Oxidative Medicine and Cellular Longevity
Volume 2011 (2011), Article ID 213686, 8 pages
http://dx.doi.org/10.1155/2011/213686
4-Hydroxy-2-Nonenal-Modified Glyceraldehyde-3-Phosphate Dehydrogenase Is Degraded by Cathepsin G in Rat Neutrophils
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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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