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Probing Intercellular Interactions between Vascular Endothelial Cadherin Pairs at Single-molecule Resolution and in Living Cells
Vascular endothelial (VE) cadherin is the surface glycoprotein cadherin specific to the endothelium that mediates cell–cell adhesion and plays a major role in the remodeling, gating, and maturation of vascular vessels. To investigate the contribution of individual VE-cadherins to endothelial cell–ce...
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Published in: | Journal of molecular biology 2006-05, Vol.358 (3), p.665-674 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Vascular endothelial (VE) cadherin is the surface glycoprotein cadherin specific to the endothelium that mediates cell–cell adhesion and plays a major role in the remodeling, gating, and maturation of vascular vessels. To investigate the contribution of individual VE-cadherins to endothelial cell–cell interactions and investigate whether different classical cadherins display different kinetics and micromechanical properties, we characterize the binding properties of VE-cadherin/VE-cadherin bonds at single-molecule resolution and in living human umbilical vein endothelial cells (HUVECs). Our single-molecule force spectroscopy measurements reveal that type II VE-cadherin molecules form bonds that are less prone to rupture and display a higher tensile strength than bonds formed by classical type I neuronal (N) cadherin and epithelial (E) cadherin. The equilibrium lifetime of the VE-cadherin/VE-cadherin bond is significantly longer than formed by N-cadherin/N-cadherin bonds and E-cadherin/E-cadherin bonds. These results indicate that VE-cadherins form bonds that have kinetics and mechanical properties that are significantly different from those formed by classical type I cadherins, properties that are particularly well adapted to the barrier and adhesive functions of VE-cadherin in endothelial cell–cell junctions. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1016/j.jmb.2006.02.021 |