A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
M Gautel, D Goulding - FEBS letters, 1996 - Wiley Online Library
M Gautel, D Goulding
FEBS letters, 1996•Wiley Online LibraryIn 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 …
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 …
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.
Wiley Online Library