共 21 条
A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
被引:98
作者:
Gautel, M
Goulding, D
机构:
[1] Europ. Molecular Biology Laboratory, Biological Structures Division, 69012 Heidelberg
来源:
FEBS LETTERS
|
1996年
/
385卷
/
1-2期
关键词:
titin;
connectin;
muscle elasticity;
ultrastructure;
immunoelectron microscopy;
monoclonal antibody;
D O I:
10.1016/0014-5793(96)00338-9
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:11 / 14
页数:4
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