Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism

Neuron. 1995 Mar;14(3):651-9. doi: 10.1016/0896-6273(95)90322-4.

Abstract

Cerebral deposition of beta-amyloid protein is a pathological feature central to Alzheimer's disease. Production of beta-amyloid by proteolytic processing of the beta-amyloid precursor protein (beta APP) is a critical initial step in beta-amyloidogenesis. We use an inhibitor of beta APP processing to block beta-amyloid peptide formation. Application of the inhibitor to cultured cells results in an accumulation of proteolytic intermediates of beta APP, enabling a precursor-product relationship between beta APP carboxy-terminal fragments and beta-amyloid peptides to be demonstrated directly. In the presence of inhibitor, these amyloidogenic carboxy-terminal fragments can be degraded to nonamyloidogenic products. The catabolism of beta APP carboxy-terminal intermediates and the formation of beta-amyloid peptides are likely to involve an early endosomal compartment as the subcellular site of processing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism
  • Amino Acid Sequence
  • Amyloid beta-Peptides / biosynthesis*
  • Amyloid beta-Protein Precursor / metabolism*
  • Animals
  • Brain / metabolism
  • CHO Cells
  • Cricetinae
  • Dipeptides / pharmacology*
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Protease Inhibitors / pharmacology*
  • Protein Processing, Post-Translational*
  • Recombinant Proteins / biosynthesis
  • Transfection

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Dipeptides
  • Peptide Fragments
  • Protease Inhibitors
  • Recombinant Proteins
  • calpain inhibitor III