Comparable dimerization found in wildtype and familial Alzheimer’s disease amyloid precursor protein mutants

摘要: Alzheimer's disease (AD) is a progressive and fatal neurodegenerative disorder marked by memory impairment cognitive deficits. A major component of AD pathology the accumulation amyloid plaques in brain, which are comprised beta (Aβ) peptides derived from amyloidogenic processing precursor protein (AβPP) β- γ-secretases. In subset patients, inheritance mutations AβPP gene responsible for altering Aβ production, leading to early onset disease. Interestingly, many these familial lie within transmembrane domain near GxxxG GxxxA dimerization motifs that important interactions. As has been linked changes it interest know whether affect full-length APP dimerization. Using bimolecular fluorescence complementation (BiFC), blue native gel electrophoresis, live cell chemical cross-linking, we found (FAD) do not transfected HEK293 COS7 cells. It follows necessary altered FAD mutations, levels more likely result alternative proteolytic processing.