Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 2 October 2007
Vol. 2007, Issue 406, p. pl5
[DOI: 10.1126/stke.4062007pl5]


Studying Integrin-Mediated Cell Adhesion at the Single-Molecule Level Using AFM Force Spectroscopy

Clemens M. Franz1*, Anna Taubenberger1, Pierre-Henri Puech2, and Daniel J. Muller1

1BioTechnological Center, University of Technology Dresden, Tatzberg 47-51, 01307 Dresden, Germany.
2INSERM UMR 600/CNRS UMR 6212, Adhésion Cellulaire et Inflammation Case 937, 163 Avenue de Luminy, 13288 Marseille, France.

Abstract: The establishment of cell adhesion involves specific recognition events between individual cell-surface receptors and molecules of the cellular environment. However, characterizing single-molecule adhesion events in the context of a living cell presents an experimental challenge. The atomic force microscope (AFM) operated in force spectroscopy mode provides an ultrasensitive method to investigate cell adhesion forces at the level of single receptor-ligand bonds. With a living cell attached to the AFM cantilever, the number of cell-substrate interactions can be controlled and limited to the formation of single receptor-ligand bonds. From force-distance (F-D) curves recorded during cell detachment, the strength of single receptor-ligand bonds can be determined. Furthermore, by varying the rate of force application during bond rupture, a dynamic force spectrum (DFS) can be generated from which additional parameters that describe the energy landscape of the interaction, such as dissociation rate and energy barrier width, can be obtained. Using the example of {alpha}2beta1 integrin–mediated adhesion to type I collagen, we provide a detailed description of how dynamic AFM single-cell force spectroscopy (SCFS) adhesion measurements can be performed with single-molecule sensitivity, and how specific energy landscape parameters of the integrin-collagen bond can be extracted from the DFS.

*Corresponding author. E-mail, franz{at}

Citation: C. M. Franz, A. Taubenberger, P.-H. Puech, D. J. Muller, Studying Integrin-Mediated Cell Adhesion at the Single-Molecule Level Using AFM Force Spectroscopy. Sci. STKE 2007, pl5 (2007).

Read the Full Text

Mechanics of the Toxoplasma gondii oocyst wall.
A. Dumetre, J. P. Dubey, D. J. P. Ferguson, P. Bongrand, N. Azas, and P.-H. Puech (2013)
PNAS 110, 11535-11540
   Abstract »    Full Text »    PDF »
Integrin adhesion and force coupling are independently regulated by localized PtdIns(4,5)2 synthesis.
K. R. Legate, S. Takahashi, N. Bonakdar, B. Fabry, D. Boettiger, R. Zent, and R. Fassler (2011)
EMBO J. 30, 4539-4553
   Abstract »    Full Text »    PDF »
Microtubule-induced nuclear envelope fluctuations control chromatin dynamics in Drosophila embryos.
B. Hampoelz, Y. Azou-Gros, R. Fabre, O. Markova, P.-H. Puech, and T. Lecuit (2011)
Development 138, 3377-3386
   Abstract »    Full Text »    PDF »
2B4 Engagement Mediates Rapid LFA-1 and Actin-Dependent NK Cell Adhesion to Tumor Cells as Measured by Single Cell Force Spectroscopy.
S. C. Hoffmann, A. Cohnen, T. Ludwig, and C. Watzl (2011)
J. Immunol. 186, 2757-2764
   Abstract »    Full Text »    PDF »
Nongenomic Effects of Cisplatin: Acute Inhibition of Mechanosensitive Transporters and Channels without Actin Remodeling.
N. Milosavljevic, C. Duranton, N. Djerbi, P. H. Puech, P. Gounon, D. Lagadic-Gossmann, M. T. Dimanche-Boitrel, C. Rauch, M. Tauc, L. Counillon, et al. (2010)
Cancer Res. 70, 7514-7522
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882