Myosin from the ventricle is more sensitive to omecamtiv mecarbil than myosin from the atrium
| Autor: | Valentina Y. Berg, L.V. Nikitina, Sergey Y. Bershitsky, Anastasia M. Kochurova, Galina V. Kopylova, D. V. Shchepkin, S. R. Nabiev |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Gene isoform Contraction (grammar) Swine Heart Ventricles Biophysics Motility macromolecular substances Myosins Biochemistry 03 medical and health sciences 0302 clinical medicine Myosin medicine Animals Urea Heart Atria Protein Interaction Maps Molecular Biology Actin Chemistry Cell Biology Myocardial Contraction Actins Omecamtiv mecarbil 030104 developmental biology medicine.anatomical_structure Ventricle 030220 oncology & carcinogenesis cardiovascular system Molecular mechanism |
| Zdroj: | Biochemical and biophysical research communications. 528(4) |
| ISSN: | 1090-2104 |
| Popis: | Omecamtiv mecarbil (OM), an activator of cardiac myosin, strongly affects contractile characteristics of the ventricles and, to a much lesser extent, the characteristics of atrial contraction. We compared the molecular mechanism of action of OM on the interaction of atrial and ventricular myosin with actin using an optical trap and an in vitro motility assay. In concentrations up to 0.5 μM, OM did not affect the step size of a myosin molecule but reduced it at a higher OM level. OM substantially prolonged the interaction of both isoforms of myosin with actin. However, the interaction characteristics of ventricular myosin with actin were more sensitive to OM than those of atrial myosin. Our results, obtained at the level of isolated proteins, can explain why the impact of OM in therapeutic concentrations on the contractile function of the atrium is less significant as compared to those of the ventricle. |
| Databáze: | OpenAIRE |
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