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Vol. 18, Issue 5, 1634-1644, May 2007

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Revealing Early Steps of ₂₁ Integrin-mediated Adhesion to Collagen Type I by Using Single-Cell Force Spectroscopy

Anna Taubenberger^*, David A. Cisneros^*, Jens Friedrichs^*, Pierre-Henri Puech^*,, Daniel J. Muller^*, and Clemens M. Franz^*

*BioTechnological Center, University of Technology Dresden, 01307 Dresden, Germany; and Institut National de la Santé et de la Recherche Médicale Unité Mixte de Recherche 600/Centre National de la Recherche Scientifique Unité Mixte de Recherche 6212, Adhésion Cellulaire et Inflammation, 13288 Marseille, France

Submitted September 5, 2006; Revised January 19, 2007; Accepted February 9, 2007
Monitoring Editor: Jean Schwarzbauer

We have characterized early steps of ₂₁ integrin-mediated cell adhesion to a collagen type I matrix by using single-cell force spectroscopy. In agreement with the role of ₂₁ as a collagen type I receptor, ₂₁-expressing Chinese hamster ovary (CHO)-A2 cells spread rapidly on the matrix, whereas ₂₁-negative CHO wild-type cells adhered poorly. Probing CHO-A2 cell detachment forces over a contact time range of 600 s revealed a nonlinear adhesion response. During the first 60 s, cell adhesion increased slowly, and forces associated with the smallest rupture events were consistent with the breakage of individual integrin–collagen bonds. Above 60 s, a fraction of cells rapidly switched into an activated adhesion state marked by up to 10-fold increased detachment forces. Elevated overall cell adhesion coincided with a rise of the smallest rupture forces above the value required to break a single-integrin–collagen bond, suggesting a change from single to cooperative receptor binding. Transition into the activated adhesion mode and the increase of the smallest rupture forces were both blocked by inhibitors of actomyosin contractility. We therefore propose a two-step mechanism for the establishment of ₂₁-mediated adhesion as weak initial, single-integrin–mediated binding events are superseded by strong adhesive interactions involving receptor cooperativity and actomyosin contractility.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Clemens M. Franz (franz{at}biotec.tu-dresden.de)

Abbreviations used: AFM, atomic force microscopy; CHO, Chinese hamster ovary; DFS, dynamic force spectroscopy; SCFS, single-cell force spectroscopy.

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