This article is published in Journal of Molecular Recognition as a special issue on Affinity 2009, edited by Gideon Fleminger, Tel-Aviv University, Tel-Aviv, Israel and George Ehrlich, Hoffmann-La Roche, Nutley, NJ, USA.
AFM functional imaging on vascular endothelial cells†
Article first published online: 28 OCT 2010
Copyright © 2010 John Wiley & Sons, Ltd.
Journal of Molecular Recognition
Special Issue: Affinity 2009 – The 18th biennial meeting of the International Society for Molecular Recognition
Volume 23, Issue 6, pages 589–596, November/December 2010
How to Cite
Chtcheglova, L. A., Wildling, L., Waschke, J., Drenckhahn, D. and Hinterdorfer, P. (2010), AFM functional imaging on vascular endothelial cells. J. Mol. Recognit., 23: 589–596. doi: 10.1002/jmr.1052
- Issue published online: 28 OCT 2010
- Article first published online: 28 OCT 2010
- Manuscript Accepted: 10 APR 2010
- Manuscript Revised: 12 MAR 2010
- Manuscript Received: 29 NOV 2009
Vascular endothelial (VE)-cadherin is predominantly responsible for the mechanical linkage between endothelial cells, where VE-cadherin molecules are clustered and linked through their cytoplasmic domain to the actin-based cytoskeleton. Clustering and linkage of VE-cadherin to actin filaments is a dynamic process and changes according to the functional state of the cells. Here nano-mapping of VE-cadherin was performed using simultaneous topography and recognition imaging (TREC) technique onto microvascular endothelial cells from mouse myocardium (MyEnd). The recognition maps revealed prominent ‘dark’ spots (domains or clusters) with the sizes from 10 to 250 nm. These spots arose from a decrease of oscillation amplitude during specific binding between VE-cadherin cis-dimers. They were assigned to characteristic structures of the topography images. After treatment with nocodazole so as to depolymerize microtubules, VE-cadherin domains with a typical ellipsoidal form were still found to be collocalized with cytoskeletal filaments supporting the hypothesis that VE-cadherin is linked to actin filaments. Compared to other conventional techniques such as immunochemistry or single molecule optical microscopy, TREC represents an alternative method to quickly obtain the local distribution of receptors on cell surface with an unprecedented lateral resolution of several nanometers. Copyright © 2010 John Wiley & Sons, Ltd.