Altered proteolysis of the amyloid precursor protein (APP) may play an important role in Alzheimer disease (AD). To better understand the role of mutant APP in the pathogenesis of the disease, we stably overexpressed the mutant APP717F approximately twofold vs. the endogenous wild-type gene in sever
Endothelial cell dysfunction in response to intracellular overexpression of amyloid precursor protein
โ Scribed by Nadia Jahroudi; Jana Kitney; Joel S. Greenberger; Robert Bowser
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 928 KB
- Volume
- 54
- Category
- Article
- ISSN
- 0360-4012
No coin nor oath required. For personal study only.
โฆ Synopsis
Previous reports have shown that exposure of vascular endothelial and smooth muscle cells to exogenous amyloid beta (Aโค) peptide results in cell damage and toxicity via oxidative injury. In this study we demonstrate that overexpression of the amyloid precursor protein (APP) is toxic to bovine aortic endothelial cells but not to bovine aortic smooth muscle cells. Intracellular coexpression of the free radical scavenger proteins metallothionein or MnSOD abolished the toxic effect of APP overexpression in endothelial cells. Our results demonstrate that endothelial cells are specifically susceptible to intracellular overexpression of APP and free radical generation is the likely mechanism of cell damage due to APP overexpression.
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