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.
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Protein Aliases: Alzheimer Disease 3; Minilin; Presenilin-1; Presenilin-1 CTF subunit; Presenilin-1 CTF12; Presenilin-1 NTF subunit; presenilin1; Protein S182; PS-1; PS1-CTF12; S182 protein; Senilin 1
Gene Aliases: AD3; Ad3h; FAD; PS-1; PS1; PSEN1; PSNL1; S182