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A more recent version of this article appeared on May 1, 2007
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Submitted on September 5, 2006
Revised on January 19, 2007
Accepted on February 9, 2007
2
1 Integrin-mediated Adhesion to Collagen Type I Using Single-Cell Force Spectroscopy
*BioTechnological Center, University of Technology Dresden, 01307 Dresden, Germany; Unité Mixte de Recherche INSERM 600/Centre National de la Recherche Scientifique Unité Mixte de Recherche 6212, Adhésion Cellulaire et Inflammation, 13288 Marseille, France
Monitoring Editor: Jean Schwarzbauer
We have characterized early steps of 
2
1 integrin-mediated cell adhesion to a collagen type I matrix using single-cell force spectroscopy. In agreement with the role of 21 as a collagen type I receptor, 21-expressing CHO-A2 cells spread rapidly on the matrix, while 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mechanism for the establishment of 21-mediated adhesion as weak initial, single-integrin-mediated binding events are superseded by strong adhesive interactions involving receptor cooperativity and actomyosin contractility.
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