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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Caremani, Marco Lombardi, Vincenzo Reconditi, Massimo Stienen, Ger J. M. Linari, Marco Pinzauti, Francesca Piazzesi, Gabriella |
| Description | Author Affiliation: Caremani M ( Laboratory of Physiology, Department of Biology, Università di Firenze, 50019 Sesto Fiorentino, Florence, Italy); Pinzauti F ( Laboratory of Physiology, Department of Biology, Università di Firenze, 50019 Sesto Fiorentino, Florence, Italy); Reconditi M ( Laboratory of Physiology, Department of Biology, Università di Firenze, 50019 Sesto Fiorentino, Florence, Italy); Piazzesi G ( Laboratory of Physiology, Department of Biology, Università di Firenze, 50019 Sesto Fiorentino, Florence, Italy); Stienen GJ ( Department of Physiology, Institute for Cardiovascular Research, VU University Medical Center, 1081 HV Amsterdam, The Netherlands); Lombardi V ( Laboratory of Physiology, Department of Biology, Università di Firenze, 50019 Sesto Fiorentino, Florence, Italy); Linari M ( Laboratory of Physiology, Department of Biology, Università di Firenze, 50019 Sesto Fiorentino, Florence, Italy); |
| Abstract | The power in the myocardium sarcomere is generated by two bipolar arrays of the motor protein cardiac myosin II extending from the thick filament and pulling the thin, actin-containing filaments from the opposite sides of the sarcomere. Despite the interest in the definition of myosin-based cardiomyopathies, no study has yet been able to determine the mechanokinetic properties of this motor protein in situ. Sarcomere-level mechanics recorded by a striation follower is used in electrically stimulated intact ventricular trabeculae from the rat heart to determine the isotonic velocity transient following a stepwise reduction in force from the isometric peak force TP to a value T(0.8-0.2 TP). The size and the speed of the early rapid shortening (the isotonic working stroke) increase by reducing T from â ¼3 nm per half-sarcomere (hs) and 1,000 s(-1) at high load to â ¼8 nmâ hs(-1) and 6,000 s(-1) at low load. Increases in sarcomere length (1.9-2.2 µm) and external [Ca(2+)]o (1-2.5 mM), which produce an increase of TP, do not affect the dependence on T, normalized for TP, of the size and speed of the working stroke. Thus, length- and Ca(2+)-dependent increase of TP and power in the heart can solely be explained by modulation of the number of myosin motors, an emergent property of their array arrangement. The motor working stroke is similar to that of skeletal muscle myosin, whereas its speed is about three times slower. A new powerful tool for investigations and therapies of myosin-based cardiomyopathies is now within our reach. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 113 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2016-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cardiac Myosins Physiology Myocardial Contraction Animals Biomechanical Phenomena Calcium Metabolism Electric Stimulation In Vitro Techniques Molecular Motor Proteins Rats, Wistar Sarcomeres Ventricular Myosins Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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