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APP Processing and Plaque Formation

Canonical processing of APP is catalyzed by α-secretase, resulting in the generation of two fragments: a large extracellular fragment secreted APP (sAPP) α (sAPPα) that is released to extracellular medium, as well as an83 amino acid C-terminal fragment α-carboxyterminal fragments (CTF) that remains in the membrane.

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APP Processing and Plaque Formation

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  1. APP Processing and Plaque Formation Alzheimer's disease (AD), the most prevalent neurodegenerative disorder in aged population, is characterized by progressive cognitive impairment and other neurodegeneration disorder. Neuropathological hallmarks of AD include neuronal loss in the neurofibrillary tangles (NFTs) and presence of extracellular neuritic plaques in the brain. The NFTs is formed of hyperphosphorylated twisted filaments of the microtubule-associated protein Tau. While, extracellular neuritic plaques are deposits of differently sized small peptides called beta-amyloid (Aβ), which are derived via sequential proteolytic cleavages of the beta-amyloid precursor protein (APP). APP belongs to a larger evolutionarily conserved APP superfamily protein family that includes the APP itself and amyloid precursor-like protein 1 (APLP1) and 2 (APLP2) in mammals. The APP superfamily shares several conserved domains, however, only APP generates an amyloidogenic fragment owing to the unique Aβ domain in sequence divergence. Though expressed in many tissues, APP is concentrated in the synapses of neurons in the CNS. All of them are single-pass transmembrane proteins with large extracellular N terminal and a shorter cytoplasmic C terminal. Find more: https://www.creative-diagnostics.com/app-processing-and-plaque-formation.htm

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