Abstract
The β-amyloid precursor protein (βAPP) is a transmembrane protein that can exist in several isoforms resulting from the alternative splicing of a single gene (Mullan and Crawford, 1993). This protein undergoes complex processing events, the alterations of which have been postulated to be likely linked to the Alzheimer’s disease (AD) neuropathology. In physiological conditions, βAPP is cleaved near the membrane by a proteolytic activity, namely α-secretase, that releases an N-terminal fragment (called APPα) that was demonstrated to participate in coagulation and wound repair (Oltersdorf et al., 1989; Smith et al., 1990) as well as in neurotrophic and cytoprotective processes (Qiu et al., 1995; Saitoh et al., 1989; Mattson et al., 1993). In normal conditions, a 40 amino-acid-long fragment called Aβ peptide can also be generated upon βAPP proteolysis by the action of two enzymes called β-and γ-secretases that liberate the N-and C-terminal moieties of Aβ peptide, respectively (see Haass and Selkoe, 1993; Checler, 1995).
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Chevallier, N. et al. (1997). Novel Cathepsin D Inhibitors Prevent the β-Secretase-Derived Intracellular Formation of a 12 kDa Potentially Amyloidogenic Product in Human Cells. In: Becker, R.E., Giacobini, E., Barton, J.M., Brown, M. (eds) Alzheimer Disease. Advances in Alzheimer Disease Therapy. Birkhäuser Boston. https://doi.org/10.1007/978-1-4612-4116-4_11
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DOI: https://doi.org/10.1007/978-1-4612-4116-4_11
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