Probing intercellular interactions between vascular endothelial cadherin pairs at single-molecule resolution and in living cells
Probing intercellular interactions between vascular endothelial cadherin pairs at single-molecule resolution and in living cells
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DOI：
10.1016/j.jmb.2006.02.021
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发表时间：
2006-05-05
影响因子：
5.6
通讯作者：
Wirtz, D
中科院分区：
文献类型：
--
作者：
Panorchan, P;George, JP;Wirtz, D
血管内皮 (VE) 钙粘蛋白是内皮特异性的表面糖蛋白钙粘蛋白，介导细胞间粘附，在血管的重塑、门控和成熟中发挥重要作用。为了研究单个VE-钙粘蛋白对内皮细胞-细胞相互作用的贡献，并研究不同的经典钙粘蛋白是否表现出不同的动力学和微机械特性，我们以单分子分辨率和活体人脐静脉内皮细胞（HUVEC）中表征了VE-钙粘蛋白/VE-钙粘蛋白键的结合特性。我们的单分子力谱测量表明，11 型 V-E-钙粘蛋白分子形成的键不易破裂，并且比经典 I 型神经元 (N) 钙粘蛋白和上皮 (E) 钙粘蛋白形成的键具有更高的拉伸强度。 VE-钙粘蛋白/VE-钙粘蛋白键的平衡寿命明显长于N-钙粘蛋白/N-钙粘蛋白键和E-钙粘蛋白/E-钙粘蛋白键形成的平衡寿命。这些结果表明，VE-钙粘蛋白形成的键具有与经典I型钙粘蛋白形成的动力学和机械特性显着不同的键，这些特性特别适合内皮细胞-细胞连接中VE-钙粘蛋白的屏障和粘附功能。 (c) 2006 Elsevier Ltd. 保留所有权利。
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 11 V-E-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. (c) 2006 Elsevier Ltd. All rights reserved.