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首页> 外文期刊>Cytoskeleton >Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding
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Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding

机译：强迫性扩展血脂的红细胞细胞骨架，几乎没有血影蛋白展开的迹象

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摘要

Force-extension curves obtained on intact human red blood cells (RBC) were compared with those of delipidated RBCs to assess the contribution of cytoskeletal flexibility to the extensibility of the intact membrane skeleton. The RBCs were first delipidated by treatment with phospholipase A 2; tensile properties of the exposed cytoskeletal structures were measured using an atomic force microscope (AFM). The AFM probes were modified either with the Band 3 specific lectin, concanavalin A, (Con A) or anti-F-actin antibody, to localize the point of interaction between the probe and the cytoskeleton. Extension of the spectrin-based cytoskeleton reached up to 2-3 μm with a force less than 70 pN without showing any force peaks before the final rupture of the adhesive bonds. Our interpretation of the result is that the spectrin-based network was slack enough to allow the observed degree of extension without unfolding the tetrameric spectrin molecules. The force-extension curves obtained either on Band 3-ankyrin loci or on junction nodes of the cytoskeleton were not significantly different. Experimental results were verified by computer simulation of pulling mechanics of a network model of the RBC cytoskeleton. Our experimental results are also in agreement with the theoretical prediction of Mirijanian and Voth [2008; Proc Natl Acad Sci USA 105:1204-1208].
机译：将在完整的人红细胞（RBC）上获得的力-延伸曲线与脂质的RBC进行比较，以评估细胞骨架柔韧性对完整膜骨架可扩展性的贡献。首先通过用磷脂酶A 2处理使RBC脱脂;然后用磷脂酶A 2处理。使用原子力显微镜（AFM）测量暴露的细胞骨架结构的拉伸性能。用Band 3特异性凝集素，伴刀豆球蛋白A（Con A）或抗F-肌动蛋白抗体对AFM探针进行修饰，以定位探针和细胞骨架之间的相互作用点。基于血影蛋白的细胞骨架的延伸以小于70pN的力达到了2-3μm，而在粘合剂键的最终断裂之前没有显示任何力峰。我们对结果的解释是，基于血影蛋白的网络足够松弛，以允许观察到的扩展程度而不会展开四聚体血影蛋白分子。在带3-锚蛋白位点上或在细胞骨架的连接节点上获得的力-延伸曲线没有显着差异。通过计算机模拟RBC细胞骨架网络模型的拉动力学来验证实验结果。我们的实验结果也与Mirijanian和Voth [2008;美国国家科学院院刊105：1204-1208]。

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