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Related Experiment Videos

Apolipoprotein E and amyloidogenesis

B Frangione1, E M Castaño, T Wisniewski

  • 1Department of Pathology, New York University Medical Center, NY 10016, USA.

Ciba Foundation Symposium
|January 1, 1996
PubMed
Summary
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Alzheimer's amyloid beta-protein (A beta) and soluble amyloid beta-protein (sA beta) are isomers that differ in structure and resistance to degradation. This study investigates their role in Alzheimer's disease amyloidosis, proposing it may be a reactive process.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Genetics

Background:

  • Alzheimer's disease (AD) involves amyloid beta-protein (A beta), a pathogenic form of soluble amyloid beta-protein (sA beta).
  • Both A beta and sA beta are conformational isomers derived from the beta-amyloid precursor protein (APP) gene.
  • A beta is resistant to degradation and forms amyloid fibrils, unlike sA beta.

Purpose of the Study:

  • To investigate the structural and functional differences between A beta and sA beta in Alzheimer's disease.
  • To explore the role of apolipoprotein E (apoE) in A beta aggregation and amyloid formation.
  • To hypothesize whether amyloidosis in AD is a reactive or causative process.

Main Methods:

  • Comparative analysis of A beta and sA beta structures and properties.

Related Experiment Videos

  • Investigation of genetic links to early-onset AD (APP, presenilin genes).
  • Examination of apoE epsilon 4 allele as a risk factor and its interaction with A beta in vitro.

    • Main Results:

    • A beta exhibits high beta-pleated sheet content and forms aggregates, while sA beta is more random-coil/alpha-helical and degradable.
    • Mutations in APP, presenilin 1, and presenilin 2 genes are linked to early-onset AD.
    • ApoE C-terminal fragments complex with A beta in plaques, and apoE isoforms modulate amyloid formation.

    Conclusions:

    • Neuritic plaques may contain both A beta and apoE amyloid fibrils.
    • Alzheimer's disease pathology involves multiple interacting proteins capable of amyloid formation.
    • Amyloidosis in AD might be a reactive response rather than the primary cause.