RESUMO
Myosins of fast and slow skeletal muscles differ by the isoform composition of the heavy and light chains. We compared functional characteristics of myosin from the fast (m. psoas) and slow (m. soleus) muscles of rabbits. The parameters of single actin-myosin interaction were measured in an optical trap, and the characteristics of the Ca2+ regulation of actin-myosin interaction were studied using an in vitro motility assay. The duration of interaction of myosin from the fast muscle with actin was shorter and the filament sliding velocity over this myosin was higher than the corresponding parameters for myosin from the slow muscle. The dependence pCa-velocity for myosin from the fast muscle was less sensitive to Ca2+ than that of slow muscle myosin. Thus, functional properties of myosin determine not only mechanical and kinetic characteristics of muscle contraction, but also the peculiarities of its Ca2+ regulation.
Assuntos
Fibras Musculares de Contração Rápida/metabolismo , Fibras Musculares de Contração Lenta/metabolismo , Miosinas/metabolismo , Actinas/metabolismo , Animais , Cálcio/metabolismo , Contração Muscular/fisiologia , Pinças Ópticas , CoelhosRESUMO
The results of the numerical simulation of the end-diastolic, end-systolic and stroke volumes of the left ventricle of the heart are presented. The simulation was based on a published simple kinetic model of cardiac muscle and approximation of the ventricle geometry with thick-wall cylinder where the fibre orientation varied linearly from sub-epicardium towards sub-endocardium. Blood flow was modelled with a liner compartment model. This simplified approach provides correct dependencies of the stroke volume on the pre- and afterload, namely end-diastolic pressure and peripheral resistance. The calculations show that the stroke volume is independent of arterial compliance and blood inertia.
Assuntos
Ventrículos do Coração/fisiopatologia , Modelos Teóricos , Pericárdio/fisiologia , Pressão Sanguínea/fisiologia , Hemodinâmica , Humanos , Contração Miocárdica/fisiologia , Volume Sistólico/fisiologiaRESUMO
The interaction of actin and myosin powers striated and smooth muscles and some other types of cell motility. Due to its highly ordered structure, skeletal muscle is a very convenient object for studying the general mechanism of the actin-myosin molecular motor. The history of investigation of the actin-myosin motor is briefly described. Modern concepts and data obtained with different techniques including protein crystallography, electron microscopy, biochemistry, and protein engineering are reviewed. Particular attention is given to X-ray diffraction studies of intact muscles and single muscle fibers with permeabilized membrane as they give insight into structural changes that underlie force generation and work production by the motor. Time-resolved low-angle X-ray diffraction on contracting muscle fibers using modern synchrotron radiation sources is used to follow movement of myosin heads with unique time and spatial resolution under near physiological conditions.