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

MPG-Autoren
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Cavalcanti-Adam,  Elisabetta Ada
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;

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Majer,  Günter
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Spatz,  Joachim P.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;

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Zitation

de Beer, A. G. F., Cavalcanti-Adam, E. A., Majer, G., Lopez-García, M., Kessler, H., & Spatz, J. P. (2010). Force-induced destabilization of focal adhesions at defined integrin spacings on nanostructured surfaces. Physical Review E, 81: 051914, pp. 1-7. doi:10.1103/PhysRevE.81.051914.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-75D5-6
Zusammenfassung
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.