., Ntimbane T., Ruiz M., Fortier A., Guertin M.C., Lavoie J., Diaz A., Levy E., Tardif J.C., Des Rosiers C. Circulating levels of linoleic acid and HDL-cholesterol are major determinants of 4-hydroxynonenal protein adducts in patients with heart failure. Redox Biol. 2014, 2:148-155.
135. Blasig I.E., Grune T., Schonheit K., Rohde E., Jakstadt M., Haseloff R.F., Siems W.G. 4-Hydroxynonenal, a novel indicator of lipid peroxidation for reperfusion injury of the myocardium. Am. J. Physiol. 1995, 269:H14-H22.
136. Renner A., Sagstetter M.R., Harms H., Lange V., Gotz M.E., Elert O. Formation of 4-hydroxy-2-nonenal protein adducts in the ischemic rat heart after transplantation. J. Heart Lung Transplant. 2005, 24:730-736.
137. Chen C.H., Budas G.R., Churchill E.N., Disatnik M.H., Hurley T.D., Mochly-Rosen D. Activation of aldehyde dehydrogenase-2 reduces ischemic damage to the heart. Science 2008, 321:1493-1495.
138. Gomes K.M., Campos J.C., Bechara L.R., Queliconi B., Lima V.M., Disatnik M.H., Magno P., Chen C.H., Brum P.C., Kowaltowski A.J., Mochly-Rosen D., Ferreira J.C. Aldehyde dehydrogenase 2 activation in heart failure restores mitochondrial function and improves ventricular function and remodelling. Cardiovasc. Res. 2014, 103:498-508.
139. Benedetti A., Casini A.F., Ferrali M., Comporti M. Extraction and partial characterization of dialysable products originating from the peroxidation of liver microsomal lipids and inhibiting microsomal glucose 6-phosphatase activity. Biochem. Pharmacol. 1979, 28:2909-2918.
140. Benedetti A., Barbieri L., Ferrali M., Casini A.F., Fulceri R., Comporti M. Inhibition of protein synthesis by carbonyl compounds (4-hydroxyalkenals) originating from the peroxidation of liver microsomal lipids. Chem. Biol. Interact. 1981, 35:331-340.
141. Fernandes P.H., Wang H., Rizzo C.J., Lloyd R.S. Site-specific mutagenicity of stereochemically defined 1, N2-deoxyguanosine adducts of trans-4-hydroxynonenal in mammalian cells. Environ. Mol. Mutagen. 2003, 42:68-74.
142. Minko I.G., Kozekov I.D., Harris T.M., Rizzo C.J., Lloyd R.S., Stone M.P. Chemistry and biology of DNA containing 1, N(2)-deoxyguanosine adducts of the alpha, beta-unsaturated aldehydes acrolein, crotonaldehyde, and 4-hydroxynonenal. Chem. Res. Toxicol. 2009, 22:759-778.
143. Voulgaridou G.P., Anestopoulos I., Franco R., Panayiotidis M.I., Pappa A. DNA damage induced by endogenous aldehydes: current state of knowledge. Mutat. Res. 2011, 711:13-27.
144. Hu W., Feng Z., Eveleigh J., Iyer G., Pan J., Amin S., Chung F.L., Tang M.S. The major lipid peroxidation product, trans-4-hydroxy-2-nonenal, preferentially forms DNA adducts at codon 249 of human p53 gene, a unique mutational hotspot in hepatocellular carcinoma. Carcinogenesis 2002, 23:1781-1789.
145. Feng Z., Hu W., Tang M.S. Trans-4-hydroxy-2-nonenal inhibits nucleotide excision repair in human cells: a possible mechanism for lipid peroxidation-induced carcinogenesis. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:8598-8602.
146. Tjalkens R.B., Cook L.W., Petersen D.R. Formation and export of the glutathione conjugate of 4-hydroxy-2, 3-E-nonenal (4-HNE) in hepatoma cells. Arch. Biochem. Biophys. 1999, 361:113-119.
147. Cheeseman K.H., Burton G.W., Ingold K.U., Slater T.F. Lipid peroxidation and lipid antioxidants in normal and tumor cells. Toxicol. Pathol. 1984, 12:235-239.
148. Biasi F., Tessitore L., Zanetti D., Cutrin J.C., Zingaro B., Chiarpotto E., Zarkovic N., Serviddio G., Poli G. Associated changes of lipid peroxidation and transforming growth factor beta1 levels in human colon cancer during tumour progression. Gut 2002, 50:361-367.
149. Zanetti D., Poli G., Vizio B., Zingaro B., Chiarpotto E., Biasi F. 4-Hydroxynonenal and transforming growth factor-beta1 expression in colon cancer. Mol. Asp. Med. 2003, 24:273-280.
150. Skrzydlewska E., Stankiewicz A., Sulkowska M., Sulkowski S., Kasacka I. Antioxidant status and lipid peroxidation in colorectal cancer. J. Toxic. Environ. Health A 2001, 64:213-222.
151. Young O., Crotty T., O'Connell R., O'Sullivan J., Curran A.J. Levels of oxidative damage and lipid peroxidation in thyroid neoplasia. Head Neck 2010, 32:750-756.
152. Karihtala P., Kauppila S., Puistola U., Jukkola-Vuorinen A. Divergent behaviour of oxidative stress markers 8-hydroxydeoxyguanosine (8-OHdG) and 4-hydroxy-2-nonenal (HNE) in breast carcinogenesis. Histopathology 2011, 58:854-862.
153. Bur H., Haapasaari K.M., Turpeenniemi-Hujanen T., Kuittinen O., Auvinen P., Marin K., Koivunen P., Sormunen R., Soini Y., Karihtala P. Oxidative stress markers and mitochondrial antioxidant enzyme expression are increased in aggressive Hodgkin lymphomas. Histopathology 2014, 65:319-327.
154. Marquez-Quinones A., Cipak A., Zarkovic K., Fattel-Fazenda S., Villa-Trevino S., Waeg G., Zarkovic N., Gueraud F. HNE-protein adducts formation in different pre-carcinogenic stages of hepatitis in LEC rats. Free Radic. Res. 2010, 44:119-127.
155. Dianzani M.U. Lipid peroxidation and cancer: a critical reconsideration. Tumori 1989, 75:351-357.
156. DeNicola G.M., Karreth F.A., Humpton T.J., Gopinathan A., Wei C., Frese K., Mangal D., Yu K.H., Yeo C.J., Calhoun E.S., Scrimieri F., Winter J.M., Hruban R.H., Iacobuzio-Donahue C., Kern S.E., Blair I.A., Tuveson D.A. Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis. Nature 2011, 475:106-109.
157. Tjalkens R.B., Luckey S.W., Kroll D.J., Petersen D.R. Alpha, beta-unsaturated aldehydes mediate inducible expression of glutathione S-transferase in hepatoma cells through activation of the antioxidant response element (ARE). Adv. Exp. Med. Biol. 1999, 463:123-131.
158. Mitsuishi Y., Taguchi K., Kawatani Y., Shibata T., Nukiwa T., Aburatani H., Yamamoto M., Motohashi H. Nrf2 redirects glucose and glutamine into anabolic pathways in metabolic reprogramming. Cancer Cell 2012, 22:66-79.
159. Leinonen H.M., Kansanen E., Polonen P., Heinaniemi M., Levonen A.L. Role of the Keap1-Nrf2 pathway in cancer. Adv. Cancer Res. 2014, 122:281-320.
160. Kansanen E., Kuosmanen S.M., Leinonen H., Levonen A.L. The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer. Redox Biol. 2013, 1:45-49.
161. Perluigi M., Coccia R., Butterfield D.A. 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies. Antioxid. Redox Signal. 2012, 17:1590-1609.
162. Sultana R., Perluigi M., Allan Butterfield D. Lipid peroxidation triggers neurodegeneration: a redox proteomics view into the Alzheimer disease brain. Free Radic. Biol. Med. 2013, 62:157-169.
163. Kim S., Kim K.T. Therapeutic approaches for inhibition of protein aggregation in Huntington's disease. Exp. Neurobiol. 2014, 23:36-44.
164. Browne S.E., Ferrante R.J., Beal M.F. Oxidative stress in Huntington's disease. Brain Pathol. 1999, 9:147-163.
165. Sorolla M.A., Reverter-Branchat G., Tamarit J., Ferrer I., Ros J., Cabiscol E. Proteomic and oxidative stress analysis in human brain samples of Huntington disease. Free Radic. Biol. Med. 2008, 45:667-678.
166. Chen C.M., Wu Y.R., Cheng M.L., Liu J.L., Lee Y.M., Lee P.W., Soong B.W., Chiu D.T. Increased oxidative damage and mitochondrial abnormalities in the peripheral blood of Huntington's disease patients. Biochem. Biophys. Res. Commun. 2007, 359:335-340.
167. Stack E.C., Matson W.R., Ferrante R.J. Evidence of oxidant damage in Huntington's disease: translational strategies using antioxidants. Ann. N. Y. Acad. Sci. 2008, 1147:79-92.
168. Lee J., Kosaras B., Del Signore S.J., Cormier K., McKee A., Ratan R.R., Kowall N.W., Ryu H. Modulation of lipid peroxidation and mitochondrial function improves neuropathology in Huntington's disease mice. Acta Neuropathol. 2011, 121:487-498.
169. Okada K., Wangpoengtrakul C., Osawa T., Toyokuni S., Tanaka K., Uchida K. 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules. J. Biol. Chem. 1999, 274:23787-23793.
170. Reed T.T. Lipid peroxidation and neurodegenerative disease. Free Radic. Biol. Med. 2011, 51:1302-1319.
171. Xiang W., Schlachetzki J.C., Helling S., Bussmann J.C., Berlinghof M., Schaffer T.E., Marcus K., Winkler J., Klucken J., Becker C.M. Oxidative stress-induced posttranslational modifications of alpha-synuclein: specific modification of alpha-synuclein by 4-hydroxy-2-nonenal increases dopaminergic toxicity. Mol. Cell. Neurosci. 2013, 54:71-83.
172. Martinez-Vicente M., Talloczy Z., Kaushik S., Massey A.C., Mazzulli J., Mosharov E.V., Hodara R., Fredenburg R., Wu D.C., Follenzi A., Dauer W., Przedborski S., Ischiropoulos H., Lansbury P.T., Sulzer D., Cuervo A.M. Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. J. Clin. Invest. 2008, 118:777-788.
173. Zarkovic K. 4-Hydroxynonenal and neurodegenerative diseases. Mol. Asp. Med. 2003, 24:293-303.
174. Anderson G., Maes M. Neurodegeneration in Parkinson's disease: interactions of oxidative stress, tryptophan catabolites and depression with mitochondria and sirtuins. Mol. Neurobiol. 2014, 49:771-783.
175. Nasstrom T., Fagerqvist T., Barbu M., Karlsson M., Nikolajeff F., Kasrayan A., Ekberg M., Lannfelt L., Ingelsson M., Bergstrom J. The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of alpha-synuclein oligomers with distinct biochemical, morphological, and functional properties. Free Radic. Biol. Med. 2011, 50:428-437.
176. Bae E.J., Ho D.H., Park E., Jung J.W., Cho K., Hong J.H., Lee H.J., Kim K.P., Lee S.J. Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of alpha-synuclein. Antioxid. Redox Signal. 2013, 18:770-783.
177. Morel P., Tallineau C., Pontcharraud R., Piriou A., Huguet F. Effects of 4-hydroxynonenal, a lipid peroxidation product, on dopamine transport and Na+/K+ ATPase in rat striatal synaptosomes. Neurochem. Int. 1998, 33:531-540.
178. van der Putten H., Lotz G.P. Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases. Neurotherapeutics 2013, 10:416-428.
179. Xu Y., Yan J., Zhou P., Li J., Gao H., Xia Y., Wang Q. Neurotransmitter receptors and cognitive dysfunction in Alzheimer's disease and Parkinson's disease. Prog. Neurobiol. 2012, 97:1-13.
180. Wyss-Coray T. Inflammation in Alzheimer disease: driving force, bystander or beneficial response?. Nat. Med. 2006, 12:1005-1015.
181. Rios J.A., Cisternas P., Arrese M., Barja S., Inestrosa N.C. Is Alzheimer's disease related to metabolic syndrome? A Wnt signaling conundrum. Prog. Neurobiol. 2014, 121:125-146.
182. Pratico D., Sung S. Lipid peroxidation and oxidative imbalance: early functional events in Alzheimer's disease. J. Alzheimers Dis. 2004, 6:171-175.
183. Zhao Y., Zhao B. Oxidative stress and the pathogenesis of Alzheimer's disease. Oxidative Med. Cell. Longev. 2013, 2013:316523.
184. Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994, 77:817-827.
185. Marcus D.L., Thomas C., Rodriguez C., Simberkoff K., Tsai J.S., Strafaci J.A., Freedman M.L. Increased peroxidation and reduced antioxidant enzyme activity in Alzheimer's disease. Exp. Neurol. 1998, 150:40-44.
186. Williams T.I., Lynn B.C., Markesbery W.R., Lovell M.A. Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in mild cognitive impairment and early Alzheimer's disease. Neurobiol. Aging 2006, 27:1094-1099.
187. McGrath L.T., McGleenon B.M., Brennan S., McColl D., Mc I.S., Passmore A.P. Increased oxidative stress in Alzheimer's disease as assessed with 4-hydroxynonenal but not malondialdehyde. QJM 2001, 94:485-490.
188. Markesbery W.R., Lovell M.A. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol. Aging 1998, 19:33-36.
189. Hardas S.S., Sultana R., Clark A.M., Beckett T.L., Szweda L.I., Murphy M.P., Butterfield D.A. Oxidative modification of lipoic acid by HNE in Alzheimer disease brain. Redox Biol. 2013, 1:80-85.
190. Butterfield D.A., Drake J., Pocernich C., Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol. Med. 2001, 7:548-554.
191. Tamagno E., Robino G., Obbili A., Bardini P., Aragno M., Parola M., Danni O. H2O2 and 4-hydroxynonenal mediate amyloid beta-induced neuronal apoptosis by activating JNKs and p38MAPK. Exp. Neurol. 2003, 180:144-155.
192. Smith D.G., Cappai R., Barnham K.J. The redox chemistry of the Alzheimer's disease amyloid beta peptide. Biochim. Biophys. Acta 2007, 1768:1976-1990.
193. Subramaniam R., Roediger F., Jordan B., Mattson M.P., Keller J.N., Waeg G., Butterfield D.A. The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters the conformation of cortical synaptosomal membrane proteins. J. Neurochem. 1997, 69:1161-1169.
194. Perluigi M., Sultana R., Cenini G., Di Domenico F., Memo M., Pierce W.M., Coccia R., Butterfield D.A. Redox proteomics identification of 4-hydroxynonenal-modified brain proteins in Alzheimer's disease: role of lipid peroxidation in Alzheimer's disease pathogenesis. Proteomics Clin. Appl. 2009, 3:682-693.
195. Shinall H., Song E.S., Hersh L.B. Susceptibility of amyloid beta peptide degrading enzymes to oxidative damage: a potential Alzheimer's disease spiral. Biochemistry 2005, 44:15345-15350.
196. Lauderback C.M., Hackett J.M., Huang F.F., Keller J.N., Szweda L.I., Markesbery W.R., Butterfield D.A. The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Abeta1-42. J. Neurochem. 2001, 78:413-416.
197. Sultana R., Boyd-Kimball D., Cai J., Pierce W.M., Klein J.B., Merchant M., Butterfield D.A. Proteomics analysis of the Alzheimer's disease hippocampal proteome. J. Alzheimers Dis. 2007, 11:153-164.
198. Chen Z.H., Niki E. 4-Hydroxynonenal (4-HNE) has been widely accepted as an inducer of oxidative stress. Is this the whole truth about it or can 4-HNE also exert protective effects?. IUBMB Life 2006, 58:372-373.
199. Rajasekaran N.S., Connell P., Christians E.S., Yan L.J., Taylor R.P., Orosz A., Zhang X.Q., Stevenson T.J., Peshock R.M., Leopold J.A., Barry W.H., Loscalzo J., Odelberg S.J., Benjamin I.J. Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice. Cell 2007, 130:427-439.