International Journal of Physiology, Pathophysiology and Pharmacology | |
Caspase cleavage of the amyloid precursor protein is prevented after overexpression of bcl-2 in a triple transgenic mouse model of Alzheimer's disease | |
Veronica Galvan1  Debra K Kumasaka1  Elizabeth Head1  Troy T Rohn1  | |
关键词: Amyloid precursor protein; beta-amyloid; caspase; mouse model; neurofibrillary tangles; plaques; tau; bcl-2; apoptosis; | |
DOI : | |
学科分类:生理学与病理学 | |
来源: e-Century Publishing Corporation | |
【 摘 要 】
A recent study demonstrated the lack of beta-amyloid (Aβ) plaque formation and accumulation of the amyloid precursor protein (APP) in a triple transgenic mouse model of Alzheimer's disease (3xTg-AD) following overexpression of the anti-apoptotic protein, Bcl-2 (Rohn et al., J. Neurosci. 28: 3051–9, 2008). The supposition from that study was the accumulation of APP resulted from a decrease in caspase-mediated processing of APP. To determine a direct role for the caspase-cleavage of APP in 3xTg-AD mice, we designed a site-directed caspasecleavage antibody to APP and demonstrated it is a specific marker for caspase-cleaved APP. Application of this antibody revealed neuronal staining in the hippocampus and subiculum of 3xTg-AD mice. These results were confirmed utilizing a similar site-directed antibody to caspase-cleaved APP (APPneo). The caspase cleavage of APP as well as the formation of extracellular Aβ plaques was prevented in 3xTg-AD animals overexpressing Bcl-2. These results provide further support that caspases play a proximal role in promoting the pathology associated with AD.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912140862947ZK.pdf | 354KB | download |