Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor

Science. 1992 Feb 7;255(5045):726-8. doi: 10.1126/science.1738846.

Abstract

The 39- to 43-amino acid amyloid beta protein (beta AP), which is deposited as amyloid in Alzheimer's disease, is encoded as an internal peptide that begins 99 residues from the carboxyl terminus of a 695- to 770-amino acid glycoprotein referred to as the amyloid beta protein precursor (beta APP). To clarify the processing that produces amyloid, carboxyl-terminal derivatives of the beta APP were analyzed. This analysis showed that the beta APP is normally processed into a complex set of 8- to 12-kilodalton carboxyl-terminal derivatives. The two largest derivatives in human brain have the entire beta AP at or near their amino terminus and are likely to be intermediates in the pathway leading to amyloid deposition.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amyloid / biosynthesis*
  • Amyloid beta-Protein Precursor / chemistry
  • Amyloid beta-Protein Precursor / genetics
  • Amyloid beta-Protein Precursor / metabolism*
  • Cell Line
  • Cell Membrane / chemistry
  • Cerebral Cortex / chemistry
  • Glycosylation
  • Humans
  • Immunoblotting
  • Immunosorbent Techniques
  • Molecular Weight
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism*
  • Transfection

Substances

  • Amyloid
  • Amyloid beta-Protein Precursor
  • Peptide Fragments