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本文引用的文献

1
Intermediate filaments: from cell architecture to nanomechanics.中间丝:从细胞结构到纳米力学
Nat Rev Mol Cell Biol. 2007 Jul;8(7):562-73. doi: 10.1038/nrm2197.
2
Muscle intermediate filaments and their links to membranes and membranous organelles.肌肉中间丝及其与膜和膜性细胞器的连接
Exp Cell Res. 2007 Jun 10;313(10):2063-76. doi: 10.1016/j.yexcr.2007.03.033. Epub 2007 Apr 3.
3
Biomechanical properties of intermediate filaments: from tissues to single filaments and back.中间丝的生物力学特性:从组织到单根丝,再回归组织
Bioessays. 2007 Jan;29(1):26-35. doi: 10.1002/bies.20514.
4
Impact of disease mutations on the desmin filament assembly process.疾病突变对结蛋白丝组装过程的影响。
J Mol Biol. 2006 Jul 28;360(5):1031-42. doi: 10.1016/j.jmb.2006.05.068. Epub 2006 Jun 16.
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A generalized description of the elastic properties of nanowires.纳米线弹性性质的一般性描述。
Nano Lett. 2006 Jun;6(6):1101-6. doi: 10.1021/nl060028u.
6
Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy.通过原子力显微镜探索单个波形蛋白中间丝的力学性能。
J Mol Biol. 2006 Jul 14;360(3):623-30. doi: 10.1016/j.jmb.2006.05.030.
7
Exploring the mechanical behavior of single intermediate filaments.探索单个中间丝的力学行为。
J Mol Biol. 2005 Dec 2;354(3):569-77. doi: 10.1016/j.jmb.2005.09.092. Epub 2005 Oct 21.
8
Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages.导致严重肌肉疾病的结蛋白突变在不同阶段干扰体外细丝组装。
Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15099-104. doi: 10.1073/pnas.0504568102. Epub 2005 Oct 10.
9
Investigation of the morphology of intermediate filaments adsorbed to different solid supports.吸附于不同固体支持物上的中间丝形态学研究。
J Struct Biol. 2005 Jun;150(3):268-76. doi: 10.1016/j.jsb.2005.02.012. Epub 2005 Apr 2.
10
Intermediate filament proteins and their associated diseases.中间丝蛋白及其相关疾病。
N Engl J Med. 2004 Nov 11;351(20):2087-100. doi: 10.1056/NEJMra040319.

单个结蛋白中间丝的拉伸特性

Tensile properties of single desmin intermediate filaments.

作者信息

Kreplak Laurent, Herrmann Harald, Aebi Ueli

机构信息

M. E Müller Institute for Structural Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland.

出版信息

Biophys J. 2008 Apr 1;94(7):2790-9. doi: 10.1529/biophysj.107.119826. Epub 2008 Jan 4.

DOI:10.1529/biophysj.107.119826
PMID:18178641
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2267133/
Abstract

Within muscle fibers, desmin intermediate filaments (IFs) are major constituents of the extrasarcomeric cytoskeleton. However, their contribution to the mechanical properties of myocytes has remained elusive. We present an experimental approach to measure the extensibility and the tensile strength of in vitro reconstituted desmin IFs adsorbed to a solid support. The tip of an atomic force microscope (AFM) was used to push on single filaments perpendicular to the filament axis. The torque of the AFM cantilever was monitored during the pushing events to yield an estimate of the lateral force necessary to bend and stretch the filaments. Desmin IFs were stretched up to 3.4-fold with a maximum force of approximately 3.5 nN. Fully stretched filaments exhibited a much smaller diameter than did native IFs, i.e., approximately 3.5 nm compared to 12.6 nm, both by AFM and electron microscopy. Moreover, we combined the morphological and lateral force data to compute an average stress-strain curve for a single desmin filament. The main features were a pronounced strain-hardening regime above 50% extension and a tensile strength of at least 240 MPa. Because of these nonlinear tensile properties, desmin IFs may dissipate mechanical energy and serve as a physical link between successive sarcomeres during large deformation.

摘要

在肌纤维内,结蛋白中间丝(IFs)是肌节外细胞骨架的主要成分。然而,它们对心肌细胞力学特性的贡献仍不明确。我们提出了一种实验方法,用于测量吸附在固体支持物上的体外重构结蛋白IFs的可伸展性和拉伸强度。使用原子力显微镜(AFM)的尖端垂直于细丝轴推压单根细丝。在推压过程中监测AFM悬臂的扭矩,以估算弯曲和拉伸细丝所需的侧向力。结蛋白IFs可拉伸至3.4倍,最大力约为3.5 nN。通过AFM和电子显微镜观察,完全拉伸的细丝直径比天然IFs小得多,即分别约为3.5 nm和12.6 nm。此外,我们结合形态学和侧向力数据,计算了单个结蛋白细丝的平均应力-应变曲线。主要特征是在延伸率超过50%时出现明显的应变硬化阶段,拉伸强度至少为240 MPa。由于这些非线性拉伸特性,结蛋白IFs可能耗散机械能,并在大变形过程中作为连续肌节之间的物理连接。