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- W951808650 abstract "Alzheimer's disease (AD) is the predominant cause of dementia in the elderly. This progressive neurodegenerative disorder is characterized pathologically by the presence of intracellular neurofibrillary tangles and extracellular neuritic plaques. The proteasome pathway is utilized to degrade excess presenilin 2 (PS2) holoproteins in the endoplasmic reticulum and this may be used to regulate the amount of presenilin that is cleaved by the endoproteolytic processing pathway. It is suggested that since the presenilins exist in vivo mainly as cleavage fragments, it is possible that the accumulation of excessive amounts of full-length presenilin cause potentially harmful effects to cells. Plasma and fibroblasts from patients and at-risk carriers carrying presenilin mutations have been shown to contain elevated levels of Aβ42, the longer and more amyloidogenic form of Aβ. It is suggested that the presenilins can undergo alternative endoproteolysis at a site distal to the normal regulated cleavage site. It is observed that caspase-mediated cleavage of the presenilins also underlies sporadic forms of AD which exponentially increases in prevalence with advanced age." @default.
- W951808650 created "2016-06-24" @default.
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- W951808650 date "1998-01-01" @default.
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- W951808650 title "The Role of the Presenilins in Alzheimer's Disease" @default.
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- W951808650 doi "https://doi.org/10.1016/b978-012734610-6/50010-5" @default.
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