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Amyloid precursor protein (APP) is a type I transmembrane glycoprotein primarily recognized for its central role in the pathogenesis of Alzheimer's disease through the generation of neurotoxic amyloid-beta (Aβ) peptides [UniProt: P05067]. Beyond the central nervous system, APP is expressed in vascular cells, including endothelial cells, smooth muscle cells, and platelets, where it functions in cell adhesion and intracellular signaling [PubMed: 28633904]. In the context of atherosclerosis, APP and its cleavage products contribute to vascular inflammation, oxidative stress, and the formation of atherosclerotic plaques [PubMed: 30213780]. Aβ peptides can impair nitric oxide-mediated vasodilation and promote a pro-thrombotic state by enhancing platelet activation [PubMed: 25135909]. While therapeutic interventions like BACE1 inhibitors and anti-Aβ antibodies were developed for neurodegeneration, their impact on vascular signaling pathways suggests potential relevance in managing cardiovascular complications associated with amyloid pathology.
Inhibition of proteolytic cleavage by beta-secretase (BACE1) or gamma-secretase to reduce amyloid-beta production; monoclonal antibody-mediated clearance of amyloid-beta aggregates from tissues.
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