Presenilin Proteins and Their Function During Embryonic Development and Alzheimer’s Disease

  • C. Haass
Conference paper
Part of the Ernst Schering Research Foundation Workshop book series (SCHERING FOUND, volume 29)


Aggregation and precipitation of peptides appear to play a major role in neurodegenerative diseases such as Alzheimer’s disease (AD) (Teplow 1998), Parkinson’s disease (Mezey et al. 1998), and Huntington’s disease (Georgalis et al. 1998). In AD, the aggregating Amyloid β-peptide (Aβ) accumulates in highly insoluble senile plaques, which are the defining pathological symptoms of the disease (Selkoe 1996). Aβ is derived by proteolytic processing from the β-Amyloid precursor protein βAPP; Selkoe 1996). Two secretases have been postulated, which either generate the N-terminus (β-secretale) or the C-terminus (γ-secretase) of Aβ (Haass and Selkoe 1993; Fig. 1). Aβ is produced under physiological conditions in cultured cells and is secreted into the media. In vivo, Aβ is detected in human plasma and cerebrospinal fluid (Haass and Selkoe 1993).


Aspartyl Protease Notch Intracellular Domain Presenilin Protein Presenilin Function Presenilin Complex 
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© Springer-Verlag Berlin Heidelberg 2000

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  • C. Haass

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