Salsolinol, a catechol neurotoxin, induces oxidative modification of cytochrome c
2
조회
0
다운로드
1
인용
0
참고문헌
키워드
초록
Methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol),an endogenous neurotoxin, is known to perform a role in the pathogenesis of Parkinson’s disease (PD). In this study, we evaluated oxidative modification of cytochrome c occurring after incubation with salsolinol. When cytochrome c was incubated with salsolinol, protein aggregation increased in a dosedependent manner. The formation of carbonyl compounds and the release of iron were obtained in salsolinol- treated cytochrome c. Salsolinol also led to the release of iron from cytochrome c. Reactive oxygen species (ROS) scavengers and iron specific chelator inhibited the salsolinol-mediated cytochrome c modification and carbonyl compound formation. It is suggested that oxidative damage of cytochrome c by salsolinol might induce the increase of iron content in cells, subsequently leading to the deleterious condition which was observed. This mechanism may, in part, provide an explanation for the deterioration of organs under neurodegenerative disorders such as PD.
Abstract
Methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol),an endogenous neurotoxin, is known to perform a role in the pathogenesis of Parkinson’s disease (PD). In this study, we evaluated oxidative modification of cytochrome c occurring after incubation with salsolinol. When cytochrome c was incubated with salsolinol, protein aggregation increased in a dosedependent manner. The formation of carbonyl compounds and the release of iron were obtained in salsolinol- treated cytochrome c. Salsolinol also led to the release of iron from cytochrome c. Reactive oxygen species (ROS) scavengers and iron specific chelator inhibited the salsolinol-mediated cytochrome c modification and carbonyl compound formation. It is suggested that oxidative damage of cytochrome c by salsolinol might induce the increase of iron content in cells, subsequently leading to the deleterious condition which was observed. This mechanism may, in part, provide an explanation for the deterioration of organs under neurodegenerative disorders such as PD.
참고문헌 (35)
- Götz, M. E., "Oxidative stress: free radical production in neural degeneration", Pharmacol. Ther, 63, pp.37~122 (1994)
- Sandler, M., "Tetrahydroisoquinoline alkaloids: in vivo metabolites of L-dopa in man", Nature, 241, pp.439~443 (1973)
- Epp, L. M., "Chronic polysystemic candidiasis as a possible contributor to onset of idiopathic Parkinson's disease", Bratisl. Lek. Listy, 107, pp.227~230 (2006)
- DeCuypere, M., "Regional distribution of tetrahydroisoquinoline derivatives in rodent, human, and Parkinson's disease brain", J. Neurochem, 107, pp.1398~1413 (2008)
- Surh, Y. J., "Iron enhancement of oxidative DNA damage and neuronal cell death induced by salsolinol", J. Toxicol. Environ. Health Part A, 65, pp.473~488 (2002)
- Galaris, D., "Oxidative stress and iron homeostasis: mechanistic and health aspects", Crit. Rev. Clin. Lab. Sci, 45, pp.1~23 (2008)
- Thomas, M., "Neurodegenerative disease and iron storage in the brain", Curr. Opin. Neurol, 17, pp.437~442 (2004)
- Zecca, L., "Iron, brain ageing and neurodegenerative disorders", Nat. Rev. Neurosci, 5, pp.863~873 (2004)
- Vina, J., "Effect of gender on mitochondrial toxicity of Alzheimer’s Abeta peptide", Antioxid. Redox. Signal, 10, pp.1677~1690 (2007)
- Jomova, K., "Metals, oxidative stress and neurodegenerative disorders", Mol. Cell Biochem, 345, pp.91~104 (2010)
- Moore, G. R., "Cytochrome c: Evolution, Structure, and Physicochemical Aspects" (1990), Springer-Verlag
- Dumont, M. E., "Role of cytochrome c heme lyase in mitochondrial import and accumulation of cytochrome c in Saccharomyces cerevisiae", Mol. Cell Biol, 11, pp.5487~5496 (1991)
- Dumont, M. E., "Noncovalent binding of heme induces a compact apocytochrome c structure", Biochemistry, 33, pp.7368~7378 (1994)
- Pelletier, H., "Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c", Science, 258, pp.1748~1755 (1992)
- Wang, X., "Equilibrium thermodynamics of a physiologically-relevant heme-protein complex", Biochemistry, 38, pp.16876~16881 (1999)
- Li, P., "Cytochrome c and dATP-dependent formation of Apaf-1", caspase- 9 complex initiates an apoptotic protease cascade, 1997, pp.91, 479~489
- Hashimoto, M., "Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease", J. Biol. Chem, 274, pp.28849~28852 (1999)
- Green, D. R., "A matter of life and death", Cancer Cell, 1, pp.19~30 (2002)
- Friedlander, R. M., "Apoptosis and caspases in neurodegenerative diseases", N. Engl. J. Med, 348, pp.1365~1375 (2003)
- Stadtman, E. R., "Reactive oxygen- mediated protein oxidation in aging and disease", Drug. Metab. Rev, 30, pp.225~243 (1998)
- Stadtman, E. R., "Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal- catalyzed reactions", Annu. Rev. Biochem, 62, pp.797~821 (1993)
- Davies, K. J., "Intracellular proteolytic systems may function as secondary antioxidant defenses: an hypothesis", J. Free Radic. Biol. Med, 2, pp.155~173 (1986)
- Oliver, C. N., "A role of mixed-function oxidation reactions in the accumulation of altered enzyme forms during aging", J. Am. Geriatr. Soc, 35, pp.947~956 (1987)
- Goldstein, S., "Mechanism of reduction of bleomycin-Cu(II) by CO2- and oxidation of bleomycin- Cu(I) by H2O2 in the absence and presence of DNA", Free Radic. Res. Commun, 51, pp.693~706 (1987)
- Gutteridge, J. M, "The role of the superoxide and hydroxyl radicals in the degradation of DNA and deoxyribose induced by a copper-phenanthroline complex", Biochem. Pharmacol, 31, pp.2801~2805 (1982)
- Imlay, J. A., "Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro", Science, 240, pp.640~642 (1988)
- Prutz, W. A., "Inhibition of DNA-ethidium bromide intercalation due to free radical attack upon DNA. II. Copper(II)-catalysed DNA damage by O2 -ㆍ", Radiat. Environ. Biophys, 23, pp.7~18 (1984)
- Millett, F, "Structual studies; in Cytochrome c, A Multidisciplinary Approach", pp.475~487 (1996), University Science Books
- Jung, Y. J., "Oxidative DNA damage and cytotoxicity induced by copper-stimulated redox cycling of salsolinol, a neurotoxic tetrahydroisoquinolin alkaloid", Free Radic. Biol. Med, 30, pp.1407~1417 (2001)
- Wanpen, S., "Salsolinol, a dopamine-derived tetrahydroisoquinoline, induces cell death by causing oxidative stress in dopaminergic SH-SY5Y cells, and the said effect is attenuated by metallothionein", Brain Res, 1005, pp.67~76 (2004)
- Smith, P. K., "Measurement of protein using bicinchoninic acid", Anal. Biochem, 150, pp.76~85 (1985)
- Laemmli, U. K., "Cleavage of structural proteins during the assembly of the head of bacteriophage T4", Nature, 227, pp.680~685 (1970)
- Reznick, A. Z., "Oxidative damage to proteins: spectrophotometric method for carbonyl assay", Methods Enzymol, 233, pp.357~363 (1994)
- Sung Ho An, "Oxidative modification of ferritin induced by methylglyoxal", BMB Reports, 45(3), pp.147~152 (2012), 생화학분자생물학회
- Jung Hoon Kang, "Salsolinol, a tetrahydroisoquinoline-derived neurotoxin, induces oxidative modification of neurofilament-L: protection by histidyl dipeptides", BMB Reports, 45(2), pp.114~119 (2012), 생화학분자생물학회