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Transition metal-mediated glycoxidation accelerates cross-linking of β-amyloid peptide.
- Source :
- European Journal of Biochemistry; Jul2000 Part 1, Vol. 267 Issue 13, p4171-4178, 8p, 2 Diagrams, 8 Graphs
- Publication Year :
- 2000
-
Abstract
- β-Amyloid deposits, hallmarks of Alzheimer’s disease, contain both sugar-derived ‘advanced glycation end products’ (AGEs) and copper and iron ions. Our in vitro experiments using synthetic β-amyloid peptide and glucose or fructose show that formation of covalently cross-linked high-molecular-mass β-amyloid peptide oligomers is accelerated by micromolar amounts of copper (Cu<superscript>+</superscript>, Cu<superscript>2+</superscript>) and iron (Fe<superscript>2+</superscript>, Fe<superscript>3+</superscript>) ions. Formation of these covalent AGE cross-links can be inhibited by capping agents of amino groups, redox-inactive metal chelators and antioxidants, suggesting that these drugs may be able to slow down the formation of insoluble β-amyloid deposits in vivo and possibly the progression of Alzheimer’s disease. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMYLOID beta-protein
ALZHEIMER'S disease
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 267
- Issue :
- 13
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 5169358
- Full Text :
- https://doi.org/10.1046/j.1432-1327.2000.01452.x