Characterization of amyloid fibril beta-peptide in familial Alzheimer's disease with APP717 mutations.


Journal Article

Amyloid fibrils were isolated from the brain tissue of two individuals who died with familial Alzheimer's disease, one with the phenylalanine 717 mutation in amyloid precursor protein (APP) and one with the isoleucine 717 APP mutation. After solubilization in guanidine hydrochloride and fractionation by sieve chromatography, low molecular weight fractions were treated with cyanogen bromide to generate the beta-peptide fragment starting after the methionine at position 35. Amino acid sequence analysis of all resultant peptides identified the peptide Val-Gly-Gly-Val-Val-Ile-Ala which represents residues 36-42 of the beta-amyloid peptide. No sequence beyond position 42 was found. These findings show that the amino acid substitution at position 717 is not incorporated into the amyloid deposits and suggests that the mutation may have metabolic affects which determine pathogenesis.

Full Text

Cited Authors

  • Liepnieks, JJ; Ghetti, B; Farlow, M; Roses, AD; Benson, MD

Published Date

  • December 1993

Published In

Volume / Issue

  • 197 / 2

Start / End Page

  • 386 - 392

PubMed ID

  • 8267572

Pubmed Central ID

  • 8267572

Electronic International Standard Serial Number (EISSN)

  • 1090-2104

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1993.2491


  • eng