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Cadherin interaction probed by atomic force microscopy.

W Baumgartner1, P Hinterdorfer, W Ness

  • 1Institute of Anatomy, University of Würzburg, Koellikerstrasse 6, D-97070 Würzburg, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|April 12, 2000
PubMed
Summary
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Vascular endothelial cadherin (VE-cadherin) forms weak adhesive bonds that strengthen through clustering. Calcium ions regulate VE-cadherin binding, crucial for cell adhesion dynamics.

Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Adhesion

Background:

  • Vascular endothelial cadherin (VE-cadherin) is crucial for endothelial cell-cell adhesion.
  • Understanding VE-cadherin's molecular interactions is key to deciphering its role in vascular integrity.

Purpose of the Study:

  • To characterize the structure, binding strength, and kinetics of VE-cadherin using single-molecule atomic force microscopy.
  • To elucidate the role of calcium ions in VE-cadherin interactions.

Main Methods:

  • Single molecule atomic force microscopy (smAFM) was employed.
  • Characterization of VE-cadherin dimers and their trans-interactions.
  • Analysis of binding affinity, dissociation rates, and unbinding forces.

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Main Results:

  • VE-cadherin dimers are ~20 nm rod-shaped molecules that collapse without Ca(2+).
  • Trans-interaction exhibits low affinity (10(-3)-10(-5) M) and low unbinding force (35-55 pN).
  • Higher-order complexes increase binding strength; Ca(2+) binding is cooperative (Hill coefficient of 5.04).

Conclusions:

  • Weak VE-cadherin unit binding requires clustering and cytoskeletal support for amplified adhesion.
  • Calcium concentration dynamically regulates VE-cadherin interactions, impacting intercellular adhesion.
  • VE-cadherin's Ca(2+)-dependent binding is vital for remodeling cell-cell communication.