Mitchell Gabriel, Lamontagne Charles-Antoine, Lebel Réjean, Grandbois Michel, Malouin François
Centre d'Etude et de Valorisation de la Diversité Microbienne (CEVDM), Département de biologie, Faculté des sciences, Université de Sherbrooke, Sherbrooke, Que., Canada J1K 2R1.
Biochem Biophys Res Commun. 2007 Dec 21;364(3):595-600. doi: 10.1016/j.bbrc.2007.10.034. Epub 2007 Oct 15.
The integrity of cohesive tissues strongly depends on the presence of the extracellular matrix, which provides support and anchorage for cells. The fibronectin protein and the heparin-like glycosaminoglycans are key components of this dynamic structural network. In this report, atomic force spectroscopy was used to gain insight into the compliance and the resistance of the fibronectin-heparin interaction. We found that this interaction can be described by an energetic barrier width of 3.1+/-0.2A and an off-rate of 0.2+/-0.1s(-1). These dissociation parameters are similar to those of other carbohydrate-protein interactions and to off-rate values reported for more complex interactions between cells and extracellular matrix components. Our results indicate that the function of the fibronectin-heparin interaction is supported by its capacity to sustain significant deformations and considerable external mechanical forces.
粘性组织的完整性在很大程度上依赖于细胞外基质的存在,细胞外基质为细胞提供支持和锚定。纤连蛋白和类肝素糖胺聚糖是这个动态结构网络的关键组成部分。在本报告中,原子力光谱被用于深入了解纤连蛋白 - 肝素相互作用的柔顺性和阻力。我们发现,这种相互作用可以用3.1±0.2埃的能量势垒宽度和0.2±0.1秒⁻¹的解离速率来描述。这些解离参数与其他碳水化合物 - 蛋白质相互作用的参数以及报道的细胞与细胞外基质成分之间更复杂相互作用的解离速率值相似。我们的结果表明,纤连蛋白 - 肝素相互作用的功能得益于其承受显著变形和相当大外部机械力的能力。