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.
Original language | English (US) |
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Pages (from-to) | 284-295 |
Number of pages | 12 |
Journal | Circulation research |
Volume | 94 |
Issue number | 3 |
DOIs | |
State | Published - Feb 20 2004 |
Externally published | Yes |
Keywords
- Connectin
- Contractility
- Myocardial stiffness
- Passive stiffness
- Stretch
ASJC Scopus subject areas
- Physiology
- Cardiology and Cardiovascular Medicine