This review highlights the critical role of the giant protein titin in determining the structural assembly and passive elastic properties of muscle sarcomeres.
Answers are grounded in this paper and cite their sources.
May refine sarcomere models in research; leaves open clinical targeting in diastolic dysfunction.
The giant protein titin is thought to play major roles in the assembly and function of muscle sarcomeres. Structural details, such as widths of Z- and M-lines and periodicities in the thick filaments, correlate with the substructure in the respective regions of the titin molecule. Sarcomere rest length, its operating range of lengths, and passive elastic properties are also directly controlled by the properties of titin. Here we review some recent titin data and discuss its implications for sarcomere architecture and elasticity.
No takes yet. Share an insight, caveat, or question.
Tskhovrebova et al. (2010) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: