Force measurements of the α5β1 integrin-fibronectin interaction
Force measurements of the α5β1 integrin-fibronectin interaction
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DOI：
10.1016/s0006-3495(03)74940-6
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发表时间：
2003-02-01
影响因子：
3.4
通讯作者：
Moy, VT
中科院分区：
文献类型：
--
作者：
Li, FY;Redick, SD;Moy, VT
α（5）β（1）整联蛋白与其配体纤连蛋白（FN）的相互作用在细胞与细胞外基质的粘附中起着至关重要的作用。α（5）β（1）/FN相互作用的一个重要内在性质是复合物对拉力的动态响应。我们已经进行了α（5）β（1）和纤连蛋白片段之间相互作用的原子力显微镜测量，所述纤连蛋白片段来自FN的第七至第十III型重复序列（即，FN 7 -10），其含有arg-gly-asp（RGD）序列和协同位点。从由附着于原子力显微镜悬臂的表达α（5）β（1）的K562细胞和吸附在基底上的FN 7 -10组成的实验系统获得的直接力测量用于确定α（5）β（1）/FN 7 -10复合物对拉力的动态响应。实验在加载速率的三个数量级变化上进行，并且在允许检测单个α（5）β（1）/FN 7 -10相互作用的条件下进行。α（5）β（1）/FN 7 -10复合物的动态断裂力揭示了两种加载方式：快速加载方式（> 10，000 pN/s）和慢速加载方式（
The interaction of the alpha(5)beta(1) integrin and its ligand, fibronectin (FN), plays a crucial role in the adhesion of cells to the extracellular matrix. An important intrinsic property of the alpha(5)beta(1)/FN interaction is the dynamic response of the complex to a pulling force. We have carried out atomic force microscopy measurements of the interaction between alpha(5)beta(1) and a fibronectin fragment derived from the seventh through tenth type III repeats of FN (i.e., FN7-10) containing both the arg-gly-asp (RGD) sequence and the synergy site. Direct force measurements obtained from an experimental system consisting of an alpha(5)beta(1) expressing K562 cell attached to the atomic force microscopy cantilever and FN7-10 adsorbed on a substrate were used to determine the dynamic response of the alpha(5)beta(1)/FN7-10 complex to a pulling force. The experiments were carried out over a three-orders-of-magnitude change in loading rate and under conditions that allowed for detection of individual alpha(5)beta(1)/FN7-10 interactions. The dynamic rupture force of the alpha(5)beta(1)/FN7-10 complex revealed two regimes of loading: a fast loading regime (>10,000 pN/s) and a slow loading regime (