Production of amyloid-beta-peptide by cultured cells: no evidence for internal initiation of translation at Met596

Neurobiol Aging. 1993 Nov-Dec;14(6):571-3. doi: 10.1016/0197-4580(93)90041-9.

Abstract

It has been suggested that the A beta fragment of the amyloid precursor protein in Alzheimer's disease arises from internal translation initiation at Met596 (1). Here we use the recently described in vitro model of A beta production and secretion (2) to examine this hypothesis. We show that A beta is no longer detectable when the beta APP reading frame is destroyed by introduction of frame shift mutations that leave the A beta coding region intact. This result strongly suggests that internal initiation at Met596 does not contribute significantly to the amount of A beta observed.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amyloid beta-Peptides / biosynthesis*
  • Amyloid beta-Protein Precursor / metabolism
  • Base Sequence
  • Cells, Cultured
  • DNA, Complementary / metabolism
  • Frameshift Mutation
  • Humans
  • Kidney / metabolism
  • Methionine / metabolism*
  • Molecular Sequence Data
  • Peptide Chain Initiation, Translational
  • Reading Frames

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • DNA, Complementary
  • Methionine