Study 25 of 26GHK-Cu literatureScience (New York, N.Y.)Top journal1996

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

Not reported in abstract.

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Where it sits

this study against the rest of the ghk-cu corpus

Preclinical · this one

Observational

Open-label

Randomised

Reviews

Summary and findings

Not reported in abstract.

How much of this paper we could read: title only (0.10). The feed gave us little more than the title, so our summary is thin. This says nothing about the study's quality — read the source. What this means →

1996

Abstract

The authors’ words, as Science (New York, N.Y.) supplied them

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.

Background

Not reported in abstract.

Methods

Not reported in abstract.

Results

Not reported in abstract.

Interpretation

Not reported in abstract.

Limitations

Not reported in abstract.

Elsewhere in the GHK-Cu corpus

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