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Presenilin1 was initially identified a marker of susceptibility to early-onset Alzheimer's disease. In addition to PEN2, nicastrin and APH-1, Presenilin1 forms the -gamma-secretase protein complex, a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key step in signaling from several cell-surface receptors and is thought to be required for the generation of the neurotoxic amyloid peptides that are central to the pathogenesis of Alzheimer's disease. Like the tumor necrosis factor-alpha-converting enzyme (TACE) and the beta-site cleavage enzyme (BACE) protease families, -gamma-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the alpha and -gamma cleavage site) or the toxic Abeta amyloid peptide (from the beta and -gamma cleavage site). It is thought that accumulation of the Abeta peptide is the precursor to Alzheimer's disease. Multiple isoforms of presenilin1 are known to exist.
AD3; Ad3h; Alzheimer Disease 3; FAD; Minilin; presenilin 1; presenilin 1 (Alzheimer disease 3); presenilin1; presenilin-1; Presenilin-1 CTF subunit; Presenilin-1 CTF12; Presenilin-1 NTF subunit; Protein S182; PS1; PS-1; PS1-CTF12; PSEN1; Psnl1; S182; S182 protein; Senilin 1
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