Ultrastructural studies on the interaction of β-amyloid peptide and mouse neuroblastoma cells NB41A3

NB41A3 cells were used to investigate the effects of binding of a synthetic β-amyloid peptide, β1–40, to cellular membranes. Using a relatively low concentration of β1–40 we observed small changes in cytoplasmic morphology and nuclear damage. We also noted increases in vacuoles, the presence of particles within the nucleus and in the expanded perinuclear cisternal space after a three-day treatment with β1–40. Using immunocyto-chemistry we directly show β1–40 bound to and inside the NB41A3 cell. This result provides further evidence suggesting AβP-induced cell death in vitro is via an apoptotic mechanism.