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BioMed Research International
Volume 2015 (2015), Article ID 174050, 9 pages
http://dx.doi.org/10.1155/2015/174050
Review Article

Glu504Lys Single Nucleotide Polymorphism of Aldehyde Dehydrogenase 2 Gene and the Risk of Human Diseases

1Department of Bioengineering, Harbin Institute of Technology at Weihai, Shandong 264209, China
2Department of Mathematics, Harbin Institute of Technology at Weihai, Shandong 264209, China

Received 7 May 2015; Revised 29 July 2015; Accepted 19 August 2015

Academic Editor: Jing Zhang

Copyright © 2015 Yan Zhao and Chuancai Wang. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. T. Isse, K. Matsuno, T. Oyama, K. Kitagawa, and T. Kawamoto, “Aldehyde dehydrogenase 2 gene targeting mouse lacking enzyme activity shows high acetaldehyde level in blood, brain, and liver after ethanol gavages,” Alcoholism: Clinical and Experimental Research, vol. 29, no. 11, pp. 1959–1964, 2005. View at Publisher · View at Google Scholar · View at Scopus
  2. A. A. Klyosov, L. G. Rashkovetsky, M. K. Tahir, and W.-M. Keung, “Possible role of liver cytosolic and mitochondrial aldehyde dehydrogenases in acetaldehyde metabolism,” Biochemistry, vol. 35, no. 14, pp. 4445–4456, 1996. View at Publisher · View at Google Scholar · View at Scopus
  3. D. W. Crabb, H. J. Edenberg, W. F. Bosron, and T.-K. Li, “Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant,” The Journal of Clinical Investigation, vol. 83, no. 1, pp. 314–316, 1989. View at Publisher · View at Google Scholar · View at Scopus
  4. H. E. Goedde, D. P. Agarwal, S. Harada et al., “Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity,” The American Journal of Human Genetics, vol. 35, no. 4, pp. 769–772, 1983. View at Google Scholar · View at Scopus
  5. K. Kamino, K. Nagasaka, M. Imagawa et al., “Deficiency in mitochondrial aldehyde dehydrogenase increases the risk for late-onset Alzheimer's disease in the Japanese population,” Biochemical and Biophysical Research Communications, vol. 273, no. 1, pp. 192–196, 2000. View at Publisher · View at Google Scholar · View at Scopus
  6. Q. Wang, S. Zhou, L. Wang et al., “ALDH2 rs671 polymorphism and coronary heart disease risk among asian populations: a meta-analysis and meta-regression,” DNA and Cell Biology, vol. 32, no. 7, pp. 393–399, 2013. View at Publisher · View at Google Scholar · View at Scopus
  7. J.-Y. Gu and L.-W. Li, “ALDH2 Glu504Lys polymorphism and susceptibility to coronary artery disease and myocardial infarction in East Asians: a meta-analysis,” Archives of Medical Research, vol. 45, no. 1, pp. 76–83, 2014. View at Publisher · View at Google Scholar · View at Scopus
  8. A. Yokoyama, T. Muramatsu, T. Ohmori et al., “Alcohol-related cancers and aldehyde dehydrogenase-2 in Japanese alcoholics,” Carcinogenesis, vol. 19, no. 8, pp. 1383–1387, 1998. View at Publisher · View at Google Scholar · View at Scopus
  9. V. Vasiliou and D. W. Nebert, “Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family,” Human Genomics, vol. 2, no. 2, pp. 138–143, 2005. View at Google Scholar · View at Scopus
  10. S. Futterman, “Enzymatic oxidation of vitamin A aldehyde to vitamin A acid,” The Journal of Biological Chemistry, vol. 237, pp. 677–680, 1962. View at Google Scholar · View at Scopus
  11. M.-K. Chern and R. Pietruszko, “Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase,” Biochemical and Biophysical Research Communications, vol. 213, no. 2, pp. 561–568, 1995. View at Publisher · View at Google Scholar · View at Scopus
  12. A. Kikonyogo and R. Pietruszko, “Aldehyde dehydrogenase from adult human brain that dehydrogenates γ-aminobutyraldehyde: purification, characterization, cloning and distribution,” Biochemical Journal, vol. 316, no. 1, pp. 317–324, 1996. View at Publisher · View at Google Scholar · View at Scopus
  13. N. Seiler and B. Eichentopf, “4 Aminobutyrate in mammalian putrescine catabolism,” Biochemical Journal, vol. 152, no. 2, pp. 201–210, 1975. View at Publisher · View at Google Scholar · View at Scopus
  14. J. W. Fisher, D. Mahle, and R. Abbas, “A human physiologically based pharmacokinetic model for trichloroethylene and its metabolites, trichloroacetic acid and free trichloroethanol,” Toxicology and Applied Pharmacology, vol. 152, no. 2, pp. 339–359, 1998. View at Publisher · View at Google Scholar · View at Scopus
  15. 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 α-hydroxy and α,β-unsaturated aldehydes by phagocytes at sites of inflammation,” The Journal of Clinical Investigation, vol. 99, no. 3, pp. 424–432, 1997. View at Publisher · View at Google Scholar · View at Scopus
  16. V. J. Feron, H. P. Til, F. de Vrijer, R. A. Woutersen, F. R. Cassee, and P. J. van Bladeren, “Aldehydes: occurrence, carcinogenic potential, mechanism of action and risk assessment,” Mutation Research/Genetic Toxicology, vol. 259, no. 3-4, pp. 363–385, 1991. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Srivastava, A. Chandra, L.-F. Wang et al., “Metabolism of the lipid peroxidation product, 4-hydroxy-trans-2-nonenal, in isolated perfused rat heart,” The Journal of Biological Chemistry, vol. 273, no. 18, pp. 10893–10900, 1998. View at Publisher · View at Google Scholar · View at Scopus
  18. D. P. Ghilarducci and R. S. Tjeerdema, “Fate and effects of acrolein,” Reviews of Environmental Contamination and Toxicology, vol. 144, pp. 95–146, 1995. View at Publisher · View at Google Scholar · View at Scopus
  19. K. Sydow, A. Daiber, M. Oelze et al., “Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance and cross-tolerance,” The Journal of Clinical Investigation, vol. 113, no. 3, pp. 482–489, 2004. View at Publisher · View at Google Scholar · View at Scopus
  20. M. J. Stewart, K. Malek, and D. W. Crabb, “Distribution of messenger RNAs for aldehyde dehydrogenase 1, aldehyde dehydrogenase 2, and aldehyde dehydrogenase 5 in human tissues,” Journal of Investigative Medicine, vol. 44, no. 2, pp. 42–46, 1996. View at Google Scholar · View at Scopus
  21. K.-Y. Bae, S.-W. Kim, H.-Y. Shin et al., “The acute effects of ethanol and acetaldehyde on physiological responses after ethanol ingestion in young healthy men with different ALDH2 genotypes,” Clinical Toxicology, vol. 50, no. 4, pp. 242–249, 2012. View at Publisher · View at Google Scholar · View at Scopus
  22. C. G. Steinmetz, P. Xie, H. Weiner, and T. D. Hurley, “Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion,” Structure, vol. 5, no. 5, pp. 701–711, 1997. View at Publisher · View at Google Scholar · View at Scopus
  23. J. Farrés, X. Wang, K. Takahashi, S. J. Cunningham, T. T. Wang, and H. Weiner, “Effects of changing glutamate 487 to lysine in rat and human liver mitochondrial aldehyde dehydrogenase: a model to study human (oriental type) class 2 aldehyde dehydrogenase,” The Journal of Biological Chemistry, vol. 269, no. 19, pp. 13854–13860, 1994. View at Google Scholar · View at Scopus
  24. H. N. Larson, H. Weiner, and T. D. Hurley, “Disruption of the coenzyme binding site and dimer interface revealed in the crystal structure of mitochondrial aldehyde dehydrogenase ‘Asian’ variant,” Journal of Biological Chemistry, vol. 280, no. 34, pp. 30550–30556, 2005. View at Publisher · View at Google Scholar · View at Scopus
  25. G.-S. Peng and S.-J. Yin, “Effect of the allelic variants of aldehyde dehydrogenase ALDH22 and alcohol dehydrogenase ADH1B2 on blood acetaldehyde concentrations,” Human Genomics, vol. 3, no. 2, pp. 121–127, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. T. L. Wall, C. M. Peterson, K. P. Peterson et al., “Alcohol metabolism in Asian-American men with genetic polymorphisms of aldehyde dehydrogenase,” Annals of Internal Medicine, vol. 127, no. 5, pp. 376–379, 1997. View at Publisher · View at Google Scholar · View at Scopus
  27. M. Yokoyama, A. Yokoyama, T. Yokoyama et al., “Hangover susceptibility in relation to aldehyde dehydrogenase-2 genotype, alcohol flushing, and mean corpuscular volume in Japanese workers,” Alcoholism: Clinical and Experimental Research, vol. 29, no. 7, pp. 1165–1171, 2005. View at Publisher · View at Google Scholar · View at Scopus
  28. T. L. Wall and C. L. Ehlers, “Acute effects of alcohol on P300 in Asians with different ALDH2 genotypes,” Alcoholism: Clinical and Experimental Research, vol. 19, no. 3, pp. 617–622, 1995. View at Publisher · View at Google Scholar · View at Scopus
  29. H.-Y. Shin, I.-S. Shin, and J.-S. Yoon, “ALDH2 genotype-associated differences in the acute effects of alcohol on P300, psychomotor performance, and subjective response in healthy young Korean men: a double-blind placebo-controlled crossover study,” Human Psychopharmacology, vol. 21, no. 3, pp. 159–166, 2006. View at Publisher · View at Google Scholar · View at Scopus
  30. S.-W. Kim, K.-Y. Bae, H.-Y. Shin et al., “The role of acetaldehyde in human psychomotor function: a double-blind placebo-controlled crossover study,” Biological Psychiatry, vol. 67, no. 9, pp. 840–845, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. I. Ohsawa, K. Kamino, K. Nagasaka et al., “Genetic deficiency of a mitochondrial aldehyde dehydrogenase increases serum lipid peroxides in community-dwelling females,” Journal of Human Genetics, vol. 48, no. 8, pp. 404–409, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Zhang and J. Ren, “ALDH2 in alcoholic heart diseases: molecular mechanism and clinical implications,” Pharmacology and Therapeutics, vol. 132, no. 1, pp. 86–95, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. S.-Y. Li, Q. Li, J. J. Shen et al., “Attenuation of acetaldehyde-induced cell injury by overexpression of aldehyde dehydrogenase-2 (ALDH2) transgene in human cardiac myocytes: role of MAP kinase signaling,” Journal of Molecular and Cellular Cardiology, vol. 40, no. 2, pp. 283–294, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. T. A. Doser, S. Turdi, D. P. Thomas, P. N. Epstein, S.-Y. Li, and J. Ren, “Transgenic overexpression of aldehyde dehydrogenase-2 rescues chronic alcohol intake-induced myocardial hypertrophy and contractile dysfunction,” Circulation, vol. 119, no. 14, pp. 1941–1949, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. S. Mak, D. C. Lehotay, M. Yazdanpanah, E. R. Azevedo, P. P. Liu, and G. E. Newton, “Unsaturated aldehydes including 4-OH-nonenal are elevated in patients with congestive heart failure,” Journal of Cardiac Failure, vol. 6, no. 2, pp. 108–114, 2000. View at Publisher · View at Google Scholar · View at Scopus
  36. P. Kaplan, Z. Tatarkova, P. Racay, J. Lehotsky, M. Pavlikova, and D. Dobrota, “Oxidative modifications of cardiac mitochondria and inhibition of cytochrome c oxidase activity by 4-hydroxynonenal,” Redox Report, vol. 12, no. 5, pp. 211–218, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. M. A. Ismahil, T. Hamid, P. Haberzettl et al., “Chronic oral exposure to the aldehyde pollutant acrolein induces dilated cardiomyopathy,” The American Journal of Physiology—Heart and Circulatory Physiology, vol. 301, no. 5, pp. H2050–H2060, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. K. M. S. Gomes, J. C. Campos, L. R. G. Bechara et al., “Aldehyde dehydrogenase 2 activation in heart failure restores mitochondrial function and improves ventricular function and remodelling,” Cardiovascular Research, vol. 103, no. 4, pp. 498–508, 2014. View at Publisher · View at Google Scholar · View at Scopus
  39. N. S. Aberle II, M. J. Picklo Sr., V. Amarnath, and J. Ren, “Inhibition of cardiac myocyte contraction by 4-hydroxy-trans-2-nonenal,” Cardiovascular Toxicology, vol. 4, no. 1, pp. 21–28, 2004. View at Publisher · View at Google Scholar · View at Scopus
  40. D. T. Lucas and L. I. Szweda, “Cardiac reperfusion injury: aging, lipid peroxidation, and mitochondrial dysfunction,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 2, pp. 510–514, 1998. View at Publisher · View at Google Scholar · View at Scopus
  41. G.-W. Wang, Y. Guo, T. M. Vondriska et al., “Acrolein consumption exacerbates myocardial ischemic injury and blocks nitric oxide-induced PKCε signaling and cardioprotection,” Journal of Molecular and Cellular Cardiology, vol. 44, no. 6, pp. 1016–1022, 2008. View at Publisher · View at Google Scholar · View at Scopus
  42. H. Ma, R. Guo, L. Yu, Y. Zhang, and J. Ren, “Aldehyde dehydrogenase 2 (ALDH2) rescues myocardial ischaemia/reperfusion injury: role of autophagy paradox and toxic aldehyde,” European Heart Journal, vol. 32, no. 8, pp. 1025–1038, 2011. View at Publisher · View at Google Scholar · View at Scopus
  43. P.-P. Hao, L. Xue, X.-L. Wang et al., “Association between aldehyde dehydrogenase 2 genetic polymorphism and serum lipids or lipoproteins: a meta-analysis of seven East Asian populations,” Atherosclerosis, vol. 212, no. 1, pp. 213–216, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. Y. Li, D. Zhang, W. Jin et al., “Mitochondrial aldehyde dehydrogenase-2 (ALDH2) Glu504Lys polymorphism contributes to the variation in efficacy of sublingual nitroglycerin,” The Journal of Clinical Investigation, vol. 116, no. 2, pp. 506–511, 2006. View at Publisher · View at Google Scholar · View at Scopus
  45. H. Zhang, D.-X. Gong, Y.-J. Zhang, S.-J. Li, and S. Hu, “Effect of mitochondrial aldehyde dehydrogenase-2 genotype on cardioprotection in patients with congenital heart disease,” European Heart Journal, vol. 33, no. 13, pp. 1606–1614, 2012. View at Publisher · View at Google Scholar · View at Scopus
  46. J. Endo, M. Sano, T. Katayama et al., “Metabolic remodeling induced by mitochondrial aldehyde stress stimulates tolerance to oxidative stress in the heart,” Circulation Research, vol. 105, no. 11, pp. 1118–1127, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. S. Takagi, S. Baba, N. Iwai et al., “The aldehyde dehydrogenase 2 gene is a risk factor for hypertension in Japanese but does not alter the sensitivity to pressor effects of alcohol: the Suita study,” Hypertension Research, vol. 24, no. 4, pp. 365–370, 2001. View at Publisher · View at Google Scholar · View at Scopus
  48. K. Amamoto, T. Okamura, S. Tamaki et al., “Epidemiologic study of the association of low-Km mitochondrial acetaldehyde dehydrogenase genotypes with blood pressure level and the prevalence of hypertension in a general population,” Hypertension Research, vol. 25, no. 6, pp. 857–864, 2002. View at Publisher · View at Google Scholar · View at Scopus
  49. P. Hui, T. Nakayama, A. Morita et al., “Common single nucleotide polymorphisms in Japanese patients with essential hypertension: aldehyde dehydrogenase 2 gene as a risk factor independent of alcohol consumption,” Hypertension Research, vol. 30, no. 7, pp. 585–592, 2007. View at Publisher · View at Google Scholar · View at Scopus
  50. M. Tsuchihashi-Makaya, M. Serizawa, K. Yanai et al., “Gene-environmental interaction regarding alcohol-metabolizing enzymes in the Japanese general population,” Hypertension Research, vol. 32, no. 3, pp. 207–213, 2009. View at Publisher · View at Google Scholar · View at Scopus
  51. Y. Wang, Y. Zhang, J. Zhang et al., “Association of a functional single-nucleotide polymorphism in the ALDH2 gene with essential hypertension depends on drinking behavior in a Chinese Han population,” Journal of Human Hypertension, vol. 27, no. 3, pp. 181–186, 2013. View at Publisher · View at Google Scholar · View at Scopus
  52. M. Guivernau, E. Baraona, and C. S. Lieber, “Acute and chronic effects of ethanol and its metabolites on vascular production of prostacyclin in rats,” Journal of Pharmacology and Experimental Therapeutics, vol. 240, no. 1, pp. 59–64, 1987. View at Google Scholar · View at Scopus
  53. Y.-C. Chang, Y.-F. Chiu, I.-T. Lee et al., “Common ALDH2 genetic variants predict development of hypertension in the SAPPHIRe prospective cohort: gene-environmental interaction with alcohol consumption,” BMC Cardiovascular Disorders, vol. 12, article 58, 2012. View at Publisher · View at Google Scholar · View at Scopus
  54. T. Nakagawa, A. Kajiwara, J. Saruwatari et al., “The combination of mitochondrial low enzyme-activity aldehyde dehydrogenase 2 allele and superoxide dismutase 2 genotypes increases the risk of hypertension in relation to alcohol consumption,” Pharmacogenetics and Genomics, vol. 23, no. 1, pp. 34–37, 2013. View at Publisher · View at Google Scholar · View at Scopus
  55. O. Niemelä, “Distribution of ethanol-induced protein adducts in vivo: relationship to tissue injury,” Free Radical Biology and Medicine, vol. 31, no. 12, pp. 1533–1538, 2001. View at Publisher · View at Google Scholar · View at Scopus
  56. Acetaldehyde, vol. 36 of IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, IARC, 1985.
  57. H. K. Seitz, S. Matsuzaki, A. Yokoyama, N. Homann, S. Vakevainen, and X. D. Wang, “Alcohol and Cancer,” Alcoholism: Clinical and Experimental Research, vol. 25, supplement s1, pp. 137S–143S, 2001. View at Publisher · View at Google Scholar
  58. “Alcohol drinking. Biological data relevant to the evaluation of carcinogenic risk to humans,” IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, vol. 44, pp. 101–152, 1988.
  59. K. Matsuo, N. Hamajima, M. Shinoda et al., “Gene-environment interaction between an aldehyde dehydrogenase-2 (ALDH2) polymorphism and alcohol consumption for the risk of esophageal cancer,” Carcinogenesis, vol. 22, no. 6, pp. 913–916, 2001. View at Publisher · View at Google Scholar · View at Scopus
  60. Y.-J. Chen, C. Chen, D.-C. Wu et al., “Interactive effects of lifetime alcohol consumption and alcohol and aldehyde dehydrogenase polymorphisms on esophageal cancer risks,” International Journal of Cancer, vol. 119, no. 12, pp. 2827–2831, 2006. View at Publisher · View at Google Scholar · View at Scopus
  61. W. F. Bosron and T.-K. Li, “Genetic polymorphism of human liver alcohol and aldehyde dehydrogenases, and their relationship to alcohol metabolism and alcoholism,” Hepatology, vol. 6, no. 3, pp. 502–510, 1986. View at Publisher · View at Google Scholar · View at Scopus
  62. Y. Yukawa, M. Muto, K. Hori et al., “Combination of ADH1B2/ALDH22 polymorphisms alters acetaldehyde-derived DNA damage in the blood of Japanese alcoholics,” Cancer Science, vol. 103, no. 9, pp. 1651–1655, 2012. View at Publisher · View at Google Scholar · View at Scopus
  63. A. Yokoyama, T. Muramatsu, T. Omori et al., “Alcohol and aldehyde dehydrogenase gene polymorphisms influence susceptibility to esophageal cancer in Japanese alcoholics,” Alcoholism: Clinical and Experimental Research, vol. 23, no. 11, pp. 1705–1710, 1999. View at Publisher · View at Google Scholar · View at Scopus
  64. A. Yokoyama, E. Tsutsumi, H. Imazeki, Y. Suwa, C. Nakamura, and T. Yokoyama, “Contribution of the alcohol dehydrogenase-1B genotype and oral microorganisms to high salivary acetaldehyde concentrations in Japanese alcoholic men,” International Journal of Cancer, vol. 121, no. 5, pp. 1047–1054, 2007. View at Publisher · View at Google Scholar · View at Scopus
  65. K. Matsuo, I. Oze, S. Hosono et al., “The aldehyde dehydrogenase 2 (ALDH2) Glu504Lys polymorphism interacts with alcohol drinking in the risk of stomach cancer,” Carcinogenesis, vol. 34, no. 7, pp. 1510–1515, 2013. View at Publisher · View at Google Scholar · View at Scopus
  66. H.-L. Wang, P.-Y. Zhou, P. Liu, and Y. Zhang, “ALDH2 and ADH1 genetic polymorphisms may contribute to the risk of gastric cancer: a meta-analysis,” PLoS ONE, vol. 9, no. 3, Article ID e88779, 2014. View at Publisher · View at Google Scholar · View at Scopus
  67. X.-F. Guo, J. Wang, S.-J. Yu et al., “Meta-analysis of the ADH1B and ALDH2 polymorphisms and the risk of colorectal cancer in East Asians,” Internal Medicine, vol. 52, no. 24, pp. 2693–2699, 2013. View at Publisher · View at Google Scholar · View at Scopus
  68. H. Zhao, K.-J. Liu, Z.-D. Lei, S.-L. Lei, and Y.-Q. Tian, “Meta-analysis of the aldehyde dehydrogenases-2 (ALDH2) Glu487Lys polymorphism and colorectal cancer risk,” PLoS ONE, vol. 9, no. 2, Article ID e88656, 2014. View at Publisher · View at Google Scholar · View at Scopus
  69. D. Zhou, L. Xiao, Y. Zhang et al., “Genetic polymorphisms of ALDH2 and ADH2 are not associated with risk of hepatocellular carcinoma among East Asians,” Tumor Biology, vol. 33, no. 3, pp. 841–846, 2012. View at Publisher · View at Google Scholar · View at Scopus
  70. J.-Y. Choi, J. Abel, T. Neuhaus et al., “Role of alcohol and genetic polymorphisms of CYP2E1 and ALDH2 in breast cancer development,” Pharmacogenetics, vol. 13, no. 2, pp. 67–72, 2003. View at Publisher · View at Google Scholar · View at Scopus
  71. T. Kawase, K. Matsuo, A. Hiraki et al., “Interaction of the effects of alcohol drinking and polymorphisms in alcohol-metabolizing enzymes on the risk of female breast cancer in Japan,” Journal of Epidemiology, vol. 19, no. 5, pp. 244–250, 2009. View at Publisher · View at Google Scholar · View at Scopus
  72. M. Goedert and M. G. Spillantini, “A century of Alzheimer's disease,” Science, vol. 314, no. 5800, pp. 777–781, 2006. View at Publisher · View at Google Scholar · View at Scopus
  73. H. W. Querfurth and F. M. LaFerla, “Alzheimer's disease,” The New England Journal of Medicine, vol. 362, no. 4, pp. 329–344, 2010. View at Publisher · View at Google Scholar · View at Scopus
  74. Y. Zhao and B. Zhao, “Oxidative stress and the pathogenesis of Alzheimer's disease,” Oxidative Medicine and Cellular Longevity, vol. 2013, Article ID 316523, 10 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  75. L. M. Sayre, D. A. Zelasko, P. L. R. Harris, G. Perry, R. G. Salomon, and M. A. Smith, “4-hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease,” Journal of Neurochemistry, vol. 68, no. 5, pp. 2092–2097, 1997. View at Google Scholar · View at Scopus
  76. W. A. Pedersen, N. R. Cashman, and M. P. Mattson, “The lipid peroxidation product 4-hydroxynonenal impairs glutamate and glucose transport and choline acetyltransferase activity in NSC-19 motor neuron cells,” Experimental Neurology, vol. 155, no. 1, pp. 1–10, 1999. View at Publisher · View at Google Scholar · View at Scopus
  77. M. D. Neely, K. R. Sidell, D. G. Graham, and T. J. Montine, “The lipid peroxidation product 4-hydroxynonenal inhibits neurite outgrowth, disrupts neuronal microtubules, and modifies cellular tubulin,” Journal of Neurochemistry, vol. 72, no. 6, pp. 2323–2333, 1999. View at Publisher · View at Google Scholar · View at Scopus
  78. A. Takeda, M. A. Smith, J. Avilá et al., “In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification,” Journal of Neurochemistry, vol. 75, no. 3, pp. 1234–1241, 2000. View at Publisher · View at Google Scholar · View at Scopus
  79. Q. Liu, M. A. Smith, J. Avilá et al., “Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations,” Free Radical Biology and Medicine, vol. 38, no. 6, pp. 746–754, 2005. View at Publisher · View at Google Scholar · View at Scopus
  80. E. Tamagno, M. Parola, P. Bardini et al., “β-site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways,” Journal of Neurochemistry, vol. 92, no. 3, pp. 628–636, 2005. View at Publisher · View at Google Scholar · View at Scopus
  81. I. Ohsawa, K. Nishimaki, C. Yasuda, K. Kamino, and S. Ohta, “Deficiency in a mitochondrial aldehyde dehydrogenase increases vulnerability to oxidative stress in PC12 cells,” Journal of Neurochemistry, vol. 84, no. 5, pp. 1110–1117, 2003. View at Publisher · View at Google Scholar · View at Scopus
  82. S. Ohta and I. Ohsawa, “Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: on defects in the cytochrome c oxidase complex and aldehyde detoxification,” Journal of Alzheimer's Disease, vol. 9, no. 2, pp. 155–166, 2006. View at Google Scholar · View at Scopus
  83. K. S. Montine, S. J. Oison, V. Amarnath, W. O. Whetsell Jr., D. G. Graham, and T. J. Montine, “Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4,” The American Journal of Pathology, vol. 150, no. 2, pp. 437–443, 1997. View at Google Scholar · View at Scopus
  84. W. A. Pedersen, S. L. Chan, and M. P. Mattson, “A mechanism for the neuroprotective effect of apolipoprotein E: isoform- specific modification by the lipid peroxidation product 4-hydroxynonenal,” Journal of Neurochemistry, vol. 74, no. 4, pp. 1426–1433, 2000. View at Publisher · View at Google Scholar · View at Scopus
  85. B. Wang, J. Wang, S. Zhou et al., “The association of mitochondrial aldehyde dehydrogenase gene (ALDH2) polymorphism with susceptibility to late-onset Alzheimer's disease in Chinese,” Journal of the Neurological Sciences, vol. 268, no. 1-2, pp. 172–175, 2008. View at Publisher · View at Google Scholar · View at Scopus
  86. S. Zhou, Huriletemuer, J. Wang et al., “Absence of association on aldehyde dehydrogenase 2 (ALDH2) polymorphism with Mongolian Alzheimer patients,” Neuroscience Letters, vol. 468, no. 3, pp. 312–315, 2010. View at Publisher · View at Google Scholar · View at Scopus
  87. P.-P. Hao, Y.-G. Chen, J.-L. Wang, X. Wang, and Y. Zhang, “Meta-analysis of aldehyde dehydrogenase 2 gene polymorphism and Alzheimer's disease in East Asians,” Canadian Journal of Neurological Sciences, vol. 38, no. 3, pp. 500–506, 2011. View at Publisher · View at Google Scholar · View at Scopus