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Maximum speed of shortening and ATPase activity in atrial and ventricular myocardia of hyperthyroid rats
No full textThe kinetic properties of the myofibrillar system of atrial and ventricular myocardia of hyperthyroid rats were analyzed by determining ATPase activity and maximum shortening velocity. Hyperthyroidism was induced by daily subcutaneous injections of triiodothyronine (0.2 mg/kg body wt) for 2 wk. The treatment induced a marked atrial and ventricular hypertrophy and, in ventricular myocardium, an isomyosin shift toward a homogeneous V1 composition. Skinned trabeculae and purified myofibrils were prepared from atrial and ventricular myocardia. Enzymatic assays on the myofibrils showed that both Ca-stimulated ATPase activity and Ca-Mg-dependent ATPase activity had equal values in atrial and ventricular myocardia. In skinned trabeculae during maximal Ca activations, force-velocity curves were determined by load-clamp maneuvers, and unloaded shortening velocity (Vo) was obtained with the slack-test method. Both maximum shortening velocities extrapolated from the force-velocity curves (Vmax) and Vo were significantly higher (+68 and +52%, respectively) in atrial than in ventricular preparations. Developed tension was significantly greater in ventricular preparations. Maximum power output was not significantly different. Previous findings (V. Cappelli, R. Bottinelli, C. Poggesi, R. Moggio, and C. Reggiani. Circ. Res. 65: 446-457, 1989) had led to the conclusion that variations in ATPase activity and shortening velocity of ventricular myocardium can be accounted for by changes in isomyosin composition. In this light, the present results suggest that 1) ATPase activity is equal in atrial and ventricular myocardia as the two tissues contain the same myosin heavy chain isoform, 2) the difference in maximum speed of shortening between atrium and ventricle might be due to the presence of tissue-specific isoforms of myosin light chains
ADP Modulation of actin sliding velocity on slow and fast skeletal myosin isoforms at different temperatures
No full textEffect of propionyl-L-carnitine (PLC) on the kinetic properties of the myofibrillar system in pressure overload cardiac hypertrophy.
No full textForce-velocity properties of human skeletal muscle fibres: myosin heavy chain isoform and temperature dependence
No full text1. A large population (n = 151) of human skinned skeletal muscle fibres has been studied. Force-velocity curves of sixty-seven fibres were obtained by load-clamp manoeuvres at 12 degrees C. In each fibre maximum shortening velocity (Vmax), maximum power output (Wmax), optimal velocity (velocity at which Wmax is developed, Vopt), optimal force (force at which Wmax is developed, Popt), specific tension (Po/CSA, isometric tension/cross-sectional area) were assessed. Unloaded shortening velocity (Vo) was also determined at 12 degrees C in a different group (n = 57) of fibres by slack-test procedure. 2. All fibres used for mechanical experiments were characterized on the basis of the myosin heavy chain (MHC) isoform composition by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis and divided into five types: type I (or slow), types IIA and IIB (or fast), and types I-IIA and IIA-IIB (or mixed types). 3. Vmax, Wmax, Vopt, Popt, Vopt/Vmax ratio, Po/CSA and Vo were found to depend on MHC isoform composition. All parameters were significantly lower in type I than in the fast (type IIA and IIB) fibres. Among fast fibres, Vmax, Wmax, Vopt and Vo were significantly lower in type IIA and than in IIB fibres, whereas Popt, Po/CSA and Vopt/Vmax were similar. 4. The temperature dependence of Vo and Po/CSA was assessed in a group of twenty-one fibres in the range 12-22 degrees C. In a set of six fibres temperature dependence of Vmax was also studied. The Q10 (5.88) and activation energy E (125 kJ mol-1) values for maximum shortening velocity calculated from Arrhenius plots pointed to a very high temperature sensitivity. Po/CSA was very temperature dependent in the 12-17 degrees C range, but less dependent between 17 and 22 degrees C
Single muscle fiber properties in aging and disuse
No full textSince the middle of the 1980s, it was understood that myosin, the motor of contraction, can be expressed in several isoforms. The isoforms of the myosin heavy-chain (MHC) portion of the molecule were found to be mostly responsible for the diversity in the contractile and energetic properties of muscle fibers. In humans, three MHC isoforms are expressed in limb muscles (MHC-1, MHC-2A and MHC-2X) and they generate three pure fiber types (types 1, 2A and 2X) and two hybrid types (types 1-2A and -2AX). Type 1, 2A and 2X fibers widely differ with respect to most of their contractile and energetic properties, and a change in their relative distribution within muscles is known to modulate their functional properties in vivo through a "qualitative" mechanism. On the basis of the MHC regulation of muscle fibers properties, it is expected that a given fiber type develops the same force and shortens at the same speed regardless of the physiologic and pathologic conditions under which the muscle works. Surprisingly, several evidences have been accumulating to show that in aging and disuse, the properties of a muscle fiber type can change with no change in its myosin isoform content. This short review considers the latter phenomenon and the possible underlying mechanisms
Temperature dependence of speed of actin filaments (Vf) propelled by different skeletal myosin isoforms
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Direct depressant effect of phosphodiesterase inhibitors on ATPase activity of rat cardiac myofibrils
No full textThe aim of this study was to determine (i) whether phosphodiesterase inhibitors influenced ATPase activity of maximally calcium activated cardiac myofibrils and (ii) whether this effect varied in relation to isomyosin composition. Myofibrils were prepared from ventricular myocardium of 2- to 3-month-old rats. ATPase activity was determined at low ionic strength at high (> 7.5) and low (4.4) pCa. Five compounds (amrinone, milrinone, enoximone, piroximone, and rolipram) were examined at concentrations between 10 microM and 1 mM. The results obtained showed that only milrinone and amrinone inhibited ATPase activity; inhibition was dose dependent, and milrinone was more potent than amrinone. To assess whether isomyosin composition might influence the responsiveness of myofibrils to phosphodiesterase inhibitors, the effect of 1 mM milrinone was also determined in myofibrils from hypothyroid rats. According to previous observations hypothyroidism caused an isomyosin shift from V1 to V3 in rat ventricular myocardium. The inhibitory effect of milrinone was lower in myofibrils prepared from hypothyroid rats than in myofibrils from euthyroid rats
Effects of acidosis on maximum shortening velocity and force-velocity relation of skinned rat cardiac muscle.
No full textThis study was designed to assess whether maximum shortening velocity and force-velocity parameters were reduced by acidosis in rat skinned cardiac trabeculae, as reported for skinned skeletal muscle. Thin trabeculae were dissected from right ventricle of adult male Wistar rats, chemically skinned, and maximally Ca-activated at pH 7.0, 6.6 and 6.2. Maximum tension (Po), maximum shortening velocity evaluated from force-velocity curves (Vmax), and maximum power output (Wmax) were significantly reduced for exposure to pH 6.6 and 6.2. When the value at pH 7.0 is taken as reference, Po decreased by 30\% and 49\%, Vmax by 17\% and 40\% and Wmax by 30\% and 60\% at pH 6.6 and 6.2 respectively. A similar reduction (25\% at pH 6.6 and 42\% and pH 6.2) was observed when unloaded shortening velocity (Vo) was determined with the slack test method. The results obtained show that both Po and Vmax or Vo are affected by a substantial decrease in pH. The combination between significantly lower Po and Vmax gives rise to significantly lower Wmax. The reduction of maximum shortening velocity (Vmax or Vo) can be explained by assuming either the existence of an internal load or an impairment in actin-myosin interaction
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