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An antibody against the Alzheimer's disease amyloid precursor protein recognizes distinct conformational isoforms

P Piccardo1, A Dagenais, A C Cuello

  • 1Department of Pharmacology and Therapeutics, McGill University, Montreal, Quebec, Canada.

Histochemistry
|May 1, 1993
PubMed

Insights

A new antibody, MAbE1, identifies specific Alzheimer's disease amyloid precursor protein (APP) isoforms. These distinct APP forms are primarily located within intracellular compartments of neuronal and glial cells.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Immunology

Background:

  • Alzheimer's disease is linked to the amyloid precursor protein (APP).
  • APP exists in multiple isoforms with extensive post-translational modifications.
  • Understanding APP isoform localization is crucial for Alzheimer's research.

Purpose of the Study:

  • To develop and characterize a novel monoclonal antibody (MAbE1) targeting specific APP isoforms.
  • To compare the reactivity of MAbE1 with a standard APP antibody (MAb22C11).
  • To investigate the cellular localization of APP isoforms recognized by MAbE1.

Main Methods:

  • Generation of MAbE1 against a synthetic APP peptide.
  • Immunoblot analysis of cell lysates and conditioned media.
  • Immunofluorescence microscopy for cellular localization studies.
  • Comparison with MAb22C11.

Main Results:

  • MAbE1 recognized a subclass of APP isoforms, distinct from MAb22C11.
  • Specific protein bands of 71 kDa and 120 kDa were detected in cell lysates.
  • No immunoreactivity was found in cell conditioned media.
  • MAbE1 showed predominantly perinuclear staining in neuronal and glial cells.

Conclusions:

  • MAbE1 identifies distinct conformational APP isoforms.
  • These specific APP isoforms are primarily located in intracellular compartments.
  • The findings provide insights into APP processing and localization in neuronal and glial cells.

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