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Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing

S S Sisodia1, E H Koo, K Beyreuther

  • 1Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2181.

Science (New York, N.Y.)
|April 27, 1990
PubMed

Insights

Alzheimer's disease involves beta-amyloid plaques. Altered processing of amyloid precursor protein (APP) may lead to the release of intact beta-amyloid, forming these toxic plaques.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Alzheimer's disease is characterized by senile plaques, primarily composed of beta-amyloid (beta/A4) protein.
  • Amyloid precursor protein (APP) is the source of beta-amyloid and is a membrane glycoprotein.
  • APP is processed via cleavage, a membrane-associated event.

Purpose of the Study:

  • To investigate the mechanism of beta-amyloid formation in Alzheimer's disease.
  • To understand the role of APP processing in the generation of amyloidogenic fragments.

Main Methods:

  • Analysis of APP cleavage sites.
  • Biochemical characterization of APP processing pathways.

Main Results:

  • APP cleavage occurs within the beta-amyloid region.
  • Normal APP catabolism does not generate intact amyloidogenic beta-amyloid fragments.

Conclusions:

  • Altered APP processing is a potential early event in Alzheimer's disease pathogenesis.
  • This altered processing may lead to the release and deposition of intact beta-amyloid, contributing to plaque formation.

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