Single-molecule dynamic force spectroscopy of the fibronectin-heparin interaction

被引:9
作者
Mitchell, Gabriel
Lamontagne, Charles-Antoine
Lebel, Rejean
Grandbois, Michel
Malouin, Francois
机构
[1] Univ Sherbrooke, Fac Med Sci Sante, Dept Pharmacol, Sherbrooke, PQ J1H 5N4, Canada
[2] Univ Sherbrooke, Fac Sci, Dept Biol, CEVDM, Sherbrooke, PQ J1K 2R1, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
extracellular matrix; glycosamynoglycans; heparan sulfate; atomic force spectroscopy; off-rate; dissociation; barrier width;
D O I
10.1016/j.bbrc.2007.10.034
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 +/- 0.2 angstrom and an off-rate of 0.2 +/- 0.1 s(-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. (C) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:595 / 600
页数:6
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