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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-75D5-6 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002E-5F96-D
Genre: Journal Article

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PhysRevE_81_2010_051914.pdf (Any fulltext), 243KB
 
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http://journals.aps.org/pre/pdf/10.1103/PhysRevE.81.051914 (Any fulltext)
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https://doi.org/10.1103/PhysRevE.81.051914 (Any fulltext)
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 Creators:
de Beer, Alex G. F., Author
Cavalcanti-Adam, Elisabetta Ada1, 2, Author           
Majer, Günter1, Author           
Lopez-García, M., Author
Kessler, H., Author
Spatz, Joachim P.1, 2, Author           
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2010-04-122010-02-042010-05-12
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 475973
DOI: 10.1103/PhysRevE.81.051914
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Title: Physical Review E
  Other : Phys. Rev. E
Source Genre: Journal
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Publ. Info: Melville, NY : American Physical Society
Pages: - Volume / Issue: 81 Sequence Number: 051914 Start / End Page: 1 - 7 Identifier: ISSN: 1539-3755
CoNE: https://pure.mpg.de/cone/journals/resource/954925225012