A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
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DOI：
10.1016/0014-5793(96)00338-9
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发表时间：
1996-04-29
期刊：
影响因子：
3.5
通讯作者：
Goulding, D
中科院分区：
文献类型：
--
作者：
Gautel, M;Goulding, D
在骨骼肌肌节的I带中，Thin的弹性区域由免疫球蛋白(Ig)结构域和富含脯氨酸、疏水和带电残基的非模块化区域(PEVK)组成。使用免疫电子显微镜和序列分配的单抗，我们证明腰椎分枝杆菌Ig区的延伸主要发生在肌节长度在2到2.8微米之间，斜率向更高的长度递减。Ig域不会展开。在2.6亩以上，由于PEVK富集区的原因，长度变化越来越大。因此，我们认为PEVK富集区的橡胶性质主要是对骨骼肌动蛋白弹性的贡献。
In the I-band of skeletal muscle sarcomeres, the elastic region of thin consists of immunoglobulin (Ig) domains, and non-modular regions rich in proline, hydrophobic, and charged residues (PEVK). Using immunoelectron microscopy with sequence-assigned monoclonal antibodies, we demonstrate that extension of the Ig regions in M. psoas occurs largely at sarcomere lengths between 2 and 2.8 mu m, decreasing in slope towards higher lengths. The Ig domains do not unfold. Above 2.6 mu m, length changes are increasingly due to the PEVK-rich regions. We therefore propose that rubber-like properties of the PEVK-rich regions are mainly contributing to skeletal titin elasticity.