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体外将微结构与束状交联F-肌动蛋白网络的流变学相关联。

Relating microstructure to rheology of a bundled and cross-linked F-actin network in vitro.

作者信息

Shin J H, Gardel M L, Mahadevan L, Matsudaira P, Weitz D A

机构信息

Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

出版信息

Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9636-41. doi: 10.1073/pnas.0308733101. Epub 2004 Jun 21.

Abstract

The organization of individual actin filaments into higher-order structures is controlled by actin-binding proteins (ABPs). Although the biological significance of the ABPs is well documented, little is known about how bundling and cross-linking quantitatively affect the microstructure and mechanical properties of actin networks. Here we quantify the effect of the ABP scruin on actin networks by using imaging techniques, cosedimentation assays, multiparticle tracking, and bulk rheology. We show how the structure of the actin network is modified as the scruin concentration is varied, and we correlate these structural changes to variations in the resultant network elasticity.

摘要

肌动蛋白单丝组装成高阶结构受肌动蛋白结合蛋白(ABP)控制。尽管ABP的生物学意义已有充分记载,但对于成束和交联如何定量影响肌动蛋白网络的微观结构和力学性能却知之甚少。在此,我们通过成像技术、共沉降分析、多粒子追踪和本体流变学来量化ABP scruin对肌动蛋白网络的影响。我们展示了随着scruin浓度的变化,肌动蛋白网络结构如何改变,并将这些结构变化与所得网络弹性的变化相关联。

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