BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지
DOI QR코드

DOI QR Code

Modification of Cu,Zn-Superoxide Dismutase by Oxidized Catecholamines

  • Published : 2004.05.31
Download PDF
⟨ Previous Next ⟩

Abstract

Oxidation of catecholamines may contribute to the pathogenesis of Parkinson's disease (PD). The effect of the oxidized products of catecholamines on the modification of Cu,Zn-superoxide dismutase (SOD) was investigated. When Cu,Zn-SOD was incubated with the oxidized 3,4-dihydroxyphenylalanine (DOPA) or dopamine, the protein was induced to be aggregated. The deoxyribose assay showed that hydroxyl radicals were generated during the oxidation of catecholamines in the presence of copper ion. Radical scavengers, azide, N-acetylcysteine, and catalase inhibited the oxidized catecholamine-mediated Cu,Zn-SOD aggregation. Therefore, the results indicate that free radicals may play a role in the aggregation of Cu,Zn-SOD. When Cu,Zn-SOD that had been exposed to catecholamines was subsequently analyzed by an amino acid analysis, the glycine and histidine residues were particularly sensitive. These results suggest that the modification of Cu,Zn-SOD by oxidized catecholamines might induce the perturbation of cellular antioxidant systems and led to a deleterious cell condition.

Keywords

References

  1. Bowling, A. C. and Beal, M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171. https://doi.org/10.1016/0024-3205(95)00055-B
  2. Dexter, D. T., Cater, C. J., Wells, F. R., Javoy-Agid, F., Agid, Y., Lees, A., Jenner, P. and Marsden, C. D. (1989) Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease. J. Neurochem. 52, 381-389. https://doi.org/10.1111/j.1471-4159.1989.tb09133.x
  3. Dexter, D. T., Jenner, P., Schapira, A. H. and Marsden, C. D. (1992) Alterations in levels of iron, ferritin and other trace metals in neurodegenerative disease affecting the basal ganglia. The Royal Kings and Queens Parkinsons Disease Research Group. Ann. Neurol. 32, S94-100. https://doi.org/10.1002/ana.410320716
  4. Graham, D. G. (1978) Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinines. Mol. Pharmacol. 14, 633-643.
  5. Graham, D. G.., Tiffany, S. M., Bell, W. R. Jr. and Gutknecht, W. F. (1978) Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro. Mol. Pharmacol. 14, 644-653.
  6. Halliwell, B. and Gutteridge, J. M. C. (1981) Formation of thiobarbituric-acid-reactive substance from deoxyribose in the presence of iron salts: the role of superoxide and hydroxyl radicals. FEBS Lett. 128, 347-352. https://doi.org/10.1016/0014-5793(81)80114-7
  7. Halliwell, B. and Gutteridge, J. M. C. (1992) Biologically relevant metal ion-dependent ${\cdot}OH$ generation. An uptake. FEBS Lett. 307, 108-112. https://doi.org/10.1016/0014-5793(92)80911-Y
  8. Ilic, T., Jovanovic, M., Jovicic A. and Tomovic, M. (1998) Oxidative stress and Parkinson's disease. Vojnosanit. Pregl. 55, 463-468.
  9. Ilic, T., Jovanovic, M., Jovicic, A. and Tomovic, M. (1999) Oxidative stress indicators are elevated in de novo Parkinson's disease patients. Funct. Neurol. 14, 141-147.
  10. Imlay, J. A., Chin, S.M. and Linn, S. (1988) Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240, 640-642. https://doi.org/10.1126/science.2834821
  11. Jellinger, K. A., Kienzl, E., Rumpelmaier, G., Paulus, W., Riederer, P., Stachelberger, H., Youdim, M. B. and Ben-Schachar, D. (1993) Iron and ferritin in substantia nigra in Parkinson' disease. Adv. Neurol. 60, 267-272.
  12. Jenner, P. (1996) Oxidative stress in Parkinsons disease and other neurodegenerative disorders. Pathol. Biol. (Paris) 44, 57-64.
  13. Kang, J. H., Choi, B. J. and Kim, S. M. (1997) Expression and characterization of recombinant human Cu,Zn-superoxide dismutase in Escherichia coli. J. Biochem. Mol. Biol. 30, 60-65.
  14. Kim, S. K., Park, P. J., Kim, J. B. and Shahidi, F. (2002) Purification and characterization of a collagenolytic protease from the filefish, Novoden modestrus. J. Biochem. Mol. Biol. 35, 165-171. https://doi.org/10.5483/BMBRep.2002.35.2.165
  15. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriphage $T_{4}$. Nature 227, 680-685.
  16. Lu, Y., LaCroix, L. B., Lowery, M. D., Solomomn, E. I., Bender, C. J. Peisach, J., Joe, J. A., Gralla, E. B. and Valentine, J. S. (1993) Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase. J. Am. Chem. Soc. 115, 5907-5918. https://doi.org/10.1021/ja00067a003
  17. McCord, J. M. and Fridovich, I. (1969) Superoxide dismutase. J. Biol. Chem. 224, 6049-6055.
  18. Maria, C. S., Revilla, E., Ayala, A., de la Cruz, C. P., and Machado, A. (1995) Changes in the histidine residues of Cu/Zn superoxide dismutase during aging. FEBS Lett. 374, 85-88. https://doi.org/10.1016/0014-5793(95)01083-Q
  19. Miller, D. M., Buettner, G. R. and Aust, S. D. (1990) Transition metals as catalysts of 'autoxidation' reactions. Free Radic. Biol. Med. 8, 95-108. https://doi.org/10.1016/0891-5849(90)90148-C
  20. Multhaup, G., Schlicksupp, A., Hesse, L., Behler, D., Ruppert, T., Masters, C. L. and Beyreuther, K. (1996) The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I). Science 271, 1406-1409. https://doi.org/10.1126/science.271.5254.1406
  21. O'Connell, M. J. and Peters, T. J. (1987) Ferritin and haemosiderin in free radical generation, lipid peroxidation and protein damage. Chem. Phys. Lipids 45, 241-249. https://doi.org/10.1016/0009-3084(87)90067-3
  22. Pall, H. S., Williams, A. C., Blake, D. R., Lunec, J., Gutteridge, J. M., Hall, M. and Taylor, A. (1987) Raised cerebrospinal-fluid copper concentration in Parkinson's disease. Lancet 2, 238-241.
  23. Pileblad, E., Slivka, A., Bratvold, D. and Cohen, G. (1988) Studies on the autoxidation of dopamine: interaction with ascorbate. Arch. Biochem. Biophys. 263, 447-452. https://doi.org/10.1016/0003-9861(88)90657-1
  24. Sagripanti, J. L. and Kraemer, K. H. (1989) Site-specific oxidative DNA damage at polyguanosines produced by copper plus hydrogen peroxide. J. Biol. Chem. 264, 1729-1734.
  25. Sagripanti, J. L., Swicord, M. L. and Davis, C. C. (1987) Microwave effects on plasmid DNA. Radiat. Res. 110, 219-231. https://doi.org/10.2307/3576900
  26. Sian, J., Dexter, D. T., Lees, A. J., Daniel, S., Agid, Y., Javoy-Agid, F., Jenner, P. and Marsden, C. D. (1994) Alterations in glutathione levels in Parkinsons disease and other neurodegenerative disorders affecting basal ganglia. Ann. Neurol. 36, 348-355. https://doi.org/10.1002/ana.410360305
  27. Sutton, H. C. and Winterbourn, C. C. (1989) On the participation of higher oxidation states of iron and copper in Fenton reactions. Free Radic. Biol. Med. 6, 53-60. https://doi.org/10.1016/0891-5849(89)90160-3
  28. Tainer, J. A., Gertzoff, E. D., Richardson, J. S. and Richardson, D. C. (1983) Structure and mechanism of copper, zinc superoxide dismutase. Nature 306, 284-287. https://doi.org/10.1038/306284a0
  29. Treerattrakool, S., Eurwlaichitr, L., Udomkit, A. and Panyim, S. (2002) Secretion of pem-CMG, a peptide in the CHH/MIH/GIH family of Penaeus monodin, in Phichia pastoris is detected by secretion signal of the $\alpha$-mating factor from Saccharomyces cerevisiae. J. Biochem. Mol. Biol. 35, 476-481. https://doi.org/10.5483/BMBRep.2002.35.5.476
  30. Waite, J. H. (1990) The physiology and chemical diversity of quinone-tanned glues and varnishes. Comp. Biochem. Physiol. 97, 19-29. https://doi.org/10.1016/0305-0491(90)90172-P

Cited by

  1. Enhanced Antioxidant Enzymes Are Associated with Reduced Hydrogen Peroxide in Barley Roots under Saline Stress vol.38, pp.2, 2005, https://doi.org/10.5483/BMBRep.2005.38.2.218
  2. Oxidative modification of human ceruloplasmin induced by a catechol neurotoxin, salsolinol vol.49, pp.1, 2016, https://doi.org/10.5483/BMBRep.2016.49.1.103
  3. Oxidative Stress and Antioxidant Capacity in Barley Grown under Space Environment vol.74, pp.7, 2010, https://doi.org/10.1271/bbb.100139