SOD1 rescues cerebral endothelial dysfunction in mice overexpressing amyloid precursor protein
- 1 February 1999
- journal article
- research article
- Published by Springer Nature in Nature Neuroscience
- Vol. 2 (2) , 157-161
- https://doi.org/10.1038/5715
Abstract
Peptides derived from proteolytic processing of the β–amyloid precursor protein (APP), including the amyloid–β peptide, are important for the pathogenesis of Alzheimer's dementia. We found that transgenic mice overexpressing APP have a profound and selective impairment in endothelium–dependent regulation of the neocortical microcirculation. Such endothelial dysfunction was not found in transgenic mice expressing both APP and superoxide dismutase–1 (SOD1) or in APP transgenics in which SOD was topically applied to the cerebral cortex. These cerebrovascular effects of peptides derived from APP processing may contribute to the alterations in cerebral blood flow and to neuronal dysfunction in Alzheimer's dementia.Keywords
This publication has 42 references indexed in Scilit:
- Amyloid‐β Deposition in Alzheimer Transgenic Mice Is Associated with Oxidative StressJournal of Neurochemistry, 1998
- Characteristics of thein VitroVasoactivity of β-Amyloid PeptidesExperimental Neurology, 1998
- Amyloid β‐Peptide Induces Cell Monolayer Albumin Permeability, Impairs Glucose Transport, and Induces Apoptosis in Vascular Endothelial CellsJournal of Neurochemistry, 1997
- Cerebrovascular endothelial dysfunction mediated by β-amyloidNeuroReport, 1997
- RAGE and amyloid-β peptide neurotoxicity in Alzheimer's diseaseNature, 1996
- β-Amyloid-mediated vasoactivity and vascular endothelial damageNature, 1996
- Age-related CNS disorder and early death in transgenic FVB/N mice overexpressing Alzheimer amyloid precursor proteinsNeuron, 1995
- An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondriaNeuron, 1995
- Hydrogen peroxide mediates amyloid β protein toxicityCell, 1994
- A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.Proceedings of the National Academy of Sciences, 1994