Force-induced destabilization of focal adhesions at defined integrin spacings on nanostructured surfaces
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...
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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
12 May 2010
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| In: |
Physical review. E, Statistical, nonlinear, and soft matter physics
Year: 2010, Jahrgang: 81, Heft: 5, Pages: 1-7 |
| ISSN: | 1550-2376 |
| DOI: | 10.1103/PhysRevE.81.051914 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1103/PhysRevE.81.051914 Verlag, lizenzpflichtig, Volltext: https://link.aps.org/doi/10.1103/PhysRevE.81.051914 
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| Verfasserangaben: | Alex G.F. de Beer, E. Ada Cavalcanti-Adam, Günter Majer, M. Lopez-García, H. Kessler, and Joachim P. Spatz |
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| 245 | 1 | 0 | |a Force-induced destabilization of focal adhesions at defined integrin spacings on nanostructured surfaces |c Alex G.F. de Beer, E. Ada Cavalcanti-Adam, Günter Majer, M. Lopez-García, H. Kessler, and Joachim P. Spatz |
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| 520 | |a 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. | ||
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