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Related Experiment Videos

Ca(2+)-dependent annexin self-association on membrane surfaces.

W J Zaks1, C E Creutz

  • 1Department of Pharmacology, University of Virginia, Charlottesville 22908.

Biochemistry
|October 8, 1991
PubMed
Summary

Annexin proteins like synexin self-associate on membranes in a calcium-dependent manner. This self-association is crucial for membrane aggregation at low calcium levels, but not high ones.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Membrane Biophysics

Background:

  • Annexins are a family of calcium-dependent phospholipid-binding proteins.
  • Annexin self-association and its role in membrane interactions are not fully understood.

Purpose of the Study:

  • To investigate the Ca(2+)-dependent self-association of specific annexins (VII, IV, VI) in solution and on membranes.
  • To determine the role of annexin self-association in Ca(2+)-induced membrane aggregation.

Main Methods:

  • 90-degree light scattering and resonance energy transfer (RET) using fluorescein and eosin labels.
  • Studies conducted in solution and with phospholipid vesicles and chromaffin granule membranes.
  • Investigated the effect of different phospholipid compositions and trifluoperazine.

Main Results:

  • Synexin (annexin VII), p32 (annexin IV), and p67 (annexin VI) exhibit Ca(2+)-dependent self-association.
  • Self-association occurs at lower Ca(2+) concentrations on chromaffin granule membranes compared to solution.
  • Annexin polymerization is linked to Ca(2+)-dependent membrane aggregation, particularly at low Ca(2+) levels.

Conclusions:

  • Annexin self-association is a Ca(2+)-dependent process that is enhanced by specific membrane compositions.
  • Annexin polymerization on membranes appears necessary for aggregation at low Ca(2+) but not high Ca(2+) concentrations.
  • Trifluoperazine inhibits both annexin self-association and membrane aggregation.

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