A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series

FEBS Letters

Gautel, Mathias¹  Goulding, David¹ 

[1] European Molecular Biology Laboratory, Biological Structures Division, Postfach 102209, 69012 Heidelberg, Germany

关键词: Titin;    Connectin;    Muscle elasticity;    Ultrastructure;    Immunoelectron microscopy;    Monoclonal antibody;   

DOI  :  10.1016/0014-5793(96)00338-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In the I-band of skeletal muscle sarcomeres, the elastic region of titin consists of immunoglobulin (1g) 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 μm, decreasing in slope towards higher lengths. The Ig domains do not unfold. Above 2.6 μm, 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.

【 授权许可】

Unknown