A common pathway for intracellular reactive oxygen species production by glycoxidative and nitroxidative stress in vascular endothelial cells and smooth muscle cells

Annals of the New York Academy of Sciences

Volumn 1043, Issue , 2005, Pages 521-528

  Taniguchi, Naoyuki ^a   Takahashi, Motoko ^a   Sakiyama, Haruhiko ^a   Park, Yong Seek ^a   Asahi, Michio ^a   Misonou, Yoshiko ^a   Miyamoto, Yasuhide ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

Dicarbonyl compound; Glycoxidative stress; Nitroxidative stress; ROS

Indexed keywords

3 DEOXYGLUCOSONE; ANTIOXIDANT; CARBONYL DERIVATIVE; GLUCOSE; METHYLGLYOXAL; REACTIVE OXYGEN METABOLITE;

ANTIOXIDANT ACTIVITY; CONFERENCE PAPER; CONTROLLED STUDY; ENDOTHELIUM CELL; GLUCOSE OXIDATION; HUMAN; HUMAN CELL; HUMAN UMBILICAL VEIN ENDOTHELIAL CELL; NITROSATION; OXIDATIVE STRESS; SIGNAL TRANSDUCTION; SMOOTH MUSCLE FIBER; VASCULAR ENDOTHELIUM;

EID: 23744515185     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1196/annals.1333.059     Document Type: Conference Paper

References (34)

1. OKADO, A., Y. KAWASAKI, Y. HASUIKE, et al. 1996. Induction of apoptotic cell death by methylglyoxal and 3-deoxyglucosone in macrophage-derived cell lines. Biochem. Biophys. Res. Commun. 225: 219-224.
2. DU, J., H. SUZUKI, F. NAGASE, et al. 2001. Superoxide-mediated early oxidation and activation of ASK1 are important for initiating methylglyoxal-induced apoptosis process. Free Radic. Biol. Med. 31: 469-478.
3. KIKUCHI, S., K. SHINPO, F. MORISAKA, et al. 1999. Neurotoxicity of methylglyoxal and 3-deoxyglucosone on cultured cortical neurons: synergism between glycation and oxidative stress, possibly involved in neurodegenerative diseases. J. Neurosci. Res. 57: 280-289.
4. CHE, W., M. ASAHI, M. TAKAHASHI, et al. 1997. Selective induction by methylglyoxal and 3-deoxyglucosone in rat aortic smooth muscle cells. The involvement of reactive oxygen species formation and a possible implication for atherogenesis in diabetes. J. Biol. Chem. 272: 18453-18459.
5. NIWA, T. & S. TSUKUSHI. 2001. 3-Deoxyglucosone and AGEs in uremic complications: inactivation of glutathione peroxidase by 3-deoxyglucosone. Kidney Int. 78: S37-S41.
6. WU, L. & B.H. JUURLINK. 2002. Increased methyglyoxal and oxidative stress in hypertensive rat vascular smooth muscle cells. Hypertension 39: 809-814.
7. PARK, Y.S., Y.H. KOH, M. TAKAHASHI, et al. 2003. Identification of the binding site of methylglyoxal on glutathione peroxidase: mathylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185. Free Radic. Res. 37: 205-211.
8. YIM, H.S., S.O. KANG, Y.C. HAH, et al. 1995. Free radicals generated during the glycation reaction of amino acids by methyglyoxal. A model study of protein-cross-linked free radicals. J. Biol. Chem. 270: 28228-28233.
9. THORNALLY, P.J., A. LANGBORG & H.S. MINHAS. 1999. Formation of glyoxal, methylglyoxal, and 3-dexyglucosone in the glycation of proteins by glucose. Biochem. J. 344: 109-116.
10. KANAZU, T., M. SHINODA, T. NAKAYAMA, et al. 1991. Aldehyde reductase is a major protein associated with 3-deoxyglucosone reductase activity in rat, pig, and human livers. Biochem. J. 279: 903-906.
11. TAKAHASHI, M., J. FUJII, T. TESHIMA, et al. 1993. Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver extablished by amino acid sequencing and cDNA expression. Gene 127: 249-253.
12. MCLELLAN, A.C., P.J. THORNALLEY, J. BENN & P.H. SONKSEN. 1994. Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. 87:21-29.
13. YAMADA, H., S. MIYATA, N. IGAKI, et al. 1994. Increase in 3-deoxyglucosone levels in diabetic rat plasma: specific in vivo determination of intermediate in advanced Maillard reaction. J. Biol. Chem. 269: 20275-20280.
14. WESTWOOD, M.E., O.K. ARGIROV, E.A. ABORDO & P.J. THORNALLEY. 1997. Methylglyoxal-modified arginine residues: a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells. Biochem. Biophys. Acta 1356: 84-94.
15. SEIDLER, N.W. & C. KOWALEWSKI. 2003. Methylglyoxal-induced glycation affects protein topography. Arch. Biochem. Biophys. 410: 149-154.
16. UCHIDA, K., O.T. KHOR, T. OYA, et al. 1997. Protein modification by a Maillard reaction intermediate methyglyoxal. Immunochemical detection of fluorescent 5-methylimidazolone derivatives in vivo. FEBS Lett. 410: 313-318.
17. KINTER, M. & R.J. ROBERTS. 1996. Glutathione consumption and glutathione peroxidase inactivation in fibroblast cell lines by 4-hydroxy-2-nonenal. Free Radic. Biol. Med. 21: 457-462.
18. KOH, Y.H., Y.S. PARK, M. TAKAHASHI, et al. 2000. Aldehyde reductase gene expression by lipid peroxidation end products MDA and HNE. Free Radic. Res. 33: 739-746.
19. ESTERBAUER, H., R.J. SCHAUR & H. ZOLLNER. 1991. Chemistry and biochemistry of 4-hydrozynonenal, malonaldehyde, and related aldehydes. Free Radic. Bio. Med. 11: 81-128.
20. UCHIDA, K., M. KANEMATSU, Y. MORIMITSU, et al. 1998. Acrolein is a product of lipid peroxidation reaction. J. Biol. Chem. 273: 16058-16066.
21. FURUHATA, A., T. ISHII, S. KUMAZAWA, et al. 2003. Ne-(3-methylpyridinium) lysine, a major antigenic adduct generated in acrolein-modified protein. J. Biol. Chem. 278: 48658-48665.
22. CAO, Z., D. HARDEJ, L.D. TROMBETTA, et al. 2003. Induction of cellular glutathione and glutathione S-transferase by 3H-1,2-dithiole-3-thione in rat aortic smooth muscle A1O cells: protection against acrolein-induced toxicity. Atherosclerosis 166: 291-301.
23. NARDINI, M., E.I. FINKELSTEIN, S. REDDY, et al. 2002. Acrolein-induced cytotoxicity in cultured human bronchial epithelial cells. Toxicology 173: 173-185.
24. AL-MAGHREBI, M.A., F. AL-MULLA & L.T. BENOV. 2003. Glycoaldehyde induces apoptosis in a human breast cancer cell line. Arch. Biochem. Biophys. 417: 123-127.
25. CLANCY, R.M., J. LESZCZYNSKA-PIZIAK & S.B. ABRAMSON. 1992. Nitric oxide, an endothelial cell relaxation factor, inhibits neutrophil Superoxide anion production via a direct action on the NADPH oxidase. J. Clin. Invest. 90: 1116-1121.
26. ASAHI, M., J. FUJII, K. SUZUKI, et al. 1995. Inactivation of glutathione peroxidase by nitric oxide. Implication for cytotoxicity. J. Biol. Chem. 270: 21035-21039.
27. ASAHI, M., J. FUJII, T. TAKAO, et al. 1997. The oxidation of selenocysteine is involved in the inactivation of glutathione peroxidase by nitric oxide donor. J. Biol. Chem. 272: 19152-19157.
28. FUJII, J. & N. TANIGUCHI. 1999. Down regulation of superoxide dismutases and glutathione peroxidase by reactive oxygen and nitrogen species. Free Radic. Res. 31: 301-308.
29. KOH, Y.H., K. SUZUKI, W. CHE, et al. 2001. Inactivation of glutathione peroxide by NO leads to the accumulation of H2O2 and the induction of HB-EGF via c-Jun NH2-terminal kinase in rat aortic smooth muscle cells. FASEB J. 15: 1472-1474.
30. HALLIWELL, B. & J.M.C. GUTTERIDGE. 1989. Free Radicals in Biology and Medicine, 3rd edit. Clarendon Press. Oxford.
31. ISCHIROPOULOS, H. & A.B. AL-MEHDI. 1995. Peroxynitrite-mediated oxidation protein modifications. FEBS Lett. 364: 279-282.
32. PADMAJA, S., G.L. SQUADRITO & W.A. PRYOR. 1998. Inactivation of glutathione peroxidase by peroxynitrite. Arch. Biochem. Biophys. 349: 1-6.
33. PARK, Y.S., N. FUJIWARA, Y.H. KHO, et al. 2002. Induction of thioredoxin reductase gene expression by peroxynitrite in human umbilical vein endothelial cells. Biol. Chem. 383: 683-691.
34. LIN, K.T., J.Y. XUE, M. NOMEN, et al. 1995. Peroxynitrite-induced apoptosis in HL-60 cells. J. Biol. Chem. 270: 16487-16490.