Oxidative and reductive metabolism of lipid-peroxidation derived carbonyls

Chemico-Biological Interactions

Volumn 234, Issue , 2015, Pages 261-273

  Singh, Mahavir ^a   Kapoor, Aniruddh ^a   Bhatnagar, Aruni ^a  

^a University of Louisville School of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4-HYDROXY-2-NONENAL; 4-OXO-2-NONENAL; ACROLEIN; ALCOHOL DEHYDROGENASE; ALDEHYDE; ALDEHYDE DEHYDROGENASE; ALDEHYDE REDUCTASE; CARBONYL REDUCTASE; GLUTATHIONE; LIPID; MALONALDEHYDE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE;

LIPID PEROXIDATION; METABOLISM; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PHYSIOLOGY; PROTEIN CARBONYLATION;

ACROLEIN; ALCOHOL OXIDOREDUCTASES; ALDEHYDE DEHYDROGENASE; ALDEHYDE REDUCTASE; ALDEHYDES; GLUTATHIONE; LIPID PEROXIDATION; LIPIDS; MALONDIALDEHYDE; OXIDATION-REDUCTION; OXIDATIVE STRESS; OXIDOREDUCTASES; PROTEIN CARBONYLATION; REACTIVE OXYGEN SPECIES;

EID: 84939950152     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2014.12.028     Document Type: Article

References (182)

1. A.A. Alfadda, and R.M. Sallam Reactive oxygen species in health and disease J. Biomed. Biotechnol. 2012 2012 936486
2. X. Wang, W. Wang, L. Li, G. Perry, H.G. Lee, and X. Zhu Oxidative stress and mitochondrial dysfunction in Alzheimer's disease Biochim. Biophys. Acta 2014 1842 1240 1247
3. H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128
4. L.J. Marnett, J.N. Riggins, and J.D. West Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein J. Clin. Invest. 111 2003 583 593
5. D.C. Liebler Protein damage by reactive electrophiles: targets and consequences Chem. Res. Toxicol. 21 2008 117 128
6. N.A. Porter, S.E. Caldwell, and K.A. Mills Mechanisms of free radical oxidation of unsaturated lipids Lipids 30 1995 277 290
7. E. Niki Lipid peroxidation: physiological levels and dual biological effects Free Radic. Biol. Med. 47 2009 469 484
8. E. Schauenstein Autoxidation of polyunsaturated esters in water: chemical structure and biological activity of the products J. Lipid Res. 8 1967 417 428
9. M.L. Selley, M.R. Bartlett, J.A. McGuiness, A.J. Hapel, and N.G. Ardlie Determination of the lipid peroxidation product trans-4-hydroxy-2-nonenal in biological samples by high-performance liquid chromatography and combined capillary column gas chromatography-negative-ion chemical ionisation mass spectrometry J. Chromatogr. 488 1989 329 340
10. L. Gil, W. Siems, B. Mazurek, J. Gross, P. Schroeder, P. Voss, and T. Grune Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes Free Radic. Res. 40 2006 495 505
11. M.L. Selley Determination of the lipid peroxidation product (E)-4-hydroxy-2-nonenal in clinical samples by gas chromatography-negative-ion chemical ionisation mass spectrometry of the O-pentafluorobenzyl oxime J. Chromatogr. B Biomed. Sci. Appl. 691 1997 263 268
12. U. Herbst, M. Toborek, S. Kaiser, M.P. Mattson, and B. Hennig 4-Hydroxynonenal induces dysfunction and apoptosis of cultured endothelial cells J. Cell. Physiol. 181 1999 295 303
13. W.Y. Ong, A.M. Jenner, N. Pan, C.N. Ong, and B. Halliwell Elevated oxidative stress, iron accumulation around microvessels and increased 4-hydroxynonenal immunostaining in zone 1 of the liver acinus in hypercholesterolemic rabbits Free Radic. Res. 43 2009 241 249
14. H.F. Hoff, J. O'Neil, G.M. Chisolm 3rd, T.B. Cole, O. Quehenberger, H. Esterbauer, and G. Jurgens Modification of low density lipoprotein with 4-hydroxynonenal induces uptake by macrophages Arteriosclerosis 9 1989 538 549
15. R.G. Salomon, K. Kaur, E. Podrez, H.F. Hoff, A.V. Krushinsky, and L.M. Sayre HNE-derived 2-pentylpyrroles are generated during oxidation of LDL, are more prevalent in blood plasma from patients with renal disease or atherosclerosis, and are present in atherosclerotic plaques Chem. Res. Toxicol. 13 2000 557 564
16. S. Srivastava, E. Vladykovskaya, O.A. Barski, M. Spite, K. Kaiserova, J.M. Petrash, S.S. Chung, G. Hunt, B. Dawn, and A. Bhatnagar Aldose reductase protects against early atherosclerotic lesion formation in apolipoprotein E-null mice Circ. Res. 105 2009 793 802
17. X. Zhu, and L.M. Sayre Long-lived 4-oxo-2-enal-derived apparent lysine michael adducts are actually the isomeric 4-ketoamides Chem. Res. Toxicol. 20 2007 165 170
18. X. Zhu, and L.M. Sayre Mass spectrometric evidence for long-lived protein adducts of 4-oxo-2-nonenal Redox Rep. 12 2007 45 49
19. J.J. Galligan, K.L. Rose, W.N. Beavers, S. Hill, K.A. Tallman, W.P. Tansey, and L.J. Marnett Stable histone adduction by 4-oxo-2-nonenal: a potential link between oxidative stress and epigenetics J. Am. Chem. Soc. 136 2014 11864 11866
20. G. Xu, and L.M. Sayre Structural characterization of a 4-hydroxy-2-alkenal-derived fluorophore that contributes to lipoperoxidation-dependent protein cross-linking in aging and degenerative disease Chem. Res. Toxicol. 11 1998 247 251
21. W.H. Zhang, J. Liu, G. Xu, Q. Yuan, and L.M. Sayre Model studies on protein side chain modification by 4-oxo-2-nonenal Chem. Res. Toxicol. 16 2003 512 523
22. Z. Liu, P.E. Minkler, and L.M. Sayre Mass spectroscopic characterization of protein modification by 4-hydroxy-2-(E)-nonenal and 4-oxo-2-(E)-nonenal Chem. Res. Toxicol. 16 2003 901 911
23. T. Oe, J.S. Arora, S.H. Lee, and I.A. Blair A novel lipid hydroperoxide-derived cyclic covalent modification to histone H4 J. Biol. Chem. 278 2003 42098 42105
24. A.K. Yocum, T. Oe, A.L. Yergey, and I.A. Blair Novel lipid hydroperoxide-derived hemoglobin histidine adducts as biomarkers of oxidative stress J. Mass Spectrom. 40 2005 754 764
25. D. Lin, H.G. Lee, Q. Liu, G. Perry, M.A. Smith, and L.M. Sayre 4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal Chem. Res. Toxicol. 18 2005 1219 1231
26. T. Shibata, Y. Shimozu, C. Wakita, N. Shibata, M. Kobayashi, S. Machida, R. Kato, H. Itabe, X. Zhu, L.M. Sayre, and K. Uchida Lipid peroxidation modification of protein generates Nepsilon-(4-oxononanoyl)lysine as a pro-inflammatory ligand J. Biol. Chem. 286 2011 19943 19957
27. P. Spiteller, W. Kern, J. Reiner, and G. Spiteller Aldehydic lipid peroxidation products derived from linoleic acid Biochim. Biophys. Acta 1531 2001 188 208
28. S.H. Lee, and I.A. Blair Characterization of 4-oxo-2-nonenal as a novel product of lipid peroxidation Chem. Res. Toxicol. 13 2000 698 702
29. M. Pollack, T. Oe, S.H. Lee, M.V. Silva Elipe, B.H. Arison, and I.A. Blair Characterization of 2′-deoxycytidine adducts derived from 4-oxo-2-nonenal, a novel lipid peroxidation product Chem. Res. Toxicol. 16 2003 893 900
30. M.V. Williams, S.H. Lee, M. Pollack, and I.A. Blair Endogenous lipid hydroperoxide-mediated DNA-adduct formation in min mice J. Biol. Chem. 281 2006 10127 10133
31. D.P. Ghilarducci, and R.S. Tjeerdema Fate and effects of acrolein Rev. Environ. Contam. Toxicol. 144 1995 95 146
32. M.M. Anderson, S.L. Hazen, F.F. Hsu, and J.W. Heinecke Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. A mechanism for the generation of highly reactive alpha-hydroxy and alpha, beta-unsaturated aldehydes by phagocytes at sites of inflammation J. Clin. Invest. 99 1997 424 432
33. K. Uchida, M. Kanematsu, K. Sakai, T. Matsuda, N. Hattori, Y. Mizuno, D. Suzuki, T. Miyata, N. Noguchi, E. Niki, and T. Osawa Protein-bound acrolein: potential markers for oxidative stress Proc. Natl. Acad. Sci. USA 95 1998 4882 4887
34. R.S. De Woskin Toxicological Review of Acrolein (Cas No. 107-02-08) in Support of Summary Information on the Integrated Risk Information System (Iris) 2003 U.S. Environmental Protection Agency Washington, DC
35. B. Shao, K.D. O'Brien, T.O. McDonald, X. Fu, J.F. Oram, K. Uchida, and J.W. Heinecke Acrolein modifies apolipoprotein A-I in the human artery wall Ann. NY. Acad. Sci. 1043 2005 396 403
36. K. Watanabe, Y. Nakazato, R. Saiki, K. Igarashi, M. Kitada, and I. Ishii Acrolein-conjugated low-density lipoprotein induces macrophage foam cell formation Atherosclerosis 227 2013 51 57
37. M.J. Duryee, L.W. Klassen, C.S. Schaffert, D.J. Tuma, C.D. Hunter, R.P. Garvin, D.R. Anderson, and G.M. Thiele Malondialdehyde-acetaldehyde adduct is the dominant epitope after MDA modification of proteins in atherosclerosis Free Radic. Biol. Med. 49 2010 1480 1486
38. S. Tsimikas, A. Miyanohara, K. Hartvigsen, E. Merki, P.X. Shaw, M.Y. Chou, J. Pattison, M. Torzewski, J. Sollors, T. Friedmann, N.C. Lai, H.K. Hammond, G.S. Getz, C.A. Reardon, A.C. Li, C.L. Banka, and J.L. Witztum Human oxidation-specific antibodies reduce foam cell formation and atherosclerosis progression J. Am. Coll. Cardiol. 58 2011 1715 1727
39. M.F. Lopes-Virella, K.J. Hunt, N.L. Baker, G. Virella, T. Moritz, and V. Investigators The levels of MDA-LDL in circulating immune complexes predict myocardial infarction in the VADT study Atherosclerosis 224 2012 526 531
40. S. Ehara, M. Ueda, T. Naruko, K. Haze, A. Itoh, M. Otsuka, R. Komatsu, T. Matsuo, H. Itabe, T. Takano, Y. Tsukamoto, M. Yoshiyama, K. Takeuchi, J. Yoshikawa, and A.E. Becker Elevated levels of oxidized low density lipoprotein show a positive relationship with the severity of acute coronary syndromes Circulation 103 2001 1955 1960
41. A.D. Watson, G. Subbanagounder, D.S. Welsbie, K.F. Faull, M. Navab, M.E. Jung, A.M. Fogelman, and J.A. Berliner Structural identification of a novel pro-inflammatory epoxyisoprostane phospholipid in mildly oxidized low density lipoprotein J. Biol. Chem. 274 1999 24787 24798
42. G. Subbanagounder, N. Leitinger, D.C. Schwenke, J.W. Wong, H. Lee, C. Rizza, A.D. Watson, K.F. Faull, A.M. Fogelman, and J.A. Berliner Determinants of bioactivity of oxidized phospholipids. Specific oxidized fatty acyl groups at the sn-2 position Arterioscler. Thromb. Vasc. Biol. 20 2000 2248 2254
43. S. Tsimikas, E.S. Brilakis, E.R. Miller, J.P. McConnell, R.J. Lennon, K.S. Kornman, J.L. Witztum, and P.B. Berger Oxidized phospholipids, Lp(a) lipoprotein, and coronary artery disease N. Engl. J. Med. 353 2005 46 57
44. J.A. Berliner, and A.D. Watson A role for oxidized phospholipids in atherosclerosis N. Engl. J. Med. 353 2005 9 11
45. Y. Jin, and T.M. Penning Aldo-keto reductases and bioactivation/detoxication Annu. Rev. Pharmacol. Toxicol. 47 2007 263 292
46. S.S. Hoog, J.E. Pawlowski, P.M. Alzari, T.M. Penning, and M. Lewis Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily Proc. Natl. Acad. Sci. USA 91 1994 2517 2521
47. K.M. Bohren, B. Bullock, B. Wermuth, and K.H. Gabbay The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases J. Biol. Chem. 264 1989 9547 9551
48. J. Fujii, R. Hamaoka, A. Matsumoto, T. Fujii, Y. Yamaguchi, M. Egashira, O. Miyoshi, N. Niikawa, and N. Taniguchi The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33 → p32 Cytogenet. Cell Genet. 84 1999 230 232
49. O.A. Barski, K.H. Gabbay, and K.M. Bohren Characterization of the human aldehyde reductase gene and promoter Genomics 60 1999 188 198
50. M. Pratt-Hyatt, A.J. Lickteig, and C.D. Klaassen Tissue distribution, ontogeny, and chemical induction of aldo-keto reductases in mice Drug Metab. Dispos. 41 2013 1480 1487
51. J.A. Watson, J.A. Hayashi, E. Schuytema, and C.C. Doughty Identification of reduced nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase in a Rhodotorula strain J. Bacteriol. 100 1969 110 116
52. A.S. Beedle, H.H. Rees, and T.W. Goodwin Some properties and a suggested reclassification of mevaldate reductase Biochem. J. 139 1974 205 209
53. K.H. Gabbay, K.M. Bohren, R. Morello, T. Bertin, J. Liu, and P. Vogel Ascorbate synthesis pathway: dual role of ascorbate in bone homeostasis J. Biol. Chem. 285 2010 19510 19520
54. M. Takahashi, S. Miyata, J. Fujii, Y. Inai, S. Ueyama, M. Araki, T. Soga, R. Fujinawa, C. Nishitani, S. Ariki, T. Shimizu, T. Abe, Y. Ihara, M. Nishikimi, Y. Kozutsumi, N. Taniguchi, and Y. Kuroki In vivo role of aldehyde reductase Biochim. Biophys. Acta 2012 1820 1787 1796
55. T. Kurahashi, M. Kwon, T. Homma, Y. Saito, J. Lee, M. Takahashi, K.I. Yamada, S. Miyata, and J. Fujii Reductive detoxification of acrolein as a potential role for aldehyde reductase (AKR1A) in mammals Biochem. Biophys. Res. Commun. 2014
56. 2; and 4-hydroxynonenal-induced cytotoxicity in human 1321N1 astrocytoma cells Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 29 2013 273 276
57. T.G. Flynn, and N.C. Green The aldo-keto reductases: an overview Adv. Exp. Med. Biol. 328 1993 251 257
58. O. Gallego, F.X. Ruiz, A. Ardevol, M. Dominguez, R. Alvarez, A.R. de Lera, C. Rovira, J. Farres, I. Fita, and X. Pares Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10 Proc. Natl. Acad. Sci. USA 104 2007 20764 20769
59. J.M. Petrash All in the family: aldose reductase and closely related aldo-keto reductases Cell. Mol. Life Sci. 61 2004 737 749
60. J.M. Petrash, T.M. Harter, S. Srivastava, A. Chandra, A. Bhatnagar, and S.K. Srivastava Structure-function studies of FR-1. A growth factor-inducible aldo-keto reductase Adv. Exp. Med. Biol. 463 1999 435 443
61. S.K. Srivastava, B. Das, G.A. Hair, R.W. Gracy, S. Awasthi, N.H. Ansari, and J.M. Petrash Interrelationships among human aldo-keto reductases: immunochemical, kinetic and structural properties Biochim. Biophys. Acta 840 1985 334 343
62. S. Srivastava, S.J. Watowich, J.M. Petrash, S.K. Srivastava, and A. Bhatnagar Structural and kinetic determinants of aldehyde reduction by aldose reductase Biochemistry 38 1999 42 54
63. S. Srivastava, A. Chandra, A. Bhatnagar, S.K. Srivastava, and N.H. Ansari Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase Biochem. Biophys. Res. Commun. 217 1995 741 746
64. S. Srivastava, D.J. Conklin, S.Q. Liu, N. Prakash, P.J. Boor, S.K. Srivastava, and A. Bhatnagar Identification of biochemical pathways for the metabolism of oxidized low-density lipoprotein derived aldehyde-4-hydroxy trans-2-nonenal in vascular smooth muscle cells Atherosclerosis 158 2001 339 350
65. S. Srivastava, M. Spite, J.O. Trent, M.B. West, Y. Ahmed, and A. Bhatnagar Aldose reductase-catalyzed reduction of aldehyde phospholipids J. Biol. Chem. 279 2004 53395 53406
66. M. Spite, S.P. Baba, Y. Ahmed, O.A. Barski, K. Nijhawan, J.M. Petrash, A. Bhatnagar, and S. Srivastava Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes Biochem. J. 405 2007 95 105
67. H.L. Rittner, V. Hafner, P.A. Klimiuk, L.I. Szweda, J.J. Goronzy, and C.M. Weyand Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis J. Clin. Invest. 103 1999 1007 1013
68. P.K. Goel, M. Shahi, A.K. Agarwal, S. Srivastava, and P.K. Seth Platelet aggregability and occurrence of restenosis following coronary angioplasty Int. J. Cardiol. 60 1997 227 231
69. J. Ruef, S.Q. Liu, C. Bode, M. Tocchi, S. Srivastava, M.S. Runge, and A. Bhatnagar Involvement of aldose reductase in vascular smooth muscle cell growth and lesion formation after arterial injury Arterioscler. Thromb. Vasc. Biol. 20 2000 1745 1752
70. K.V. Ramana, A. Bhatnagar, S. Srivastava, U.C. Yadav, S. Awasthi, Y.C. Awasthi, and S.K. Srivastava 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. 281 2006 17652 17660
71. C. Taragnat, M. Berger, and C. Jean Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens J. Reprod. Fertil. 83 1988 835 842
72. E.T. Lau, D. Cao, C. Lin, S.K. Chung, and S.S. Chung Tissue-specific expression of two aldose reductase-like genes in mice: abundant expression of mouse vas deferens protein and fibroblast growth factor-regulated protein in the adrenal gland Biochem. J. 312 Pt. 2 1995 609 615
73. C. Aigueperse, A. Martinez, A.M. Lefrancois-Martinez, G. Veyssiere, and C.I. Jean Cyclic AMP regulates expression of the gene coding for a mouse vas deferens protein related to the aldo-keto reductase superfamily in human and murine adrenocortical cells J. Endocrinol. 160 1999 147 154
74. C. Baumann, B. Davies, M. Peters, U. Kaufmann-Reiche, M. Lessl, and F. Theuring AKR1B7 (mouse vas deferens protein) is dispensable for mouse development and reproductive success Reproduction 134 2007 97 109
75. W.N. Jagoe, K. Howe, S.C. O'Brien, and J. Carroll Identification of a role for a mouse sperm surface aldo-keto reductase (AKR1B7) and its human analogue in the detoxification of the reactive aldehyde, acrolein Andrologia 45 2013 326 331
76. A. Martinez, C. Aigueperse, P. Val, M. Dussault, C. Tournaire, M. Berger, G. Veyssiere, C. Jean, and A. Lefrancois Martinez Physiological functions and hormonal regulation of mouse vas deferens protein (AKR1B7) in steroidogenic tissues Chem. Biol. Interact. 130-132 2001 903 917
77. J. Tirard, J. Gout, A.M. Lefrancois-Martinez, A. Martinez, M. Begeot, and D. Naville A novel inhibitory protein in adipose tissue, the aldo-keto reductase AKR1B7: its role in adipogenesis Endocrinology 148 2007 1996 2005
78. P. Kotokorpi, C. Gardmo, C.S. Nystrom, and A. Mode Activation of the glucocorticoid receptor or liver X receptors interferes with growth hormone-induced akr1b7 gene expression in rat hepatocytes Endocrinology 145 2004 5704 5713
79. S. Endo, T. Matsunaga, A. Fujita, K. Tajima, O. El-Kabbani, and A. Hara Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal Biol. Pharm. Bull. 33 2010 1886 1890
80. E. Pastel, J.C. Pointud, F. Volat, A. Martinez, and A.M. Lefrancois-Martinez Aldo-keto reductases 1B in endocrinology and metabolism Front. Pharmacol. 3 2012 148
81. P.J. Donohue, G.F. Alberts, B.S. Hampton, and J.A. Winkles A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase J. Biol. Chem. 269 1994 8604 8609
82. A. Joshi, S. Rajput, C. Wang, J. Ma, and D. Cao Murine aldo-keto reductase family 1 subfamily B: identification of AKR1B8 as an ortholog of human AKR1B10 Biol. Chem. 391 2010 1371 1378
83. Y. Shen, L. Zhong, S. Johnson, and D. Cao Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds Chem. Biol. Interact. 191 2011 192 198
84. H.J. Martin, and E. Maser Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes Chem. Biol. Interact. 178 2009 145 150
85. M.E. Burczynski, G.R. Sridhar, N.T. Palackal, and T.M. Penning The reactive oxygen species- and michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the α, β-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene J. Biol. Chem. 276 2001 2890 2897
86. M. Khanna, K.N. Qin, R.W. Wang, and K.C. Cheng Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases J. Biol. Chem. 270 1995 20162 20168
87. K. Matsuura, H. Shiraishi, A. Hara, K. Sato, Y. Deyashiki, M. Ninomiya, and S. Sakai Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity J. Biochem. 124 1998 940 946
88. Y. Tian, L. Zhao, H. Zhang, X. Liu, L. Zhao, X. Zhao, Y. Li, and J. Li AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression Diagn. Pathol. 9 2014 42
89. R.C. Lyon, D. Li, G. McGarvie, and E.M. Ellis Aldo-keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells Neurochem. Int. 62 2013 113 121
90. T. Leicher, R. Bahring, D. Isbrandt, and O. Pongs Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium channel J. Biol. Chem. 273 1998 35095 35101
91. T.M. Penning The aldo-keto reductases (AKRs): overview Chem. Biol. Interact. 2014
92. S.M. Tipparaju, S.Q. Liu, O.A. Barski, and A. Bhatnagar NADPH binding to beta-subunit regulates inactivation of voltage-gated K(+) channels Biochem. Biophys. Res. Commun. 359 2007 269 276
93. S.M. Tipparaju, X.P. Li, P.J. Kilfoil, B. Xue, V.N. Uversky, A. Bhatnagar, and O.A. Barski Interactions between the C-terminus of Kv1.5 and Kvbeta regulate pyridine nucleotide-dependent changes in channel gating Pflugers Arch. 463 2012 799 818
94. S.M. Tipparaju, O.A. Barski, S. Srivastava, and A. Bhatnagar Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel Biochemistry 47 2008 8840 8854
95. Z. Xie, O.A. Barski, J. Cai, A. Bhatnagar, and S.M. Tipparaju Catalytic reduction of carbonyl groups in oxidized PAPC by Kvbeta2 (AKR6) Chem. Biol. Interact. 191 2011 255 260
96. O.A. Barski, S.M. Tipparaju, and A. Bhatnagar Kinetics of nucleotide binding to the beta-subunit (AKR6A2) of the voltage-gated potassium (Kv) channel Chem. Biol. Interact. 178 2009 165 170
97. A. Hinshelwood, G. McGarvie, and E.M. Ellis Substrate specificity of mouse aldo-keto reductase AKR7A5 Chem. Biol. Interact. 143-144 2003 263 269
98. L.S. Ireland, D.J. Harrison, G.E. Neal, and J.D. Hayes Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase Biochem. J. 332 Pt 1 1998 21 34
99. L.P. Knight, T. Primiano, J.D. Groopman, T.W. Kensler, and T.R. Sutter CDNA cloning, expression and activity of a second human aflatoxin B1-metabolizing member of the aldo-keto reductase superfamily, AKR7A3 Carcinogenesis 20 1999 1215 1223
100. V.P. Kelly, E.M. Ellis, M.M. Manson, S.A. Chanas, G.J. Moffat, R. McLeod, D.J. Judah, G.E. Neal, and J.D. Hayes Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver Cancer Res. 60 2000 957 969
101. V.P. Kelly, L.S. Ireland, E.M. Ellis, and J.D. Hayes Purification from rat liver of a novel constitutively expressed member of the aldo-keto reductase 7 family that is widely distributed in extrahepatic tissues Biochem. J. 348 Pt. 2 2000 389 400
102. A. Hinshelwood, G. McGarvie, and E. Ellis Characterisation of a novel mouse liver aldo-keto reductase AKR7A5 FEBS Lett. 523 2002 213 218
103. E.M. Ellis, and J.D. Hayes Substrate specificity of an aflatoxin-metabolizing aldehyde reductase Biochem. J. 312 Pt 2 1995 535 541
104. J.D. Hayes, D.J. Judah, and G.E. Neal Resistance to aflatoxin B1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin Cancer Res. 53 1993 3887 3894
105. E.M. Ellis, D.J. Judah, G.E. Neal, and J.D. Hayes An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases Proc. Natl. Acad. Sci. USA 90 1993 10350 10354
106. R. Gardner, S. Kazi, and E.M. Ellis Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase Toxicol. Lett. 148 2004 65 72
107. R.C. Lyon, S.M. Johnston, D.G. Watson, G. McGarvie, and E.M. Ellis Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2 J. Biol. Chem. 282 2007 25986 25992
108. T. O'Connor, L.S. Ireland, D.J. Harrison, and J.D. Hayes Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members Biochem. J. 343 Pt. 2 1999 487 504
109. M.J. Picklo Sr., S.J. Olson, J.D. Hayes, W.R. Markesbery, and T.J. Montine Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease Brain Res. 916 2001 229 238
110. D. Li, and E.M. Ellis Inducible protection of human astrocytoma 1321N1 cells against hydrogen peroxide and aldehyde toxicity by 7-hydroxycoumarin is associated with the upregulation of aldo-keto reductases Neurotoxicology 33 2012 1368 1374
111. D. Li, M. Ferrari, and E.M. Ellis Human aldo-keto reductase AKR7A2 protects against the cytotoxicity and mutagenicity of reactive aldehydes and lowers intracellular reactive oxygen species in hamster V79-4 cells Chem. Biol. Interact. 195 2012 25 34
112. D. Li, A. Hinshelwood, R. Gardner, G. McGarvie, and E.M. Ellis Mouse aldo-keto reductase AKR7A5 protects V79 cells against 4-hydroxynonenal-induced apoptosis Toxicology 226 2006 172 180
113. D. Li, and E.M. Ellis Aldo-keto reductase 7A5 (AKR7A5) attenuates oxidative stress and reactive aldehyde toxicity in V79-4 cells Toxicol. In Vitro 28 2014 707 714
114. V. Vasiliou, A. Bairoch, K.F. Tipton, and D.W. Nebert Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping Pharmacogenetics 9 1999 421 434
115. N.A. Sophos, and V. Vasiliou Aldehyde dehydrogenase gene superfamily: the 2002 update Chem. Biol. Interact. 143-144 2003 2002 5 22
116. N.A. Sophos, A. Pappa, T.L. Ziegler, and V. Vasiliou Aldehyde dehydrogenase gene superfamily: the 2000 update Chem. Biol. Interact. 130-132 2001 2000 323 337
117. T.L. Ziegler, and V. Vasiliou Aldehyde dehydrogenase gene superfamily. The 1998 update Adv. Exp. Med. Biol. 463 1999 1998 255 263
118. V. Vasiliou, A. Pappa, and T. Estey Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism Drug Metab. Rev. 36 2004 279 299
119. C. Ginestier, M.H. Hur, E. Charafe-Jauffret, F. Monville, J. Dutcher, M. Brown, J. Jacquemier, P. Viens, C.G. Kleer, S. Liu, A. Schott, D. Hayes, D. Birnbaum, M.S. Wicha, and G. Dontu ALDH1 is a marker of normal and malignant human mammary stem cells and a predictor of poor clinical outcome Cell Stem Cell 1 2007 555 567
120. E. Charafe-Jauffret, C. Ginestier, F. Iovino, C. Tarpin, M. Diebel, B. Esterni, G. Houvenaeghel, J.M. Extra, F. Bertucci, J. Jacquemier, L. Xerri, G. Dontu, G. Stassi, Y. Xiao, S.H. Barsky, D. Birnbaum, P. Viens, and M.S. Wicha Aldehyde dehydrogenase 1-positive cancer stem cells mediate metastasis and poor clinical outcome in inflammatory breast cancer Clin. Cancer Res. 16 2010 45 55
121. S. Deng, X. Yang, H. Lassus, S. Liang, S. Kaur, Q. Ye, C. Li, L.P. Wang, K.F. Roby, S. Orsulic, D.C. Connolly, Y. Zhang, K. Montone, R. Butzow, G. Coukos, and L. Zhang Distinct expression levels and patterns of stem cell marker, aldehyde dehydrogenase isoform 1 (ALDH1), in human epithelial cancers PLoS One 5 2010 e10277
122. C.N. Landen Jr., B. Goodman, A.A. Katre, A.D. Steg, A.M. Nick, R.L. Stone, L.D. Miller, P.V. Mejia, N.B. Jennings, D.M. Gershenson, R.C. Bast Jr., R.L. Coleman, G. Lopez-Berestein, and A.K. Sood Targeting aldehyde dehydrogenase cancer stem cells in ovarian cancer Mol. Cancer Ther. 9 2010 3186 3199
123. G. King, and R. Holmes Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens J. Exp. Zool. 282 1998 12 17
124. S. Choudhary, T. Xiao, L.A. Vergara, S. Srivastava, D. Nees, J. Piatigorsky, and N.H. Ansari Role of aldehyde dehydrogenase isozymes in the defense of rat lens and human lens epithelial cells against oxidative stress Invest. Ophthalmol. Vis. Sci. 46 2005 259 267
125. T. Xiao, M. Shoeb, M.S. Siddiqui, M. Zhang, K.V. Ramana, S.K. Srivastava, V. Vasiliou, and N.H. Ansari Molecular cloning and oxidative modification of human lens ALDH1A1: implication in impaired detoxification of lipid aldehydes J. Toxicol. Environ. Health A 72 2009 577 584
126. F. Jiang, Q. Qiu, A. Khanna, N.W. Todd, J. Deepak, L. Xing, H. Wang, Z. Liu, Y. Su, S.A. Stass, and R.L. Katz Aldehyde dehydrogenase 1 is a tumor stem cell-associated marker in lung cancer Mol. Cancer Res. 7 2009 330 338
127. B. Chang, G. Liu, F. Xue, D.G. Rosen, L. Xiao, X. Wang, and J. Liu ALDH1 expression correlates with favorable prognosis in ovarian cancers Mod. Pathol. 22 2009 817 823
128. Z.A. Rasheed, J. Yang, Q. Wang, J. Kowalski, I. Freed, C. Murter, S.M. Hong, J.B. Koorstra, N.V. Rajeshkumar, X. He, M. Goggins, C. Iacobuzio-Donahue, D.M. Berman, D. Laheru, A. Jimeno, M. Hidalgo, A. Maitra, and W. Matsui Prognostic significance of tumorigenic cells with mesenchymal features in pancreatic adenocarcinoma J. Natl Cancer Inst. 102 2010 340 351
129. Y. Su, Q. Qiu, X. Zhang, Z. Jiang, Q. Leng, Z. Liu, S.A. Stass, and F. Jiang Aldehyde dehydrogenase 1 A1-positive cell population is enriched in tumor-initiating cells and associated with progression of bladder cancer Cancer Epidemiol. Biomarkers Prev. 19 2010 327 337
130. T. Li, Y. Su, Y. Mei, Q. Leng, B. Leng, Z. Liu, S.A. Stass, and F. Jiang ALDH1A1 is a marker for malignant prostate stem cells and predictor of prostate cancer patients' outcome Lab. Invest. 90 2010 234 244
131. J.S. Moreb, D. Ucar, S. Han, J.K. Amory, A.S. Goldstein, B. Ostmark, and L.J. Chang The enzymatic activity of human aldehyde dehydrogenases 1A2 and 2 (ALDH1A2 and ALDH2) is detected by Aldefluor, inhibited by diethylaminobenzaldehyde and has significant effects on cell proliferation and drug resistance Chem. Biol. Interact. 195 2012 52 60
132. N.E. Sladek, R. Kollander, L. Sreerama, and D.T. Kiang Cellular levels of aldehyde dehydrogenases (ALDH1A1 and ALDH3A1) as predictors of therapeutic responses to cyclophosphamide-based chemotherapy of breast cancer: a retrospective study. Rational individualization of oxazaphosphorine-based cancer chemotherapeutic regimens Cancer Chemother. Pharmacol. 49 2002 309 321
133. S. Vakevainen, J. Tillonen, D.P. Agarwal, N. Srivastava, and M. Salaspuro High salivary acetaldehyde after a moderate dose of alcohol in ALDH2-deficient subjects: strong evidence for the local carcinogenic action of acetaldehyde Alcohol. Clin. Exp. Res. 24 2000 873 877
134. I. Ohsawa, K. Nishimaki, Y. Murakami, Y. Suzuki, M. Ishikawa, and S. Ohta Age-dependent neurodegeneration accompanying memory loss in transgenic mice defective in mitochondrial aldehyde dehydrogenase 2 activity J. Neurosci. 28 2008 6239 6249
135. C.H. Chen, J.C. Ferreira, E.R. Gross, and D. Mochly-Rosen Targeting aldehyde dehydrogenase 2: new therapeutic opportunities Physiol. Rev. 94 2014 1 34
136. C.G. Steinmetz, P. Xie, H. Weiner, and T.D. Hurley Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion Structure 5 1997 701 711
137. D.W. Crabb, M. Matsumoto, D. Chang, and M. You Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology Proc. Nutr. Soc. 63 2004 49 63
138. H.R. Thomasson, H.J. Edenberg, D.W. Crabb, X.L. Mai, R.E. Jerome, T.K. Li, S.P. Wang, Y.T. Lin, R.B. Lu, and S.J. Yin Alcohol and aldehyde dehydrogenase genotypes and alcoholism in Chinese men Am. J. Hum. Genet. 48 1991 677 681
139. X.J. Luo, B. Liu, Q.L. Ma, and J. Peng Mitochondrial aldehyde dehydrogenase, a potential drug target for protection of heart and brain from ischemia/reperfusion injury Curr. Drug Targets 2014
140. V.O. Zambelli, E.R. Gross, C.H. Chen, V.P. Gutierrez, Y. Cury, and D. Mochly-Rosen Aldehyde dehydrogenase-2 regulates nociception in rodent models of acute inflammatory pain Sci. Transl. Med. 6 2014 251ra118
141. L.R. Hiraoka, L. Hsu, and C.L. Hsieh Assignment of ALDH3 to human chromosome 17p11.2 and ALDH5 to human chromosome 9p13 Genomics 25 1995 323 325
142. A. Pappa, C. Chen, Y. Koutalos, A.J. Townsend, and V. Vasiliou Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage Free Radic. Biol. Med. 34 2003 1178 1189
143. R.A. Canuto, G. Muzio, M. Ferro, M. Maggiora, R. Federa, A.M. Bassi, R. Lindahl, and M.U. Dianzani Inhibition of class-3 aldehyde dehydrogenase and cell growth by restored lipid peroxidation in hepatoma cell lines Free Radic. Biol. Med. 26 1999 333 340
144. L. Uma, J. Hariharan, Y. Sharma, and D. Balasubramanian Corneal aldehyde dehydrogenase displays antioxidant properties Exp. Eye Res. 63 1996 117 120
145. N. Lassen, A. Pappa, W.J. Black, J.V. Jester, B.J. Day, E. Min, and V. Vasiliou Antioxidant function of corneal ALDH3A1 in cultured stromal fibroblasts Free Radic. Biol. Med. 41 2006 1459 1469
146. J.S. Wang, Q. Fang, D.J. Sun, J. Chen, X.L. Zhou, G.W. Lin, H.Z. Lu, and J. Fei Genetic modification of hematopoietic progenitor cells for combined resistance to 4-hydroperoxycyclophosphamide, vincristine, and daunorubicin Acta Pharmacol. Sin. 22 2001 949 955
147. R.A. Canuto, M. Maggiora, A. Trombetta, G. Martinasso, and G. Muzio Aldehyde dehydrogenase 3 expression is decreased by clofibrate via PPAR gamma induction in JM2 rat hepatoma cell line Chem. Biol. Interact. 143-144 2003 29 35
148. A. Pappa, D. Brown, Y. Koutalos, J. DeGregori, C. White, and V. Vasiliou Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells J. Biol. Chem. 280 2005 27998 28006
149. G. Muzio, A. Trombetta, M. Maggiora, G. Martinasso, V. Vasiliou, N. Lassen, and R.A. Canuto Arachidonic acid suppresses growth of human lung tumor A549 cells through down-regulation of ALDH3A1 expression Free Radic. Biol. Med. 40 2006 1929 1938
150. M. Patel, L. Lu, D.S. Zander, L. Sreerama, D. Coco, and J.S. Moreb ALDH1A1 and ALDH3A1 expression in lung cancers: correlation with histologic type and potential precursors Lung Cancer 59 2008 340 349
151. M. Gasparetto, S. Sekulovic, C. Brocker, P. Tang, A. Zakaryan, P. Xiang, F. Kuchenbauer, M. Wen, K. Kasaian, M.F. Witty, P. Rosten, Y. Chen, S. Imren, G. Duester, D.C. Thompson, R.K. Humphries, V. Vasiliou, and C. Smith Aldehyde dehydrogenases are regulators of hematopoietic stem cell numbers and B-cell development Exp. Hematol. 40 2012 318-329.e312
152. J.H. Jang, S. Bruse, Y. Liu, V. Duffy, C. Zhang, N. Oyamada, S. Randell, A. Matsumoto, D.C. Thompson, Y. Lin, V. Vasiliou, Y. Tesfaigzi, and T. Nyunoya Aldehyde dehydrogenase 3A1 protects airway epithelial cells from cigarette smoke-induced DNA damage and cytotoxicity Free Radic. Biol. Med. 68 2014 80 86
153. A. Pappa, T. Estey, R. Manzer, D. Brown, and V. Vasiliou Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea Biochem. J. 376 2003 615 623
154. T. Estey, J. Piatigorsky, N. Lassen, and V. Vasiliou ALDH3A1: a corneal crystallin with diverse functions Exp. Eye Res. 84 2007 3 12
155. W. Black, Y. Chen, A. Matsumoto, D.C. Thompson, N. Lassen, A. Pappa, and V. Vasiliou Molecular mechanisms of ALDH3A1-mediated cellular protection against 4-hydroxy-2-nonenal Free Radic. Biol. Med. 52 2012 1937 1944
156. A.J. Townsend, S. Leone-Kabler, R.L. Haynes, Y. Wu, L. Szweda, and K.D. Bunting Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells Chem. Biol. Interact. 130-132 2001 261 273
157. V. Vasiliou, S.F. Reuter, C.A. Kozak, and D.W. Nebert Mouse dioxin-inducible cytosolic aldehyde dehydrogenase-3: AHD4 cDNA sequence, genetic mapping, and differences in mRNA levels Pharmacogenetics 3 1993 281 290
158. M.K. Korkalainen, A.R. Torronen, and S.O. Karenlampi Comparison of expression of aldehyde dehydrogenase 3 and CYP1A1 in dominant and recessive aryl hydrocarbon hydroxylase-deficient mutant mouse hepatoma cells Chem. Biol. Interact. 94 1995 121 134
159. J. Davis, D. Davis, B. Norman, and J. Piatigorsky Gene expression of the mouse corneal crystallin Aldh3a1: activation by Pax6, Oct1, and p300 Invest. Ophthalmol. Vis. Sci. 49 2008 1814 1826
160. J. Yan, J. De Melo, J.C. Cutz, T. Aziz, and D. Tang Aldehyde dehydrogenase 3A1 associates with prostate tumorigenesis Br. J. Cancer 110 2014 2593 2603
161. M.D. Boleda, N. Saubi, J. Farres, and X. Pares Physiological substrates for rat alcohol dehydrogenase classes: aldehydes of lipid peroxidation, omega-hydroxyfatty acids, and retinoids Arch. Biochem. Biophys. 307 1993 85 90
162. W.F. Bosron, and T.K. Li Catalytic properties of human liver alcohol dehydrogenase isoenzymes Enzyme 37 1987 19 28
163. M. Yasunami, I. Kikuchi, D. Sarapata, and A. Yoshida The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome Genomics 7 1990 152 158
164. J.C. Burnell, L.G. Carr, F.E. Dwulet, H.J. Edenberg, T.K. Li, and W.F. Bosron The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding Biochem. Biophys. Res. Commun. 146 1987 1127 1133
165. S. Harada Classification of alcohol metabolizing enzymes and polymorphisms - specificity in Japanese Nihon Arukoru Yakubutsu Igakkai Zasshi 36 2001 85 106
166. O. Danielsson, J. Shafqat, M. Estonius, and H. Jornvall Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization Eur. J. Biochem. 225 1994 1081 1088
167. K.K. Hintz, D.P. Relling, J.T. Saari, A.J. Borgerding, J. Duan, B.H. Ren, K. Kato, P.N. Epstein, and J. Ren Cardiac overexpression of alcohol dehydrogenase exacerbates cardiac contractile dysfunction, lipid peroxidation, and protein damage after chronic ethanol ingestion Alcohol. Clin. Exp. Res. 27 2003 1090 1098
168. J.O. Hoog, M. Estonius, and O. Danielsson Site-directed mutagenesis and enzyme properties of mammalian alcohol dehydrogenases correlated with their tissue distribution EXS 71 1994 301 309
169. R. Kaiser, M.R. Fernandez, X. Pares, and H. Jornvall Origin of the human alcohol dehydrogenase system: implications from the structure and properties of the octopus protein Proc. Natl. Acad. Sci. USA 90 1993 11222 11226
170. R.W. Cotton, and D. Goldman Review of the molecular biology of the human alcohol dehydrogenase genes and gene products Adv. Alcohol Subst. Abuse 7 1988 171 182
171. L.G. Carr, Y. Xu, W.H. Ho, and H.J. Edenberg Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit Alcohol. Clin. Exp. Res. 13 1989 594 596
172. Y. Matsuo, R. Yokoyama, and S. Yokoyama The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide Eur. J. Biochem. 183 1989 317 320
173. D. Hasin, E. Aharonovich, X. Liu, Z. Mamman, K. Matseoane, Lg Carr, and T.K. Li Alcohol dependence symptoms and alcohol dehydrogenase 2 polymorphism: Israeli Ashkenazis, Sephardics, and recent Russian immigrants Alcohol. Clin. Exp. Res. 26 2002 1315 1321
174. L. Chrostek, W. Jelski, M. Szmitkowski, and Z. Puchalski Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the human pancreas Dig. Dis. Sci. 48 2003 1230 1233
175. L. Chrostek, W. Jelski, M. Szmitkowski, and Z. Puchalski Gender-related differences in hepatic activity of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in humans J. Clin. Lab. Anal. 17 2003 93 96
176. D. Yin, and Y. Brunk Carbonyl Toxification Hypothesis of Biological Aging 1995 CRC Press Inc. Boca Raton, FL
177. A. Okado-Matsumoto, and I. Fridovich The role of alpha, beta-dicarbonyl compounds in the toxicity of short chain sugars J. Biol. Chem. 275 2000 34853 34857
178. K.M. Humphries, Y. Yoo, and L.I. Szweda Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal Biochemistry 37 1998 552 557
179. A. Bhatnagar Electrophysiological effects of 4-hydroxynonenal, an aldehydic product of lipid peroxidation, on isolated rat ventricular myocytes Circ. Res. 76 1995 293 304
180. S.G. Codreanu, J.C. Ullery, J. Zhu, K.A. Tallman, W.N. Beavers, N.A. Porter, L.J. Marnett, B. Zhang, and D.C. Liebler Alkylation damage by lipid electrophiles targets functional protein systems Mol. Cell. Proteomics 13 2014 849 859
181. F.X. Ruiz, A. Moro, O. Gallego, A. Ardevol, C. Rovira, J.M. Petrash, X. Pares, and J. Farres Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde Chem. Biol. Interact. 191 2011 199 205
182. K.V. Ramana, B.L. Dixit, S. Srivastava, G.K. Balendiran, S.K. Srivastava, and A. Bhatnagar Selective recognition of glutathiolated aldehydes by aldose reductase Biochemistry 39 2000 12172 12180