Alzheimer's disease is associated with a dense accumulation of proteins in amyloid plaques in the brain containing fragments of amyloid-beta as the main component. If the development of amyloid plaques is responsible for neurodegeneration in Alzheimer's disease, a reduction in the formation of beta-amyloid and the progress of development may prevent the symptoms of the disease. Fragments of beta amyloid proteolytic processing of the amyloid precursor protein (APP) derivatives in neurons and the subsequent release of fragments in the extracellular space. APP is cleaved in the ER at residue 17 encoded by the activity of the alpha-secretase protease ADAM-10 and TACE. Beta-secretase activity, as recently identified BACE cleaves the N-terminus of beta-amyloid fragment. Gamma secretase cuts in the APP transmembrane domain at amino acids 40 and 42, the release of residues amyloid beta fragments 1-40 / 42 and short articles as ASP3 (residues 17-40 / 42), alpha secretase cleavage requires. The gamma-secretase activity requires the transmembrane protein presenilin-1, which is divided into an N-terminal fragment and C-terminal which are both required for the gamma-secretase activity. Mutations in presenilin-1 are genetically associated with familial forms of Alzheimer's disease, even supporting the role of APP processing to develop the disease. Inhibition of beta or gamma secretase can provide a mechanism to treat this disease. Other mechanisms altering the degradation of beta-amyloid and use of vaccines against amyloid beta aggregates to contain to remove.
