Role of reactive aldehyde in cardiovascular diseases

Free Radical Biology and Medicine

Volumn 28, Issue 12, 2000, Pages 1685-1696

  Uchida, Koji ^a  

^a NAGOYA UNIVERSITY   (Japan)

Author keywords

Atherosclerosis; Free radicals; Glycation; Lipid peroxidation; Low density lipoproteins; Oxidative stress; Reactive aldehydes

Indexed keywords

ALDEHYDE DERIVATIVE;

ATHEROSCLEROSIS; CARDIOVASCULAR DISEASE; CYTOTOXICITY; DIABETIC ANGIOPATHY; GLYCATION; LIPID PEROXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN MODIFICATION; REVIEW;

ANIMALIA;

EID: 0034659147     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(00)00226-4     Document Type: Article

References (84)

1. Esterbauer H., Schaur J.S., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes. Free Radic. Biol. Med. 11:1991;81-128.
2. Zyzak D.V., Richardson J.M., Thorpe S.R., Baynes J.W. Formation of reactive intermediates from Amadori compounds under physiological conditions. Arch. Biochem. Biophys. 316:1995;547-554.
3. Kristal B.S., Park B.K., Yu B.P. 4-hydroxyhexenal is a potent inducer of the mitochondrial permeability transition. J. Biol. Chem. 271:1996;6033-6038.
4. Jain S.K. The accumulation of malondialdehyde, a product of fatty acid peroxidation, can disturb amino phospholipid organization in the membrane bilayer of human erythrocytes. J. Biol. Chem. 259:1984;3391-3394.
5. Fu M.-X., Requena J.R., Jenkins A.J., Lyons T.J., Baynes J.W., Thorpe S.R. The advanced glycation end product, Nε-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J. Biol. Chem. 271:1996;9982-9986.
6. Bucala R., Cerami A. Advanced glycosylation chemistry, biology, and implications for diabetes and aging . Adv. Pharmacol. 23:1992;1-34.
7. Anderson M.M., Hazen S.L., Hsu F.F., Heinecke J.W. 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 . J. Clin. Invest. 99:1997;424-432.
8. Daugherty A., Dunn J.L., Rateri D.L., Heinecke J.W. Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J. Clin. Invest. 94:1994;437-444.
9. Savenkova M.L., Mueller D.M., Heinecke J.W. Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein. J. Biol. Chem. 269:1994;20394-20400.
10. Podrez E.A.P., Hazen S.L. Myeloperoxidase-generated oxidants and atherosclerosis. Free Radic. Biol. Med. 28:2000;1717-1725.
11. Uchida K., Kanematsu M., Sakai K., Matsuda M., Hattori N., Mizuno Y., Suzuki D., Miyata T., Noguchi N., Niki E., Osawa T. Protein-bound acrolein potential markers for oxidative stress . Proc. Natl. Acad. Sci. USA. 95:1998;4882-4887.
12. Uchida K., Kanematsu M., Morimitsu Y., Osawa T., Noguchi N., Niki E. Acrolein is a product of lipid peroxidation reaction formation of acrolein and its conjugate with lysine residues in oxidized low-density lipoprotein . J. Biol. Chem. 273:1998;16058-16066.
13. Satoh K., Yamada S., Koike Y., Toyokuni S., Kumano T., Takahata T., Hayakari M., Tuchida S., Uchida K. A 1-hour enzyme-linked immunosorbent assay for quantitation of acrolein and hydroxynonenal-modified proteins. Anal. Biochem. 270:1999;323-328.
14. Schauenstein E., Taufer M., Esterbauer H., Kylianek A., Seelich T. Reaction of protein SH-groups with 4-hydroxy-2-nonenal. Monatsh. Chem. 102:1971;517-529.
15. Esterbauer H., Zollner H., Scholz N. Reaction of glutathione with conjugated carbonyls. Z. Naturforsch. [C]. 30:1975;466-473.
16. Esterbauer H., Ertl A., Scholz N. The reaction of cysteine with α,β-unsaturated aldehydes. Tetrahedron. 32:1976;285-289.
17. Uchida K., Stadtman E.R. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc. Natl. Acad. Sci. USA. 89:1992;4544-4548.
18. Uchida K., Stadtman E.R. Selective cleavage of thioether linkage in protein modified with 4-hydroxynonenal. Proc. Natl. Acad. Sci. USA. 89:1992;5611-5615.
19. Uchida K., Stadtman E.R. Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase a possible involvement of intramolecular and intermolecular cross-linking reactions . J. Biol. Chem. 268:1993;6388-6393.
20. Sayre L.M., Arora P.K., Iyer R.S., Salomon R.G. Pyrrole formation from 4-hydroxynonenal and primary amines. Chem. Res. Toxicol. 6:1993;19-22.
21. Itakura K., Osawa T., Uchida K. Structure of a fluorescent compound from 4-hydroxy-2-nonenal and Nα-hippuryllysine a model for fluorophores derived from protein modifications by lipid peroxidation . J . Org. Chem. 63:1998;185-187.
22. Mark R.J., Lovell M.A., Markesbery W.R., Uchida K., Mattson M.P. A role for 4-hydroxynonenal in disruption of iron homeostasis and neuronal death induced by amyloid β-peptide. J. Neurochem. 68:1997;255-264.
23. Mark R.J., Pang Z., Geddes J.W., Uchida K., Mattson M.P. Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons involvement of membrane lipid peroxidation . J. Neurosci. 17:1997;1046-1054.
24. Keller J.N., Mark R.J., Bruce A.J., Blanc E.M., Rothstein J.D., Uchida K., Mattson M.P. 4-hydroxynonenal, an aldehydic product of membrane lipid peroxidation, impairs glutamate transport and mitochondrial function in synaptosomes. Neuroscience. 80:1997;685-696.
25. Blanc E.M., Kelly J.F., Mark R.J., Mattson M.P. 4-hydroxynonenal, an aldehydic product of lipid peroxidation, impairs signal transduction associated with muscarinic acetylcholine and metabotropic glutamate receptors possible action on G alpha(q/11) . J. Neurochem. 69:1997;570-580.
26. Mattson M.P., Fu W., Waeg G., Uchida K. 4-hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau. NeuroReport. 8:1997;2275-2281.
27. Chio K.S., Tappel A.L. Synthesis and characterization of the fluorescent products derived from malondialdehyde and amino acids. Biochemistry. 8:1969;2821-2827.
28. McGirr L.G., Hadley M., Draper H.H. Identification of Nα-acetyl-ε-(2-propenal)lysine as a urinary metabolite of malondialdehyde. J. Biol. Chem. 260:1985;15427-15431.
29. Draper H.H., Hadley M., Lissemore L., Laing N.M., Cole P.D. Identification of Nε-(2-propenal)lysine as a major urinary metabolite of malondialdehyde. Lipids. 23:1988;626-628.
30. Kikugawa K., Ido Y. Studies on peroxidized lipids. V. Formation and characterization of 1,4-dihydropyridine-3,5-dicarbaldehydes as model of fluorescent components in lipofuscin. Lipids. 19:1984;600-608.
31. Slatter D.A., Murray M., Bailey A.J. Formation of dihydropyridine derivative as a potential cross-link derived from malondialdehyde in physiological systems. FEBS Lett. 421:1998;180-184.
32. Itakura K., Uchida K., Osawa T. A novel fluorescent malondialdehyde-lysine adduct. Chem. Physiol. Lipids. 84:1996;75-79.
33. Wells-Knecht K.J., Brinkman E., Baynes J.W. Characterization of an imidazolium salt formed from glyoxal and Nα-hippuryllysine a model for Maillard reaction crosslinks in proteins . J. Org. Chem. 60:1995;6246-6247.
34. Schwarzenbolz U., Henle T., Haebner R., Klostermeyer H.Z. On the reaction of glyoxal with proteins. Lebensm. Unters. Forsch A. 205:1997;121-124.
35. Westwood M.E., Thornalley P.J. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins comparison with glucose-derived advanced glycation endproduct-modified serum albumins . J. Protein Chem. 14:1995;359-372.
36. Nagaraj R.H., Shipanova I.N., Faust F.M. Protein cross-linking by the Maillard reaction isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal . J. Biol. Chem. 271:1996;19338-19345.
37. Ahmed M.U., Thorpe S.R., Baynes J.W. Identification of Nε-carboxymethyllysine as a degradation product of fluctoselysine in glycated protein. J. Biol. Chem. 261:1986;4889-4894.
38. Oya T., Hattori N., Mizuno Y., Miyata S., Maeda S., Osawa T., Uchida K. Methylglyoxal modification of protein chemical and immunochemical characterization of methylglyoxal-arginine adducts . J. Biol. Chem. 274:1999;18492-18502.
39. Shipanova I.N., Glomb M.A., Nagaraj R.H. Protein modification by methylglyoxal chemical nature and synthetic mechanism of a major fluorescent adduct . Arch. Biochem. Biophys. 344:1997;29-36.
40. Weber A.L. Nonenzymatic formation of "energy-rich" lactoyl and glyceroyl thioesthers from glyceraldehyde and a thiol. J. Mol. Evol. 20:1984;157-166.
41. Hayase F., Nagaraj R.H., Miyata S., Njoroge F.G., Monnier V.M. Aging of proteins immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo . J. Biol. Chem. 263:1989;3758-3764.
42. Dyer D.G., Blackledge J.A., Thorpe S.R., Baynes J.W. Formation of pentosidine during nonenzymatic browning of proteins by glucose. J. Biol. Chem. 266:1991;11654-11660.
43. Niwa T., Katsuzaki T., Miyazaki S., Miyazaki T., Ishizaki Y., Hayase F., Tatemichi N., Takei Y. Immunohistochemical detection of imidazolone, a novel advanced glycation end product, in kidneys and aortas of diabetic patients. J. Clin. Invest. 99:1997;1272-1280.
44. Kawakishi S., Tsunehiro J., Uchida K. Autoxidative degradation of Amadori compounds in the presence of copper ion. Carbohydr. Res. 211:1991;167-171.
45. Cheng R.Z., Tsunehiro J., Uchida K., Kawakishi S. Oxidative damage of glycated protein in the presence of transition metal ion. Agr. Biol. Chem. 55:1991;1993-1998.
46. Baker J.R., Zyzak D.V., Thorpe S.R., Baynes J.W. Chemistry of the fructosamine assay D-glucosone is the product of oxidation of Amadori compounds . Clin. Chem. 40:1994;1950-1955.
47. Steinberg D. Role of oxidized LDL and antioxidants in atherosclerosis. Adv. Exp. Med. Biol. 369:1995;39-48.
48. Steinberg D., Parthasarathy S., Carew T.E., Khoo J.C., Witztum J.L. Modification of low-density lipoprotein that increases its atherogenecity. N. Engl. J. Med. 320:1989;915-924.
49. Bucala R., Makita Z., Koschinsky T., Cerami A., Vlassara H. Lipid advanced glycosylation pathway for lipid oxidation in vivo . Proc. Natl. Acad. Sci. USA. 90:1993;6434-6438.
50. Bucala R., Makita Z., Vega G., Grundy S., Koschinsky T., Cerami A., Vlassara H. Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency. Proc. Natl. Acad. Sci. USA. 91:1994;9441-9445.
51. Al-Abed Y., Liebich H., Voelter W., Bucala R. Hydroxyalkenal formation induced by advanced glycosylation of low density lipoprotein. J. Biol. Chem. 271:1996;2892-2896.
52. Uchida K., Toyokuni S., Nishikawa K., Kawakishi S., Oda H., Hiai H., Stadtman E.R. Michael addition-type 4-hydroxy-2-nonenal adducts in modified low density lipoproteins markers for atherosclerosis . Biochemistry. 33:1994;12487-12494.
53. Uchida K., Sakai K., Itakura K., Osawa T., Toyokuni S. Protein modification by lipid peroxidation products formation of malondialdehyde-derived Nε-(2-propenal)lysine in proteins . Arch. Biochem. Biophys. 346:1997;45-52.
54. Requena J.R., Fu M.-X., Ahmed M.U., Jenkins A.J., Lyons T.J., Baynes J.W., Thorpe S.R. Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein. Biochem. J. 322:1997;317-325.
55. Bolgar M.S., Yang C.-Y., Gaskell S.J. First direct evidence for lipid/protein conjugation in oxidized human low density lipoprotein. J. Biol. Chem. 271:1996;27999-28001.
56. Haberland M.E., Fong D., Cheng L. Malondialdehyde-altered protein occurs in atheroma of Watanabe Heritable Hyperlipidemic rabbits. Science. 241:1988;215-217.
57. Palinski W., Rosenfeld M.E., Ylä-Herttuala S., Gurtner G.C., Socher S.S., Butler S.W., Parthasarathy S., Carew T.E., Steinberg D. Low density lipoprotein undergoes oxidative modification in vivo. Proc. Natl. Acad. Sci. USA. 86:1989;1372-1376.
58. Uchida K., Itakura K., Kawakishi S., Hiai H., Toyokuni S., Stadtman E.R. Characterization of epitopes recognized by 4-hydroxy-2-nonenal specific antibodies. Arch. Biochem. Biophys. 324:1995;241-248.
59. Baynes J.W. Role of oxidative stress in development of complications in diabetes. Diabetes. 40:1991;405-412.
60. Shamsi F.A., Partal A., Sady C., Glomb M.A., Nagaraj R.H. Immunological evidence for methylglyoxal-derived modifications in vivo determination of antigenic epitopes . J. Biol. Chem. 273:1998;6928-6936.
61. Witztum J.L., Steinberg D. Role of oxidized low density lipoprotein in atherogenesis. J. Clin. Invest. 88:1991;1785-1792.
62. Berliner J.A., Navab M., Fogelman A.M., Frank J.S., Demer L.L., Edwards P.A., Watson A.D., Lusis A.J. Atherosclerosis basic mechanisms. Oxidation, inflammation, and genetics . Circulation. 91:1995;2488-2496.
63. Brand K., Eisele T., Kreusel U., Page M., Page S., Haas H., Gerling A., Kaltshmidt C., Neumann F.-J., Mackman N., Baeuerle P.A., Walli A.K., Neumeier D. Dysregulation of monocytic nuclear factor-kappa B by oxidized low-density lipoprotein. Arterioscler. Thromb. Vasc. Biol. 17:1997;1901-1907.
64. Uchida K., Shiraishi M., Naito Y., Torii Y., Nakamura Y., Osawa T. Activation of stress signaling pathways by the end-product of lipid peroxidation 4-hydroxy-2-nonenal is a potential inducer of intracellular peroxide production . J. Biol. Chem. 274:1999;2234-2242.
65. Che W., Asahi M., Takahashi M., Kaneto H.A., Okado A., Higashiyama S., Taniguchi N. Selective induction of heparin-binding epidermal growth factor-like growth factor by methylglyoxal and 3-deoxyglucosone in rat aortic smooth muscle cells. J. Biol. Chem. 272:1997;18453-18459.
66. Marshall C.J. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Gen. Dev. 4:1994;82-89.
67. Kyriakis J.M., Avruch J. Sounding the alarm. Protein kinase cascades activated by stress and inflammation. J. Biol. Chem. 271:1996;24313-24316.
68. Parola M., Robino G., Marra F., Pinzani M., Bellomo G., Leonnarduzzi 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. 102:1998;1942-1950.
69. Rao G.N., Glasgow W.C., Eling T.E., Runge M.S. Role of hydroperoxyeicosatetraenoic acid in oxidative stress-induced activating protein 1 (AP-1) activity. J. Biol. Chem. 271:1996;27760-27764.
70. 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. 97:1998;1071-1078.
71. Page S., Fischer C., Baumgartner B., Haas M., Kreusel U., Loidl G., Hayn M., Ziegler-Heitbrock H.W.L., Neumeier D., Brand K. 4-Hydroxynonenal prevents NF-κB activation and tumor necrosis factor expression by inhibiting IκB phosphorylation and subsequent proteolysis. J. Biol. Chem. 274:1999;11611-11618.
72. Horton N., Biswal S.S., Corrigan L.L., Bratta J., Kehrer J.P. Acrolein causes inhibitor κB-independent decreases in nuclear factor κB activation in human lung adenocarcinoma (A549) cells. J. Biol. Chem. 274:1999;9200-9206.
73. Rushmore T.H., Pickett C.B. Transcriptional regulation of the rat glutathione S-transfearse Ya subunit gene characterization of a xenobiotic-response element controlling inducible expression by phenolic anti-oxidants . J. Biol. Chem. 265:1990;14648-14653.
74. Nguyen T., Pickett C.B. Regulation of rat glutathione S-transferase Ya subunit gene expression DNA-protein interaction at the antioxidant responsive element . J. Biol. Chem. 267:1992;13535-13539.
75. Favreau L.V., Pickett C.B. The rat quinone reductase antioxidant response element identification of the nucleotide sequence required for basal and inducible activity and detection of antioxidant response-element binding proteins in hepatoma and non-hepatoma cell lines . J. Biol. Chem. 270:1995;24468-24474.
76. Fukuda A., Nakamura Y., Ohigashi H., Osawa T., Uchida K. Cellular response to the redox active lipid peroxidation products induction of glutathione S-transferase by 4-hydroxy-2-nonenal . Biochem. Biophys. Res. Commun. 236:1997;505-509.
77. Tjalkens R.B., Luckey S.W., Kroll D.J., Petersen D.R. α,β-unsaturated aldehydes increase glutathione S-transferase mRNA and protein correlation with activation of the antioxidant response element . Arch. Biochem. Biophys. 359:1998;42-50.
78. 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. 52:1992;4866-4871.
79. Parola M., Pinzani M., Casini A., Albano E., Poli G., Gentilini A., Gentilini P., Dianzani M.U. Stimulation of lipid peroxidation or 4-hydroxynonenal treatment increases procollagen α1 (I) gene expression in human liver fat-sorting cells. Biochem. Biophys. Res. Commun. 194:1993;1044-1050.
80. Spycher S., Tabataba-Vakili S., O'Donnell V.B., Palomba L., Azzi A. 4-hydroxy-2,3-trans-nonenal induces transcription and expression of aldose reductase. Biochem. Biophys. Res. Commun. 226:1996;512-516.
81. Rittner H.L., Hafner V., Klimiuk P.A., Szweda L.I., Goronzy J.J., Weyand C.M. Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis. J. Clin. Invest. 103:1999;1007-1013.
82. Barrera G., Pizzimenti S., Serra A., Ferretti C., Fazio V.M., Saglio G., 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. 227:1996;589-593.
83. Leonarduzzi G., Scavazza A., Biasi F., Chiarpotto E., Camandola S., Vogl S., Dargel R., Poli G. The lipid peroxidation end product 4-hydroxy-2-nonenal up-regulates transforming growth factor β1 expression in the macrophage lineage. A link between oxidative injury and fibrosclerosis. FASEB J. 11:1997;851-857.
84. Yang C.W., Vlassara H., Peten E.P., He C.J., Striker G.E., Striker L. Advanced glycation end products up-regulate gene expression found in diabetic glomerular disease. Proc. Natl. Acad. Sci. USA. 91:1994;9436-9440.