Abstract
The sarcomere contains, in addition to thin and thick filaments, a filament composed of the giant protein titin (also known as connectin). Titin molecules anchor in the Z-disc and extend to the M-line region of the sarcomere. The majority of titin’s I-band region functions as a molecular spring. This spring maintains the precise structural arrangement of thick and thin filaments, and gives rise to passive muscle stiffness; an important determinant of diastolic filling. Earlier work on titin has been reviewed before. In this study, our main focus is on recent findings vis-à-vis titin’s molecular spring segments in cardiac titins, including the discovery of fetal cardiac isoforms with novel spring elements. We also discuss new insights regarding the role of titin as a biomechanical sensor and signaling molecule. We will end with focusing on the rapidly growing knowledge regarding titinopathies.
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Dates
Type | When |
---|---|
Created | 21 years, 6 months ago (Feb. 19, 2004, 4:38 p.m.) |
Deposited | 1 year, 3 months ago (May 12, 2024, 2:14 p.m.) |
Indexed | 4 weeks, 1 day ago (Aug. 7, 2025, 4:27 p.m.) |
Issued | 21 years, 6 months ago (Feb. 20, 2004) |
Published | 21 years, 6 months ago (Feb. 20, 2004) |
Published Print | 21 years, 6 months ago (Feb. 20, 2004) |
@article{Granzier_2004, title={The Giant Protein Titin: A Major Player in Myocardial Mechanics, Signaling, and Disease}, volume={94}, ISSN={1524-4571}, url={http://dx.doi.org/10.1161/01.res.0000117769.88862.f8}, DOI={10.1161/01.res.0000117769.88862.f8}, number={3}, journal={Circulation Research}, publisher={Ovid Technologies (Wolters Kluwer Health)}, author={Granzier, Henk L. and Labeit, Siegfried}, year={2004}, month=feb, pages={284–295} }