期刊
EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 267, 期 13, 页码 4171-4178出版社
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1432-1327.2000.01452.x
关键词
advanced glycation end products; Alzheimer's disease; beta-amyloid peptide; transition metals
beta-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 beta-amyloid peptide and glucose or fructose show that formation of covalently cross-linked high-molecular-mass beta-amyloid peptide oligomers is accelerated by micromolar amounts of copper (Cu+, Cu2+) and iron (Fe2+, Fe3+) 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 beta-amyloid deposits in vivo and possibly the progression of Alzheimer's disease.
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