Human Brain βA4 Amyloid Protein Precursor of Alzheimer's Disease: Purification and Partial Characterization

Robert D. Moir, Ralph N. Martins, Ashley I. Bush, David H. Small, Elizabeth A. Milward, Baden A. Rumble, Gerd Multhaup, Konrad Beyreuther, Colin L. Masters*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

Abstract: The major component of the amyloid deposition that characterizes Alzheimer's disease is the 4‐kDa βA4 protein, which is derived from a much larger amyloid protein precursor (APP). A procedure for the complete purification of APP from human brain is described. The same amino terminal sequence of APP was found in two patients with Alzheimer's disease and one control subject. Two major forms of APP were identified in human brain with apparent molecular masses of 100–110 kDa and 120–130 kDa. Soluble and membrane fractions of brain contained nearly equal amounts of APP in both humans and rats. Immunoprecipitation with carboxyl terminus‐directed antibodies indicates that the soluble forms of APP are truncated. Carboxyl terminus truncation of membrane‐associated forms of human brain APP was also found to occur during postmortem autolysis. The availability of purified human brain APP will facilitate the investigation of its normal function and the events that lead to its abnormal cleavage in patients with Alzheimer's disease.

Original languageEnglish
Pages (from-to)1490-1498
Number of pages9
JournalJournal of Neurochemistry
Volume59
Issue number4
DOIs
Publication statusPublished - 1992
Externally publishedYes

Keywords

  • Alzheimer's disease
  • Amyloid protein precursor
  • Membrane protein
  • Postmortem degradation
  • Protein sequence
  • Proteolysis
  • βA4 amyloid

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