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骨骼肌肌原纤维中伴肌动蛋白弹性特性的微观分析。

Microscopic analysis of the elastic properties of nebulin in skeletal myofibrils.

作者信息

Yasuda K, Anazawa T, Ishiwata S

机构信息

Advanced Research Laboratory, Hitachi Ltd., Saitama, Japan.

出版信息

Biophys J. 1995 Feb;68(2):598-608. doi: 10.1016/S0006-3495(95)80221-3.

DOI:10.1016/S0006-3495(95)80221-3
PMID:7696512
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1281724/
Abstract

The elastic properties of nebulin were studied by measuring the elasticity of single skeletal myofibrils, from which the portion of the thin filament located at the I band had been selectively removed by treatment with plasma gelsolin under rigor conditions. In this myofibril model, a portion of each nebulin molecule at the I band was expected to be free of actin filaments and exposed. The length of the exposed portion of the nebulin molecule was controlled by performing the gelsolin treatment at various sarcomere lengths. The relation between the passive tension and extension of the exposed portion of the nebulin showed a convex curve starting from a slack length, apparently in a fashion similar to that of wool. The slack sarcomere length shifted depending on the length of the exposed portion of the nebulin, however, the relation being represented by a single master curve. The elastic modulus of nebulin was estimated to be two to three orders of magnitude smaller than that of an actin filament. Based on these results, we conclude that nebulin attaches to an actin filament in a side-by-side fashion and that it does not significantly contribute to the elastic modulus of thin filaments. The relation between the passive tension and extension of connectin (titin) was obtained for a myofibril from which thin filaments had been completely removed with gelsolin under contracting conditions; this showed a concave curve, consistent with the previous results obtained in single fibers.

摘要

通过测量单个骨骼肌肌原纤维的弹性来研究伴肌动蛋白的弹性特性，在严格条件下用血浆凝溶胶蛋白处理后，位于I带的细肌丝部分已被选择性去除。在这个肌原纤维模型中，预计I带处每个伴肌动蛋白分子的一部分没有肌动蛋白丝并暴露在外。通过在不同肌节长度下进行凝溶胶蛋白处理来控制伴肌动蛋白分子暴露部分的长度。伴肌动蛋白暴露部分的被动张力与伸长之间的关系呈现出从松弛长度开始的凸曲线，显然与羊毛的情况类似。然而，松弛肌节长度随伴肌动蛋白暴露部分的长度而变化，这种关系由一条单一的主曲线表示。伴肌动蛋白的弹性模量估计比肌动蛋白丝的弹性模量小两到三个数量级。基于这些结果，我们得出结论，伴肌动蛋白以并排的方式附着在肌动蛋白丝上，并且它对细肌丝的弹性模量没有显著贡献。对于在收缩条件下用凝溶胶蛋白完全去除细肌丝的肌原纤维，获得了连接蛋白（肌联蛋白）的被动张力与伸长之间的关系；这显示出一条凹曲线，与之前在单纤维中获得的结果一致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/6452c6b32148/biophysj00066-0207-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/da0d4d4b398a/biophysj00066-0206-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/bfe5664b63c5/biophysj00066-0206-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/6452c6b32148/biophysj00066-0207-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/da0d4d4b398a/biophysj00066-0206-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/bfe5664b63c5/biophysj00066-0206-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8358/1281724/6452c6b32148/biophysj00066-0207-a.jpg

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Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments.心肌原位弹性丝：结合肌动蛋白和肌球蛋白丝的选择性去除进行深度蚀刻复型分析
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