Force-induced destabilization of focal adhesions at defined integrin spacings on nanostructured surfaces

Phys Rev E Stat Nonlin Soft Matter Phys. 2010 May;81(5 Pt 1):051914. doi: 10.1103/PhysRevE.81.051914. Epub 2010 May 12.

Abstract

Focal adhesions are the anchoring points of cells to surfaces and are responsible for a large number of surface sensing processes. Nanopatterning studies have shown physiological changes in fibroblasts as a result of decreasing density of external binding ligands. The most striking of these changes is a decreased ability to form mature focal adhesions when lateral ligand distances exceed 76 nm. These changes are usually examined in the context of protein signaling and protein interactions. We show a physical explanation based on the balance between the forces acting on individual ligand connections and the reaction kinetics of those ligands. We propose three stability regimes for focal adhesions as a function of ligand spacing and applied stress: a stable regime, an unstable regime in which a large fraction of unbound protein causes adhesion disintegration, and a regime in which the applied force is too high to form an adhesion structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Cytosol / metabolism
  • Fibroblasts / metabolism
  • Fibronectins / chemistry
  • Focal Adhesions / chemistry*
  • Integrins / chemistry*
  • Kinetics
  • Ligands
  • Micelles
  • Nanostructures / chemistry*
  • Nanotechnology / methods
  • Protein Interaction Mapping
  • Rats
  • Signal Transduction

Substances

  • Fibronectins
  • Integrins
  • Ligands
  • Micelles