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Alternative, Non-secretase Processing of Alzheimer's β-Amyloid Precursor Protein during Apoptosis by Caspase-6 and -8
Abstract
Alzheimer's disease (AD) is a progressive neurodegenerative disorder. Although the pathogenesis of AD is unknown, it is widely accepted that AD is caused by extracellular accumulation of a neurotoxic peptide, known as Abeta. Mutations in the beta-amyloid precursor protein (APP), from which Abeta arises by proteolysis, are associated with some forms of familial AD (FAD) and result in increased Abeta production. Two other FAD genes, presenilin-1 and -2, have also been shown to regulate Abeta production; however, studies examining the biological role of these FAD genes suggest an alternative theory for the pathogenesis of AD. In fact, all three genes have been shown to regulate programmed cell death, hinting at the possibility that dysregulation of apoptosis plays a primary role in causing neuronal loss in AD. In an attempt to reconcile these two hypotheses, we investigated APP processing during apoptosis and found that APP is processed by the cell death proteases caspase-6 and -8. APP is cleaved by caspases in the intracellular portion of the protein, in a site distinct from those processed by secretases. Moreover, it represents a general effect of apoptosis, because it occurs during cell death induced by several stimuli both in T cells and in neuronal cells.
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Caspase-3, -6 and -8 cleave APP mainly between amino acids V664-D665 (APP695 numbering) within the intracytoplasmic domain.
“Several studies have demonstrated in a variety of culture cell systems the ability of caspase-3, -6 and -8 to cleave APP, mainly between amino acids V664-D665 (APP695 numbering) within the intracytoplasmic domain (Gervais et al., 1999; LeBlanc et al., 1999; Pellegrini et al., 1999; Weidemann et al., 1999).”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Pellegrini et al., 1999
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“Of note, unprovoked seizures occur in AD patients at rates 8‐ to 10‐fold higher than in the general population (Hauser, Morris, Heston & Anderson, 1986; Scarmeas et al., 2009) and at even higher rates in FAD cases (Cabrejo et al., 2006; Mendez & Lim, 2003; Palop & Mucke, 2016).”
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Metadata
- Authors
- Pellegrini, L., Passer, B. J., Tabaton, M., Ganjei, J. K., & D'Adamio, L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-07
- Volume
- 274
- Issue
- 30
- Pages
- 21011-21016
- ISSN
- 0021-9258
- Cited by
- 139
- References
- 7
- Language
- en
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