Binding of cystatin C to Alzheimer’s amyloid β inhibits in vitro amyloid fibril formation

摘要: Abstract The colocalization of cystatin C, an inhibitor cysteine proteases, with amyloid β (Aβ) in parenchymal and vascular deposits brains Alzheimer’s disease (AD) patients may reflect C involvement amyloidogenesis. We therefore sought to determine the association Aβ. Immunofluorescence analysis transfected cultured cells demonstrated precursor protein (βAPP) intracellularly on cell surface. Western blot immunoprecipitated lysate or medium proteins revealed binding full-length βAPP secreted (sβAPP). Deletion mutants localized site within Aβ region. Cystatin resulted increased sβAPP but did not affect levels Analysis a specific, saturable high affinity between both 1–42 1–40 . Notably, results concentration-dependent inhibition fibril formation.