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Science. 1996 Mar 8;271(5254):1406-9.

The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)

Author information

1
ZMBH-Center for Molecular Biology Heidelberg, University of Heidelberg, Germany.

Abstract

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.

PMID:
8596911
DOI:
10.1126/science.271.5254.1406
[Indexed for MEDLINE]

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