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Journal of the mechanics and physics of solids, 2016-10, Vol.95 (C), p.557-574
2016
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Autor(en) / Beteiligte
Titel
Why do receptor–ligand bonds in cell adhesion cluster into discrete focal-adhesion sites?
Ist Teil von
  • Journal of the mechanics and physics of solids, 2016-10, Vol.95 (C), p.557-574
Ort / Verlag
United States: Elsevier Ltd
Erscheinungsjahr
2016
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
  • Cell adhesion often exhibits the clustering of the receptor–ligand bonds into discrete focal-adhesion sites near the contact edge, thus resembling a rosette shape or a contracting membrane anchored by a small number of peripheral forces. The ligands on the extracellular matrix are immobile, and the receptors in the cell plasma membrane consist of two types: high-affinity integrins (that bond to the substrate ligands and are immobile) and low-affinity integrins (that are mobile and not bonded to the ligands). Thus the adhesion energy density is proportional to the high-affinity integrin density. This paper provides a mechanistic explanation for the clustering/assembling of the receptor–ligand bonds from two main points: (1) the cellular contractile force leads to the density evolution of these two types of integrins, and results into a large high-affinity integrin density near the contact edge and (2) the front of a propagating crack into a decreasing toughness field will be unstable and wavy. From this fracture mechanics perspective, the chemomechanical equilibrium is reached when a small number of patches with large receptor–ligand bond density are anticipated to form at the cell periphery, as opposed to a uniform distribution of bonds on the entire interface. Cohesive fracture simulations show that the de-adhesion force can be significantly enhanced by this nonuniform bond density field, but the de-adhesion force anisotropy due to the substrate elastic anisotropy is significantly reduced.
Sprache
Englisch
Identifikatoren
ISSN: 0022-5096
DOI: 10.1016/j.jmps.2016.05.012
Titel-ID: cdi_osti_scitechconnect_1357997

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