Amyloid precursor protein (APP) is a type I membrane protein with several human isoforms due to alternative splicing. APP-770, -751, and -733 contain a Kunitz protease inhibitor (KPI) domain (residue 291 - 342, Accession # NP_000475) and APP-695 does not. APP is a cell surface molecule with many functions. It can be processed proteolytically in two different pathways. In one pathway, β- and γ-secretase cleave at the β site between residue 670 and 671 and the γ site between residue 711 and 714 to produce β-amyloid peptide (Aβ40 and Aβ42), a major component in plaques found in brains of patients with Alzheimer's disease.The other pathway involves α-secretase that cleaves residues between 687 and 688. It is antiamyloidogenic due to its benign character and the prevention of the Aβ peptide formation. Soluble APP containing the KPI domain, also referred to as protease nexin II, is a potent inhibitor of serine proteases and may have additional functions. For example, it may regulate the contact face of blood coagulation and limit thrombosis specially in brain due to its localization and coagulation factor XI inhibiting activity.
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