Expression of potentially amyloidogenic derivatives of the Alzheimer amyloid precursor protein in cultured 293 cells

Neurosci Lett. 1994 Oct 24;180(2):151-4. doi: 10.1016/0304-3940(94)90509-6.

Abstract

The expression of the carboxyl-terminal 100 (C-100) residues of the amyloid precursor protein (APP) may provide a model for studying the processing of APP to the 42-43 residue beta-amyloid peptide (beta A4) implicated in Alzheimer's disease. Expression of human C-100 in mammalian cells reportedly causes 'toxicity' and amyloid-like fibrils. We have expressed the C-100 fragment in human embryonic kidney cells (293 cells) in a transient assay and compared it to the expression of transfected wild type and mutant (Swedish familial Alzheimer's disease) full length APP. Products were characterized by Western blot analysis using antibodies to the carboxyl-terminal region of APP.

Publication types

  • Comparative Study

MeSH terms

  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism
  • Amyloid / genetics
  • Amyloid / metabolism*
  • Amyloid beta-Protein Precursor / biosynthesis*
  • Amyloid beta-Protein Precursor / genetics
  • Cells, Cultured
  • Cytomegalovirus / genetics
  • Humans
  • Kidney
  • Molecular Weight
  • Peptide Fragments / biosynthesis*
  • Peptide Fragments / genetics
  • Prion Proteins
  • Prions
  • Promoter Regions, Genetic
  • Protein Precursors / genetics
  • Protein Precursors / metabolism*
  • Protein Sorting Signals / genetics
  • Protein Sorting Signals / metabolism
  • Recombinant Fusion Proteins / biosynthesis*
  • Transfection

Substances

  • Amyloid
  • Amyloid beta-Protein Precursor
  • PRNP protein, human
  • Peptide Fragments
  • Prion Proteins
  • Prions
  • Protein Precursors
  • Protein Sorting Signals
  • Recombinant Fusion Proteins
  • amyloid precursor protein, carboxy-terminal 100 residues