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Related Experiment Videos

The beta A4 amyloid precursor protein binding to copper

L Hesse1, D Beher, C L Masters

  • 1Center for Molecular Biology Heidelberg, University Heidelberg, Germany.

FEBS Letters
|July 25, 1994
PubMed
Summary

Amyloid precursor protein (APP) binds copper ions, inhibiting its self-binding. This discovery suggests APP and related proteins may play roles in cellular electron transfer and radical reactions.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • The extracellular domain of amyloid precursor protein (APP) is known to bind zinc(II) and extracellular matrix molecules like collagen, laminin, and proteoglycans.
  • APP is implicated in various cellular processes, and its interactions with metal ions are of significant interest.

Purpose of the Study:

  • To investigate the potential binding of copper ions to APP.
  • To characterize the specific copper binding site within APP.
  • To determine the functional consequences of copper binding to APP.

Main Methods:

  • Site-directed mutagenesis to identify key residues in copper binding.
  • Spectroscopic analysis to confirm copper ion binding.
  • Biochemical assays to assess the effect of copper on APP homophilic binding.

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Main Results:

  • A copper type II binding site was identified within residues 135-155 of the cysteine-rich domain of APP695.
  • The identified copper binding site involves conserved histidines, also present in the related protein APLP2.
  • Copper(II) binding was demonstrated to inhibit homophilic binding of APP.

Conclusions:

  • APP possesses a functional copper binding site.
  • Copper binding to APP modulates its homophilic interaction.
  • The findings suggest a potential role for APP and APLP2 in electron transfer and radical reactions within the cell.