Expression of BRI-amyloid beta peptide fusion proteins: a novel method for specific high-level expression of amyloid beta peptides

Biochim Biophys Acta. 2001 Jul 27;1537(1):58-62. doi: 10.1016/s0925-4439(01)00054-0.


In order to develop transgenic animal models that selectively overexpress various Abeta peptides, we have developed a novel expression system that selectively expresses Abeta40 or Abeta42 in the secretory pathway. This system utilizes fusion constructs in which the sequence encoding the 23-amino-acid ABri peptide at the carboxyl terminus of the 266-amino-acid type 2 transmembrane protein BRI is replaced with a sequence encoding either Abeta40 or Abeta42. Constitutive processing of the resultant BRI-Abeta fusion proteins in transfected cells results in high-level expression and secretion of the encoded Abeta peptide. Significantly, expression of Abeta42 from the BRI-Abeta42 construct resulted in no increase in secreted Abeta40, suggesting that the majority of Abeta42 is not trimmed by carboxypeptidase to Abeta40 in the secretory pathway.

Publication types

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

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amyloid / genetics*
  • Amyloid beta-Peptides / genetics*
  • Animals
  • Cell Line
  • Cells, Cultured
  • Humans
  • Membrane Glycoproteins
  • Membrane Proteins
  • Mice
  • Models, Molecular
  • Peptide Fragments / biosynthesis
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics*
  • Transfection


  • Adaptor Proteins, Signal Transducing
  • Amyloid
  • Amyloid beta-Peptides
  • ITM2B protein, human
  • Itm2b protein, mouse
  • Membrane Glycoproteins
  • Membrane Proteins
  • Peptide Fragments
  • Recombinant Fusion Proteins