Publication Date:
1996-03-08
Description:
The transition metal ion copper(II) has a critical role in chronic neurologic diseases. The amyloid precursor protein (APP) of Alzheimer's disease or a synthetic peptide representing its copper-binding site reduced bound copper(II) to copper(I). This copper ion-mediated redox reaction led to disulfide bond formation in APP, which indicated that free sulfhydryl groups of APP were involved. Neither superoxide nor hydrogen peroxide had an effect on the kinetics of copper(II) reduction. The reduction of copper(II) to copper(I) by APP involves an electron-transfer reaction and could enhance the production of hydroxyl radicals, which could then attack nearby sites. Thus, copper-mediated toxicity may contribute to neurodegeneration in Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Multhaup, G -- Schlicksupp, A -- Hesse, L -- Beher, D -- Ruppert, T -- Masters, C L -- Beyreuther, K -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1406-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ZMBH-Center for Molecular Biology Heidelberg, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596911" target="_blank"〉PubMed〈/a〉
Keywords:
Alzheimer Disease/*metabolism
;
Amyloid beta-Protein Precursor/antagonists & inhibitors/chemistry/*metabolism
;
Binding Sites
;
Copper/*metabolism
;
Cysteine/chemistry
;
Cystine/metabolism
;
Electron Transport
;
Ferric Compounds/metabolism
;
Histidine/chemistry
;
Humans
;
Hydrogen Peroxide/metabolism
;
Hydroxyl Radical/metabolism
;
Mass Spectrometry
;
Oligopeptides/pharmacology
;
Oxidation-Reduction
;
Peptide Fragments/chemistry/metabolism
;
Recombinant Fusion Proteins/metabolism
;
Superoxides/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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