Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

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

MPG-Autoren
/persons/resource/persons75354

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;

/persons/resource/persons75813

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

/persons/resource/persons76135

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;

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
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: https://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.