Browse > Article

Iron Can Accelerate the Conjugation Reaction between Abeta 1-40 Peptide and MDA  

Park, Yong-Hoon (Inam Neuroscience Research Center, San bon Medical Center, Wonkwang University)
Jung, Jai-Yun (Department of Anesthesiology and Pain Medicine, San bon Medical Center, Wonkwang University)
Son, Il-Hong (Inam Neuroscience Research Center, San bon Medical Center, Wonkwang University)
Publication Information
Molecular & Cellular Toxicology / v.5, no.2, 2009 , pp. 108-112 More about this Journal
Abstract
Alzheimer's disease(AD) is a neurodegenerative disorder characterized pathologically by senile plaques, neurofibrillary tangles, and synapse loss. Especially, extracellular beta-amyloid (Abeta) deposition is a major pathological hallmark of Alzheimer's disease (AD). In AD senile plaques, high level of iron and car-bonylated Abeta were detected. Iron has a Lewis acid property which can increase the electrophilicity of carbonyls, which may react catalytically with nucleophiles, such as amines. Hence, this study investigated whether or not iron could promote the carbonylation of amine with malondialdehyde (MDA) in the physiological condition. As the basic study, we examined that iron might promote the conjugation reaction between propylamine, monoamine molecule and MDA in the physiological condition. As the concentration of iron increased, the fluorescence intensity produced from the conjugation reaction increased in a dose-dependent manner. Instead of propylamine, we applied the same reaction condition to Abeta 1-40 peptide, one of major components founded in AD senile plaques for the conjugation reaction. As the result, the fluorescence intensity produced from the conjugation reaction between Abeta 1-40 peptide and MDA showed the similar trend to that of the reaction used with propylamine. This study suggests that iron can accelerate the conjugation reaction of MDA to Abeta 1-40 peptide and play an another important role in deterioration of AD brain.
Keywords
Beta-amyloid; Iron; Conjugation; Malondialdehyde; Senile plaque; Alzheimer's disease;
Citations & Related Records

Times Cited By Web Of Science : 0  (Related Records In Web of Science)
연도 인용수 순위
  • Reference
1 Seidler, N. W., Craig, H. D. & Squire, T. J. Endogenous plastic composite material in the Alzheimer's brain. Med Hypotheses 67:467-470 (2006)   DOI   ScienceOn
2 Dei, R. et al. Lipid peroxidation and advanced glycation end products in the brain in normal aging and in Alzheimer's disease. Acta Neuropathol (Berl) 104:113-122 (2002)   DOI   ScienceOn
3 Wentworth, P. Jr. et al. Evidence for ozone formation in human atherosclerotic arteries. Science 302:1053-1056 (2003)   DOI   ScienceOn
4 Sayer, L. M. et al. Metal ions and oxidative protein modification in neurological disease. Ann Ist Super Sanita 41:143-164 (2005)   PUBMED   ScienceOn
5 Gubisne-Haberle, D. et al. Protein cross-linkage induced by formaldehyde derived from semicarbazide-sensitive amine oxidase-mediated deamination of methylamine. J Pharmacol Exp Therap 310:1125-1132 (2004)   DOI   ScienceOn
6 Kobayashi, S., Kakumoto, K. & Sugiura, M. Transition metal salts-catalyzed aza-Michael reactions of enones with carbamates. Org Lett 4:1319-1322 (2002)   DOI   PUBMED   ScienceOn
7 Yamada, S. et al. Immunochemical detection of a lipofuscin-like fluorophore derived from malondialdehyde and lysine. J Lipid Res 42:1187-1196 (2001)   PUBMED   ScienceOn
8 Sayre, L. M., Moreira, P. I., Smith, M. A. & Perry, G. Metal ions and oxidative protein modification in neurological disease. Ann Ist Super Sanita 41:143-164 (2005)   PUBMED   ScienceOn
9 Klein, W. L., Stine, W. B. Jr. & Teplow, D. B. Small assemblies of unmodified amyloid-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 25:569-580 (2004)   DOI   ScienceOn
10 Castegna, A. et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic Biol Med 33:562-571 (2002)   DOI   ScienceOn
11 Chen, K., Kazachkov, M. & Yu, P. H. Effect of aldehydes derived from oxidative deamination and oxidative stress on beta-amyloid aggregation; pathological implications to Alzheimer's disease. J Neural Transm 114:835-839 (2007)   DOI   ScienceOn
12 Butterfield, D. A., Perluigi, M. & Sultana, R. Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur J Pharmacol 545:39-50 (2006)   DOI   ScienceOn
13 Zhang, Q. et al. Metabolite-initiated protein misfolding may trigger Alzheimer's disease. Proc Natl Acad Sci USA 101:4752-4757 (2004)   DOI   ScienceOn
14 Chen, K., Maley, J. & Yu, P. H. Potential implications of endogenous aldehydes in beta-amyloid misfolding, oligomerization and fibrillogenesis. Journal of Neurochemistry 99:1413-1424 (2006)   DOI   ScienceOn
15 Dyrks, T. et al. Amyloidogenicity of $\beta$A4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J Biol Chem 267:18210-18217 (1992)   PUBMED
16 Bush, A. L. et al. Modulation of A/3 adhesiveness and secretase site cleavage by zinc. J Biol Chem 269:12152-12158 (1994)   PUBMED
17 Mori, H. et al. Mass spectrometry of purified amyloid beta protein in Alzheimer's disease. J Biol Chem 267:17082-17086 (1992)   PUBMED
18 Hensley, K. et al. Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation. J Neurochem 65:2146-2156 (1995)   DOI   PUBMED   ScienceOn
19 Kayed, R. et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489 (2003)   DOI   PUBMED   ScienceOn
20 Stanyer, L., Betteridge, D. J. & Smith, C. C. Exaggerated polymerization of beta-amyloid 40 stimulated by plasma lipoproteins results in fibrillar Abeta preparations that are ineffective in promoting ADP-induced platelet aggregation. Biochim Biophys Acta 1674:305-311 (2004)   DOI   PUBMED   ScienceOn
21 Castegna, A. et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alphaenolase and heat shock cognate 71. J Neurochem 82:1524-1532 (2002)   DOI   ScienceOn
22 Liu, G. et al. Metal exposure and Alzheimer's pathogenesis. J Struct Biol 155:45-51 (2006)   DOI   ScienceOn
23 Chua, C. M. et al. The iron (III) chloride-mediated 1,4-addition of mercaptans to $\alpha,\beta$-unsaturated ketones and esters under solvent free conditions. Tetrahedron Letters 47:7375-7380 (2006)   DOI   ScienceOn
24 Esterbauer, H., Schaur, R. J. & Zollner, H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radical Biol Med 11:81-128 (1991)   DOI   ScienceOn
25 Katzman, R. & Saitoh, T. Advances in Alzheimer's disease. FASEB J 5:278-286 (1991)   DOI
26 Selkoe, D. J. Alzheimer's disease: genes, protein and therapy. Physiol Rev 81:741-766 (2002)   ScienceOn
27 Loo, D. T. et al. Apoptosis is induced by beta-amyloid in cultured central nervous system neurons. Proc Natl Acad Sci USA 90:7951-7955 (1993)   DOI   ScienceOn
28 Mantyh, P. W. et al. Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of beta-amyloid peptide. J Neurochem 61:1171-1174(1993)   DOI   PUBMED
29 Lovell, M. A. et al. Copper, iron and zinc in Alzheimer's disease senile plaques. J Neurol Sci 158:47-52 (1998)   DOI   ScienceOn
30 Dib, M. et al. Can MDA be used as a biological marker of progression in neurodegenerative disease? J Neurol 249:367-374 (2002)   DOI   ScienceOn
31 Sayre, L. M. et al. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J Neurochem 68:2092-2097 (1997)   DOI   PUBMED   ScienceOn
32 Ma, J. et al. Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372:92-94 (1994)   DOI   PUBMED   ScienceOn