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The physiology of the β‐amyloid precursor protein intracellular domain AICD
Abstract
J. Neurochem. (2012) 120 (Suppl. 1), 109–124. The amyloid‐β precursor protein (βAPP) undergoes several cleavages by enzymatic activities called secretases. Numerous studies aimed at studying the biogenesis and catabolic fate of Aβ peptides, the proteinaceous component of the senile plaques that accumulate in Alzheimer’s disease‐affected brains. Relatively recently, another secretase‐mediated β‐APP‐derived catabolite called APP IntraCellular Domain (AICD) entered the game. Whether AICD corresponded to a biologically inert by‐pass product of βAPP processing or whether it could harbor its own function remained questionable. In this study, we review the mechanisms by which AICD is generated and how its production is regulated. Furthermore, we discuss the degradation mechanism underlying its rapid catabolic fate. Finally, we review putative AICD‐related functions and more particularly, the numerous studies indicating that AICD could translocate to the nucleus and control at a transcriptional level, the expression of a series of proteins involved in various functions including the control of cell death and Aβ degradation.
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“The latter can be translocated in the nucleus and engages in transcriptional activities, which are to some extent still controversial in the AD field (reviewed in Pardossi-Piquard and Checler, 2012) (Table 1).”
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 Pardossi-Piquard and Checler, 2012
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“Although AICD can theoretically be produced in both amyloidogenic and nonamyloidogenic pathways (Konietzko, 2012; Pardossi-Piquard and Checler, 2012), we and others have shown that AICD is preferentially derived from C99 in the amyloidogenic pathway (Goodger et al., 2009; Belyaev et al., 2010;…”
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Metadata
- Authors
- Pardossi‐Piquard, R., & Checler, F.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2011-11-28
- Volume
- 120
- Issue
- s1
- Pages
- 109-124
- ISSN
- 0022-3042
- 1471-4159
- Cited by
- 159
- References
- 14
- Language
- en
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