An Overview of APP Processing Enzymes and Products
By Vivian W. Chow, Mark P. Mattson, Philip C. Wong, M. Gleichmann. Neuromolecular medicine, 2010
645 citations recorded by the source corpus.
The generation of amyloid β-peptide (Aβ) by enzymatic cleavages of the β-amyloid precursor protein (APP) has been at the center of Alzheimer’s disease (AD) research. While the basic process of β- and γ-secretase-mediated generation of Aβ is text book knowledge, new aspects of Aβ and other cleavage products have emerged in recent years. Also our understanding of the enzymes involved in APP proteolysis has increased dramatically. All of these discoveries contribute to a more complete understanding of APP processing and the physiologic and pathologic roles of its secreted and intracellular protein products. Understanding APP processing is important for any therapeutic strategy aimed at reducing Aβ levels in AD. In this review, we provide a concise description of the current state of understanding the enzymes involved in APP processing, the cleavage products generated by different processing patterns, and the potential functions of those cleavage products.
Subfields: Computational Theory and Mathematics, Pharmacology, Physiology
View Paper: https://www.semanticscholar.org/paper/b9c1349a191a091387dfb9e22c708b7bb2883812
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Citations in the corpus
- The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy (2016, background): “Aβ is a 38 to 43 amino acid long peptide generated by the sequential proteolytic cleavage of amyloid precursor protein (APP) byβ- and γ-secretases (Chow et al., 2010).”
- Neuroinflammation and M2 microglia: the good, the bad, and the inflamed (2014, background): “Amyloid β is generated from a parent protein called the amyloid precursor protein (APP), which is cleaved in two steps by the enzymes β then γ secretase, leading to release of the Aβ fragment [119].”
- Oxidative stress and the amyloid beta peptide in Alzheimer’s disease (2017, background): “Both pathways also lead first to the formation of aminoterminal fragments (secreted APP (sAPP) α or β) and carboxyterminal fragments (CTF83 or CTF99) and then to the formation of the aminoterminal APP intracellular domain (AICD) [20].”