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Am J Physiol Heart Circ Physiol 281: H1793-H1799, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 4, H1793-H1799, October 2001

Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently

K. Trombitás1, Y. Wu1, D. Labeit2, S. Labeit2, and H. Granzier1

1 Veterinary and Comparative Anatomy, Pharmacology and Physiology, Washington State University, Pullman, Washington 99164-6520; and 2 Anesthesiology and Intensive Operative Medicine, University Hospital Mannheim, Mannheim, Germany 68135

Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that contain length variants of the molecular spring segment. We investigated how coexpression of isoforms takes place at the level of the half-sarcomere, and whether coexpression affects the extensibility of the isoforms. Immunoelectron microscopy was used to study local coexpression of isoforms in a range of species. It was found that the cardiac sarcomere of large mammals coexpresses N2B and N2BA titin isoforms at the level of the half-sarcomere, and that when coexpressed, the isoforms act independently of one another. Coexpressing isoforms at varying ratios results in modulation of the passive mechanical behavior of the sarcomere without impacting other functions of titin and allows for adjustment of the diastolic properties of the myocardium.

diastole; elasticity; structure; mechanics; physiology


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