Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2013, Article ID 629028, 7 pages
http://dx.doi.org/10.1155/2013/629028
Review Article

Role of Lipid Peroxidation-Derived α, β-Unsaturated Aldehydes in Vascular Dysfunction

Department of Microbiology, School of Medicine, Kyung Hee University, No.1 Hoegi-dong, Dongdaemun-gu, Seoul 130-701, Republic of Korea

Received 28 January 2013; Revised 30 April 2013; Accepted 7 May 2013

Academic Editor: Kota V. Ramana

Copyright © 2013 Seung Eun Lee and Yong Seek Park. 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. R. Stocker and J. F. Keaney Jr., “Role of oxidative modifications in atherosclerosis,” Physiological Reviews, vol. 84, no. 4, pp. 1381–1478, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. A. D. Lopez, C. D. Mathers, M. Ezzati, D. T. Jamison, and C. J. Murray, “Global and regional burden of disease and risk factors, 2001: systematic analysis of population health data,” The Lancet, vol. 367, no. 9524, pp. 1747–1757, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. S. Sevinç and A. D. Akyol, “Cardiac risk factors and quality of life in patients with coronary artery disease,” Journal of Clinical Nursing, vol. 19, no. 9-10, pp. 1315–1325, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. T. Sonta, T. Inoguchi, H. Tsubouchi et al., “Evidence for contribution of vascular NAD(P)H oxidase to increased oxidative stress in animal models of diabetes and obesity,” Free Radical Biology and Medicine, vol. 37, no. 1, pp. 115–123, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. A. Negre-Salvayre, C. Coatrieux, C. Ingueneau, and R. Salvayre, “Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors,” British Journal of Pharmacology, vol. 153, no. 1, pp. 6–20, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. K. Uchida, “Role of reactive aldehyde in cardiovascular diseases,” Free Radical Biology and Medicine, vol. 28, no. 12, pp. 1685–1696, 2000. View at Publisher · View at Google Scholar · View at Scopus
  7. L. Chen, R. Na, M. Gu, A. Richardson, and Q. Ran, “Lipid peroxidation up-regulates BACE1 expression in vivo: a possible early event of amyloidogenesis in Alzheimer's disease,” Journal of Neurochemistry, vol. 107, no. 1, pp. 197–207, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. I. Rahman, “Oxidative stress in pathogenesis of chronic obstructive pulmonary disease: cellular and molecular mechanisms,” Cell Biochemistry and Biophysics, vol. 43, no. 1, pp. 167–188, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. A. Negre-Salvayre, N. Auge, V. Ayala et al., “Pathological aspects of lipid peroxidation,” Free Radical Research, vol. 44, no. 10, pp. 1125–1171, 2010. View at Publisher · View at Google Scholar · View at Scopus
  10. M. E. Szapacs, H. H. Kim, N. A. Porter, and D. C. Liebler, “Identification of proteins adducted by lipid peroxidation products in plasma and modifications of apolipoprotein A1 with a novel biotinylated phospholipid probe,” Journal of Proteome Research, vol. 7, no. 10, pp. 4237–4246, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. M. P. Mattson, “Roles of the lipid peroxidation product 4-hydroxynonenal in obesity, the metabolic syndrome, and associated vascular and neurodegenerative disorders,” Experimental Gerontology, vol. 44, no. 10, pp. 625–633, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. E. I. Finkelstein, J. Ruben, C. W. Koot, M. Hristova, and A. Van Der Vliet, “Regulation of constitutive neutrophil apoptosis by the α,β- unsaturated aldehydes acrolein and 4-hydroxynonenal,” American Journal of Physiology, vol. 289, no. 6, pp. L1019–L1028, 2005. View at Publisher · View at Google Scholar · View at Scopus
  13. L. J. Marnett, J. N. Riggins, and J. D. West, “Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein,” Journal of Clinical Investigation, vol. 111, no. 5, pp. 583–593, 2003. View at Publisher · View at Google Scholar · View at Scopus
  14. R. M. LoPachin, T. Gavin, D. R. Petersen, and D. S. Barber, “Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: nucleophilic targets and adduct formation,” Chemical Research in Toxicology, vol. 22, no. 9, pp. 1499–1508, 2009. View at Publisher · View at Google Scholar · View at Scopus
  15. I. G. Minko, I. D. Kozekov, T. M. Harris, C. J. Rizzo, R. S. Lloyd, and M. P. Stone, “Chemistry and biology of DNA containing 1,N2-deoxyguanosine adducts of the α,β-unsaturated aldehydes acrolein, crotonaldehyde, and 4-hydroxynonenal,” Chemical Research in Toxicology, vol. 22, no. 5, pp. 759–778, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. R. M. Lopachin, D. S. Barber, and T. Gavin, “Molecular mechanisms of the conjugated α,β-unsaturated carbonyl derivatives: relevance to neurotoxicity and neurodegenerative diseases,” Toxicological Sciences, vol. 104, no. 2, pp. 235–249, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. N. Y. Calingasan, K. Uchida, and G. E. Gibson, “Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease,” Journal of Neurochemistry, vol. 72, no. 2, pp. 751–756, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. N. L. Tsakadze, S. Srivastava, S. O. Awe, A. S. O. Adeagbo, A. Bhatnagar, and S. E. D'Souza, “Acrolein-induced vasomotor responses of rat aorta,” American Journal of Physiology, vol. 285, no. 2, pp. H727–H734, 2003. View at Google Scholar · View at Scopus
  19. K. Uchida, M. Kanematsu, Y. Morimitsu, T. Osawa, N. Noguchi, and E. Niki, “Acrolein is a product of lipid peroxidation reaction: formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins,” Journal of Biological Chemistry, vol. 273, no. 26, pp. 16058–16066, 1998. View at Publisher · View at Google Scholar · View at Scopus
  20. K. Hamann, A. Durkes, H. Ouyang, K. Uchida, A. Pond, and R. Shi, “Critical role of acrolein in secondary injury following ex vivo spinal cord trauma,” Journal of Neurochemistry, vol. 107, no. 3, pp. 712–721, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. Y. S. Park, J. Kim, Y. Misonou et al., “Acrolein induces cyclooxygenase-2 and prostaglandin production in human umbilical vein endothelial cells: roles of p38 MAP kinase,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 6, pp. 1319–1325, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. S. E. Lee, S. H. Lee, D. S. Ryu, C. Park, K. Park, and Y. S. Park, “Differentially-expressed genes related to atherosclerosis in acrolein-stimulated human umbilical vein endothelial cells,” Biochip Journal, vol. 4, no. 4, pp. 264–271, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. D. J. Conklin, A. Bhatnagar, H. R. Cowley et al., “Acrolein generation stimulates hypercontraction in isolated human blood vessels,” Toxicology and Applied Pharmacology, vol. 217, no. 3, pp. 277–288, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. M. R. McCall, J. Y. Tang, J. K. Bielicki, and T. M. Forte, “Inhibition of lecithin-cholesterol acyltransferase and modification of HDL apolipoproteins by aldehydes,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 15, no. 10, pp. 1599–1606, 1995. View at Google Scholar · View at Scopus
  25. L. Alfredsson, N. Hammar, and C. Hogstedt, “Incidence of myocardial infarction and mortality from specific causes among bus drivers in Sweden,” International Journal of Epidemiology, vol. 22, no. 1, pp. 57–61, 1993. View at Google Scholar · View at Scopus
  26. M. P. Stonez, Y. Cho, H. Huang et al., “Interstrand DNA cross-links induced by α,β-unsaturated aldehydes derived from lipid peroxidation and environmental sources,” Accounts of Chemical Research, vol. 41, no. 7, pp. 793–804, 2008. View at Publisher · View at Google Scholar · View at Scopus
  27. E. Eder and B. Budiawan, “Cancer risk assessment for the environmental mutagen and carcinogen crotonaldehyde on the basis of TD50 and comparison with 1,N2-propanodeoxyguanosine adduct levels,” Cancer Epidemiology Biomarkers and Prevention, vol. 10, no. 8, pp. 883–888, 2001. View at Google Scholar · View at Scopus
  28. M. Kawaguchi-Niida, N. Shibata, S. Morikawa et al., “Crotonaldehyde accumulates in glial cells of Alzheimer's disease brain,” Acta Neuropathologica, vol. 111, no. 5, pp. 422–429, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. E. Eder, D. Schuler, and B. Budiawan, “Cancer risk assessment for crotonaldehyde and 2-hexenal: an approach,” IARC Scientific Publications, no. 150, pp. 219–232, 1999. View at Google Scholar · View at Scopus
  30. T. Neudecker, E. Eder, C. Deininger, and D. Henschler, “Crotonaldehyde is mutagenic in Salmonella typhimurium TA100,” Environmental and Molecular Mutagenesis, vol. 14, no. 3, pp. 146–148, 1989. View at Google Scholar · View at Scopus
  31. H. Esterbauer, R. J. Schaur, and H. Zollner, “Chemistry and Biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes,” Free Radical Biology and Medicine, vol. 11, no. 1, pp. 81–128, 1991. View at Publisher · View at Google Scholar · View at Scopus
  32. M. Van Der Toorn, M. P. Smit-de Vries, D. Slebos et al., “Cigarette smoke irreversibly modifies glutathione in airway epithelial cells,” American Journal of Physiology, vol. 293, no. 5, pp. L1156–L1162, 2007. View at Publisher · View at Google Scholar · View at Scopus
  33. X. Liu, Z. Yang, X. Pan, M. Zhu, and J. Xie, “Crotonaldehyde induces oxidative stress and caspase-dependent apoptosis in human bronchial epithelial cells,” Toxicology Letters, vol. 195, no. 1, pp. 90–98, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. K. Uchida, M. Shiraishi, Y. Naito, Y. Torii, Y. Nakamura, and T. Osawa, “Activation of stress signaling pathways by the end product of lipid peroxidation: 4-Hydroxy-2-nonenal is a potential inducer of intracellular peroxide production,” Journal of Biological Chemistry, vol. 274, no. 4, pp. 2234–2242, 1999. View at Publisher · View at Google Scholar · View at Scopus
  35. A. Kode, S. Yang, and I. Rahman, “Differential effects of cigarette smoke on oxidative stress and proinflammatory cytokine release in primary human airway epithelial cells and in a variety of transformed alveolar epithelial cells,” Respiratory Research, vol. 7, article 132, 2006. View at Publisher · View at Google Scholar · View at Scopus
  36. T. Kumagai, N. Matsukawa, Y. Kaneko, Y. Kusumi, M. Mitsumata, and K. Uchida, “A lipid peroxidation-derived inflammatory mediator: identification of 4-hydroxy-2-nonenal as a potential inducer of cyclooxygenase-2 in macrophages,” Journal of Biological Chemistry, vol. 279, no. 46, pp. 48389–48396, 2004. View at Publisher · View at Google Scholar · View at Scopus
  37. D. A. Butterfield, M. L. Bader Lange, and R. Sultana, “Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease,” Biochimica et Biophysica Acta, vol. 1801, no. 8, pp. 924–929, 2010. View at Publisher · View at Google Scholar · View at Scopus
  38. I. Rahman, A. A. M. Van Schadewijk, A. J. L. Crowther et al., “4-Hydroxy-2-nonenal, a specific lipid peroxidation product, is elevated in lungs of patients with chronic obstructive pulmonary disease,” American Journal of Respiratory and Critical Care Medicine, vol. 166, no. 4, pp. 490–495, 2002. View at Publisher · View at Google Scholar · View at Scopus
  39. G. J. Quinlan, T. W. Evans, and J. M. C. Gutteridge, “4-Hydroxy-2-nonenal levels increase in the plasma of patients with adult respiratory distress syndrome as linoleic acid appears to fall,” Free Radical Research, vol. 21, no. 2, pp. 95–106, 1994. View at Google Scholar · View at Scopus
  40. C. Napoli, F. P. D'Armiento, F. P. Mancini et al., “Fatty streak formation occurs in human fetal aortas and is greatly enhanced maternal, hypercholesterolemia. Intimal accumulation of low density lipoprotein and its oxidation precede monocyte recruitment into early atheroeclerotic lesions,” Journal of Clinical Investigation, vol. 100, no. 11, pp. 2680–2690, 1997. View at Google Scholar · View at Scopus
  41. M. A. Lovell, C. Xie, and W. R. Markesbery, “Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures,” Neurobiology of Aging, vol. 22, no. 2, pp. 187–194, 2001. View at Publisher · View at Google Scholar · View at Scopus
  42. M. A. Bradley, W. R. Markesbery, and M. A. Lovell, “Increased levels of 4-hydroxynonenal and acrolein in the brain in preclinical Alzheimer disease,” Free Radical Biology and Medicine, vol. 48, no. 12, pp. 1570–1576, 2010. View at Publisher · View at Google Scholar · View at Scopus
  43. N. Uesugi, N. Sakata, M. Nangaku et al., “Possible mechanism for medial smooth muscle cell injury in diabetic nephropathy: glycoxidation-mediated local complement activation,” American Journal of Kidney Diseases, vol. 44, no. 2, pp. 224–238, 2004. View at Publisher · View at Google Scholar · View at Scopus
  44. J. Grigsby, B. Betts, E. Vidro-Kotchan, R. Culbert, and A. Tsin, “A possible role of acrolein in diabetic retinopathy: involvement of a VEGF/TGFbeta signaling pathway of the retinal pigment epithelium in hyperglycemia,” Current Eye Research, vol. 37, no. 11, pp. 1045–1053, 2012. View at Google Scholar
  45. S. Srivastava, S. D. Sithu, E. Vladykovskaya et al., “Oral exposure to acrolein exacerbates atherosclerosis in apoE-null mice,” Atherosclerosis, vol. 215, no. 2, pp. 301–308, 2011. View at Publisher · View at Google Scholar · View at Scopus
  46. T. Wang, Y. Liu, L. Chen et al., “Effect of sildenafil on acrolein-induced airway inflammation and mucus production in rats,” European Respiratory Journal, vol. 33, no. 5, pp. 1122–1132, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. G. Volpi, F. Facchinetti, N. Moretto, M. Civelli, and R. Patacchini, “Cigarette smoke and α,β-unsaturated aldehydes elicit VEGF release through the p38 MAPK pathway in human airway smooth muscle cells and lung fibroblasts,” British Journal of Pharmacology, vol. 163, no. 3, pp. 649–661, 2011. View at Publisher · View at Google Scholar · View at Scopus
  48. K. Tsirulnikov, N. Abuladze, A. Bragin et al., “Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal,” Toxicology and Applied Pharmacology, vol. 263, no. 3, pp. 303–314, 2012. View at Google Scholar
  49. P. Eaton, J. Li, D. J. Hearse, and M. J. Shattock, “Formation of 4-hydroxy-2-nonenal-modified proteins in ischemic rat heart,” American Journal of Physiology, vol. 276, no. 3, pp. H935–H943, 1999. View at Google Scholar · View at Scopus
  50. G. Leonarduzzi, E. Chiarpotto, F. Biasi, and G. Poli, “4-Hydroxynonenal and cholesterol oxidation products in atherosclerosis,” Molecular Nutrition and Food Research, vol. 49, no. 11, pp. 1044–1049, 2005. View at Publisher · View at Google Scholar · View at Scopus
  51. B. Halliwell and H. E. Poulsen, Cigarette Smoke and Oxidative Stress, Springer, Berlin, Germany, 2006.
  52. Y. S. Park, Y. Misonou, N. Fujiwara et al., “Induction of thioredoxin reductase as an adaptive response to acrolein in human umbilical vein endothelial cells,” Biochemical and Biophysical Research Communications, vol. 327, no. 4, pp. 1058–1065, 2005. View at Publisher · View at Google Scholar · View at Scopus
  53. S. E. Lee, S. I. Jeong, G. Kim et al., “Upregulation of heme oxygenase-1 as an adaptive mechanism for protection against crotonaldehyde in human umbilical vein endothelial cells,” Toxicology Letters, vol. 201, no. 3, pp. 240–248, 2011. View at Publisher · View at Google Scholar · View at Scopus
  54. J. D. Adams Jr. and L. K. Klaidman, “Acrolein-induced oxygen radical formation,” Free Radical Biology and Medicine, vol. 15, no. 2, pp. 187–193, 1993. View at Publisher · View at Google Scholar · View at Scopus
  55. J. P. Kehrer and S. S. Biswal, “The molecular effects of acrolein,” Toxicological Sciences, vol. 57, no. 1, pp. 6–15, 2000. View at Google Scholar · View at Scopus
  56. J. Whitsett, M. J. Picklo Sr., and J. Vasquez-Vivar, “4-Hydroxy-2-nonenal increases superoxide anion radical in endothelial cells via stimulated GTP cyclohydrolase proteasomal degradation,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 11, pp. 2340–2347, 2007. View at Publisher · View at Google Scholar · View at Scopus
  57. M. R. Yun, H. M. Park, K. W. Seo, S. J. Lee, D. S. Im, and C. D. Kim, “5-Lipoxygenase plays an essential role in 4-HNE-enhanced ROS production in murine macrophages via activation of NADPH oxidase,” Free Radical Research, vol. 44, no. 7, pp. 742–750, 2010. View at Publisher · View at Google Scholar · View at Scopus
  58. R. Foncea, C. Carvajal, C. Almarza, and F. Leighton, “Endothelial cell oxidative stress and signal transduction,” Biological Research, vol. 33, no. 2, pp. 89–96, 2000. View at Google Scholar · View at Scopus
  59. T. Nguyen, C. S. Yang, and C. B. Pickett, “The pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress,” Free Radical Biology and Medicine, vol. 37, no. 4, pp. 433–441, 2004. View at Publisher · View at Google Scholar · View at Scopus
  60. Y. Miyamoto, Y. H. Koh, Y. S. Park et al., “Oxidative stress caused by inactivation of glutathione peroxidase and adaptive responses,” Biological Chemistry, vol. 384, no. 4, pp. 567–574, 2003. View at Publisher · View at Google Scholar · View at Scopus
  61. Y. Misonou, M. Takahashi, Y. S. Park et al., “Acrolein induces Hsp72 via both PKCδ/JNK and calcium signaling pathways in human umbilical vein endothelial cells,” Free Radical Research, vol. 39, no. 5, pp. 507–512, 2005. View at Publisher · View at Google Scholar · View at Scopus
  62. N. J. Lee, S. E. Lee, S. H. Lee, D. S. Ryu, and Y. S. Park, “Acrolein induces adaptive response through upregulate of HO-1 via activation of Nrf2 in RAW 264. 7 macrophage,” Molecular & Cellular Toxicology, vol. 5, no. 3, p. 77, 2009. View at Google Scholar
  63. C. C. Wu, C. W. Hsieh, P. H. Lai, J. B. Lin, Y. C. Liu, and B. S. Wung, “Upregulation of endothelial heme oxygenase-1 expression through the activation of the JNK pathway by sublethal concentrations of acrolein,” Toxicology and Applied Pharmacology, vol. 214, no. 3, pp. 244–252, 2006. View at Publisher · View at Google Scholar · View at Scopus
  64. A. Ishikado, Y. Nishio, K. Morino et al., “Low concentration of 4-hydroxy hexenal increases heme oxygenase-1 expression through activation of Nrf2 and antioxidative activity in vascular endothelial cells,” Biochemical and Biophysical Research Communications, vol. 402, no. 1, pp. 99–104, 2010. View at Publisher · View at Google Scholar · View at Scopus
  65. Y. S. Park and N. Taniguchi, “Acrolein induces inflammatory response underlying endothelial dysfunction: a risk factor for atherosclerosis,” Annals of the New York Academy of Sciences, vol. 1126, pp. 185–189, 2008. View at Publisher · View at Google Scholar · View at Scopus
  66. L. Li, R. F. Hamilton Jr., and A. Holian, “Effect of acrolein on human alveolar macrophage NF-κB activity,” American Journal of Physiology, vol. 277, no. 3, pp. L550–L557, 1999. View at Google Scholar · View at Scopus
  67. P. Haberzettl, E. Vladykovskaya, S. Srivastava, and A. Bhatnagar, “Role of endoplasmic reticulum stress in acrolein-induced endothelial activation,” Toxicology and Applied Pharmacology, vol. 234, no. 1, pp. 14–24, 2009. View at Publisher · View at Google Scholar · View at Scopus
  68. S. J. Lee, C. E. Kim, K. W. Seo, and C. D. Kim, “HNE-induced 5-LO expression is regulated by NF-κB/ERK and Sp1/p38 MAPK pathways via EGF receptor in murine macrophages,” Cardiovascular Research, vol. 88, no. 2, pp. 352–359, 2010. View at Publisher · View at Google Scholar · View at Scopus
  69. M. E. Burleigh, V. R. Babaev, J. A. Oates et al., “Cyclooxygenase-2 promotes early atherosclerotic lesion formation in LDL receptor-deficient mice,” Circulation, vol. 105, no. 15, pp. 1816–1823, 2002. View at Publisher · View at Google Scholar · View at Scopus
  70. T. E. O'Toole, Y. Zheng, J. Hellmann, D. J. Conklin, O. Barski, and A. Bhatnagar, “Acrolein activates matrix metalloproteinases by increasing reactive oxygen species in macrophages,” Toxicology and Applied Pharmacology, vol. 236, no. 2, pp. 194–201, 2009. View at Publisher · View at Google Scholar · View at Scopus
  71. C. E. Kim, S. J. Lee, K. W. Seo et al., “Acrolein increases 5-lipoxygenase expression in murine macrophages through activation of ERK pathway,” Toxicology and Applied Pharmacology, vol. 245, no. 1, pp. 76–82, 2010. View at Publisher · View at Google Scholar · View at Scopus
  72. S. Akiba, S. Kumazawa, H. Yamaguchi et al., “Acceleration of matrix metalloproteinase-1 production and activation of platelet-derived growth factor receptor β in human coronary smooth muscle cells by oxidized LDL and 4-hydroxynonenal,” Biochimica et Biophysica Acta, vol. 1763, no. 8, pp. 797–804, 2006. View at Publisher · View at Google Scholar · View at Scopus