Table of Contents Author Guidelines Submit a Manuscript
Table of Contents Alerts

To receive news and publication updates for Oxidative Medicine and Cellular Longevity, enter your email address in the box below.

Oxidative Medicine and Cellular Longevity
Volume 2011, Article ID 213686, 8 pages
http://dx.doi.org/10.1155/2011/213686
Research Article

4-Hydroxy-2-Nonenal-Modified Glyceraldehyde-3-Phosphate Dehydrogenase Is Degraded by Cathepsin G in Rat Neutrophils

Yukihiro Tsuchiya,1 Go Okada,2 Shigeki Kobayashi,3 Toshiyuki Chikuma,3 and Hiroshi Hojo2

1Department of Degenerative Neurological Diseases, National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan
2Department of Hygienic Chemistry, Showa Pharmaceutical University, 3-3165 Higashi-Tamagawagakuen, Machida, Tokyo 194-8543, Japan
3Department of Analytical Chemistry of Medicines, Showa Pharmaceutical University, 3-3165 Higashi-Tamagawagakuen, Machida, Tokyo 194-8543, Japan

Received 26 November 2010; Accepted 17 January 2011

Academic Editor: Kenneth Maiese

Copyright © 2011 Yukihiro Tsuchiya et al. 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. J. Bouayed, H. Rammal, and R. Soulimani, “Oxidative stress and anxiety. Relationship and cellular pathways,” Oxidative Medicine and Cellular Longevity, vol. 2, no. 2, pp. 1–5, 2009. View at Google Scholar · View at Scopus
  2. M. M. Elahi, Y. U. X. Kong, and B. M. Matata, “Oxidative stress as a mediator of cardiovascular disease,” Oxidative Medicine and Cellular Longevity, vol. 2, no. 5, pp. 259–269, 2009. View at Google Scholar · View at Scopus
  3. E. E. Essick and F. Sam, “Oxidative stress and autophagy in cardiac disease, neurological disorders, aging and cancer,” Oxidative Medicine and Cellular Longevity, vol. 3, no. 3, pp. 168–177, 2010. View at Publisher · View at Google Scholar · View at PubMed
  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,” Journal of Clinical Investigation, vol. 111, no. 5, pp. 583–593, 2003. View at Publisher · View at Google Scholar
  5. K. Uchida, “4-Hydroxy-2-nonenal: a product and mediator of oxidative stress,” Progress in Lipid Research, vol. 42, no. 4, pp. 318–343, 2003. View at Publisher · View at Google Scholar · View at Scopus
  6. 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
  7. C. M. Lauderback, J. M. Hackett, F. F. Huang et al., “The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Aβ1-42,” Journal of Neurochemistry, vol. 78, no. 2, pp. 413–416, 2001. View at Publisher · View at Google Scholar · View at Scopus
  8. W. R. Markesbery and M. A. Lovell, “Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease,” Neurobiology of Aging, vol. 19, no. 1, pp. 33–36, 1998. View at Publisher · View at Google Scholar · View at Scopus
  9. M. E. Rosenfeld, W. Palinski, S. Yla-Herttuala, S. Butler, and J. L. Witztum, “Distribution of oxidation specific lipid-protein adducts and apolipoprotein B in atherosclerotic lesions of varying severity from WHHL rabbits,” Arteriosclerosis, vol. 10, no. 3, pp. 336–349, 1990. View at Google Scholar · View at Scopus
  10. 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
  11. T. Ishii, E. Tatsuda, S. Kumazawa, T. Nakayama, and K. Uchida, “Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase,” Biochemistry, vol. 42, no. 12, pp. 3474–3480, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  12. L. I. Szweda, K. Uchida, L. Tsai, and E. R. Stadtman, “Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Selective modification of an active-site lysine,” Journal of Biological Chemistry, vol. 268, no. 5, pp. 3342–3347, 1993. View at Google Scholar · View at Scopus
  13. D. L. V. Jagt, L. A. Hunsaker, T. J. V. Jagt et al., “Inactivation of glutathione reductase by 4-hydroxynonenal and other endogenous aldehydes,” Biochemical Pharmacology, vol. 53, no. 8, pp. 1133–1140, 1997. View at Publisher · View at Google Scholar · View at Scopus
  14. D. W. Davis, R. F. Hamilton, and A. Holian, “4-hydroxynonenal inhibits interleukin-1β converting enzyme,” Journal of Interferon and Cytokine Research, vol. 17, no. 4, pp. 205–210, 1997. View at Google Scholar · View at Scopus
  15. R. J. Mark, M. A. Lovell, W. R. Markesbery, K. Uchida, and M. P. Mattson, “A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β- peptide,” Journal of Neurochemistry, vol. 68, no. 1, pp. 255–264, 1997. View at Google Scholar · View at Scopus
  16. W. Liu, A. A. Akhand, M. Kato et al., “4-Hydroxynonenal triggers an epidermal growth factor receptor-linked signal pathway for growth inhibition,” Journal of Cell Science, vol. 112, no. 14, pp. 2409–2417, 1999. View at Google Scholar · View at Scopus
  17. K. Okada, C. Wangpoengtrakul, T. Osawa, S. Toyokuni, K. Tanaka, and K. Uchida, “4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules,” Journal of Biological Chemistry, vol. 274, no. 34, pp. 23787–23793, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. T. Grune and K. J. A. Davies, “The proteasomal system and HNE-modified proteins,” Molecular Aspects of Medicine, vol. 24, no. 4-5, pp. 195–204, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. K. J. A. Davies, “Degradation of oxidized proteins by the 20S proteasome,” Biochimie, vol. 83, no. 3-4, pp. 301–310, 2001. View at Publisher · View at Google Scholar · View at Scopus
  20. C. Marques, P. Pereira, A. Taylor et al., “Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells,” FASEB Journal, vol. 18, no. 12, pp. 1424–1426, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. M. A. Sirover, “New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase,” Biochimica et Biophysica Acta, vol. 1432, no. 2, pp. 159–184, 1999. View at Publisher · View at Google Scholar · View at Scopus
  22. M. A. Sirover, “New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells,” Journal of Cellular Biochemistry, vol. 95, no. 1, pp. 45–52, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  23. D. A. Butterfield, S. S. Hardas, and M. L.B. Lange, “Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration,” Journal of Alzheimer's Disease, vol. 20, no. 2, pp. 369–393, 2010. View at Publisher · View at Google Scholar · View at PubMed
  24. M. Yamaguchi, Y. Tsuchiya, K. Hishinuma, T. Chikuma, and H. Hojo, “Conformational change of glyceraldehyde-3-phosphate dehydrogenase induced by acetylleucine chloromethyl ketone is followed by unique enzymatic degradation,” Biological and Pharmaceutical Bulletin, vol. 26, no. 12, pp. 1648–1651, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. Y. Tsuchiya, M. Yamaguchi, T. Chikuma, and H. Hojo, “Degradation of glyceraldehyde-3-phosphate dehydrogenase triggered by 4-hydroxy-2-nonenal and 4-hydroxy-2-hexenal,” Archives of Biochemistry and Biophysics, vol. 438, no. 2, pp. 217–222, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  26. Y. Tsuchiya, Y. Okuno, K. Hishinuma et al., “4-Hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G,” Free Radical Biology and Medicine, vol. 43, no. 12, pp. 1604–1615, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  27. K. M. Heutinck, I. J.M. ten Berge, C. E. Hack, J. Hamann, and A. T. Rowshani, “Serine proteases of the human immune system in health and disease,” Molecular Immunology, vol. 47, no. 11-12, pp. 1943–1955, 2010. View at Publisher · View at Google Scholar · View at PubMed
  28. C. Summers, S. M. Rankin, A. M. Condliffe, N. Singh, A. M. Peters, and E. R. Chilvers, “Neutrophil kinetics in health and disease,” Trends in Immunology, vol. 31, no. 8, pp. 318–324, 2010. View at Publisher · View at Google Scholar · View at PubMed
  29. M. Häger, J. B. Cowland, and N. Borregaard, “Neutrophil granules in health and disease,” Journal of Internal Medicine, vol. 268, no. 1, pp. 25–34, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  30. 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,” Chemical Research in Toxicology, vol. 13, no. 7, pp. 557–564, 2000. View at Publisher · View at Google Scholar · View at Scopus
  31. J. Whitsett, M. J. Picklo, 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 PubMed · View at Scopus
  32. P. V. Usatyuk and V. Natarajan, “Role of mitogen-activated protein kinases in 4-hydroxy-2-nonenal-induced actin remodeling and barrier function in endothelial cells,” Journal of Biological Chemistry, vol. 279, no. 12, pp. 11789–11797, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  33. P. V. Usatyuk, N. L. Parinandi, and V. Natarajan, “Redox regulation of 4-hydroxy-2-nonenal-mediated endothelial barrier dysfunction by focal adhesion, adherens, and tight junction proteins,” Journal of Biological Chemistry, vol. 281, no. 46, pp. 35554–35566, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  34. Y. Yang, Y. Yang, M. B. Trent et al., “Glutathione-S-transferase A4-4 modulates oxidative stress in endothelium: possible role in human atherosclerosis,” Atherosclerosis, vol. 173, no. 2, pp. 211–221, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  35. J. Li, R. Sharma, B. Patrick et al., “Regulation of CD95 (Fas) expression and Fas-mediated apoptotic signaling in HLE B-3 cells by 4-hydroxynonenal,” Biochemistry, vol. 45, no. 40, pp. 12253–12264, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  36. D. A. Butterfield, H. F. Poon, D. ST. Clair et al., “Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease,” Neurobiology of Disease, vol. 22, no. 2, pp. 223–232, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. D. A. Butterfield, T. Reed, S. F. Newman, and R. Sultana, “Roles of amyloid β-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment,” Free Radical Biology and Medicine, vol. 43, no. 5, pp. 658–677, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  38. T. Reed, M. Perluigi, R. Sultana et al., “Redox proteomic identification of 4-Hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease,” Neurobiology of Disease, vol. 30, no. 1, pp. 107–120, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  39. C. T. N. Pham, “Neutrophil serine proteases: specific regulators of inflammation,” Nature Reviews Immunology, vol. 6, no. 7, pp. 541–550, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. B. Korkmaz, T. Moreau, and F. Gauthier, “Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions,” Biochimie, vol. 90, no. 2, pp. 227–242, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  41. D. A. Ferrington and R. J. Kapphahn, “Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal,” FEBS Letters, vol. 578, no. 3, pp. 217–223, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  42. B. Friguet and L. I. Szweda, “Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein,” FEBS Letters, vol. 405, no. 1, pp. 21–25, 1997. View at Publisher · View at Google Scholar · View at Scopus
  43. D. Botzen and T. Grune, “Degradation of HNE-modified proteins—possible role of ubiquitin,” Redox Report, vol. 12, no. 1-2, pp. 63–67, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  44. J. S. Ho, J. P. Buchweitz, R. A. Roth, and P. E. Ganey, “Identification of factors from rat neutrophils responsible for cytotoxicity to isolated hepatocytes,” Journal of Leukocyte Biology, vol. 59, no. 5, pp. 716–724, 1996. View at Google Scholar · View at Scopus
  45. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Google Scholar · View at Scopus
  46. U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970. View at Publisher · View at Google Scholar · View at Scopus
  47. P. Ferrer-Lopez, P. Renesto, M. Schattner, S. Bassot, P. Laurent, and M. Chignard, “Activation of human platelets by C5a-stimulated neutrophils: a role for cathepsin G,” American Journal of Physiology, vol. 258, no. 6, pp. C1100–C1107, 1990. View at Google Scholar · View at Scopus
  48. B. Löser, S. O. Kruse, M. F. Melzig, and A. Nahrstedt, “Inhibition of neutrophil elastase activity by cinnamic acid derivatives from Cimicifuga racemosa,” Planta Medica, vol. 66, no. 8, pp. 751–753, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. K. Suzuki, H. Ota, and S. Sasagawa, “Assay method for myeloperoxidase in human polymorphonuclear leukocytes,” Analytical Biochemistry, vol. 132, no. 2, pp. 345–352, 1983. View at Google Scholar · View at Scopus