• Nishikawa, Kiisa
• Nissen, D.
• Irving, T.
• Mishra, D.
• Kuehn, M.
• Joumaa, V.
• Freundt, J.
• Wa, Linke
• Hessel, Anthony

Abstract

In muscle, titin proteins connect myofilaments together and are thought to be critical for contraction, especially during residual force enhancement (RFE) when force is elevated after an active stretch. We investigated titin’s function during contraction using small-angle X-ray diffraction to track structural changes before and after 50% titin cleavage and in the RFE-deficient, <i>mdm</i> titin mutant. We report that the RFE state is structurally distinct from pure isometric contractions, with increased thick filament strain and decreased lattice spacing, most likely caused by elevated titin-based forces. Furthermore, no RFE structural state was detected in <i>mdm</i> muscle. We posit that decreased lattice spacing, increased thick filament stiffness, and increased non-crossbridge forces are the major contributors to RFE. We conclude that titin directly contributes to RFE.<h4>One-sentence summary</h4>Titin contributes to active force production and residual force enhancement in skeletal muscles.

Topics

• impedance spectroscopy
• small-angle X-ray diffraction