Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Papillary muscle mechanics and ventricular myosin calcium-activated ATPase activity were measured in the same heart as a function of temperature (8--28 degrees) in rabbits and marmots, in order to examine further the hypothesis that the velocity of cardiac muscle shortening at zero load (Vmax) is correlated with myosin ATPase activity. There was a similar Q10 for Vmax in each muscle type, as measured with isotonic afterloaded quick-releases at 30--33% time-to-peak tension; the calcium activated ATPase of myosin in the two muscle types also was similar. The least squares linear regression of rabbit Vmax on calcium-activated myosin ATPase activity was the same as in the marmot, so all the data were pooled to yield a linear regression (Y = 0.47 +/- 3.82X) with a high correlation between the two variables [r = 0.95, P less than 0.01 (ANOV)]. Furthermore, the correlation proved to be predictive of cardiac Vmax and myosin ATPase activity levels in other experiments where these two measurements decreased below normal as a result of hypertrophic growth. Consequently, the quantitative relationship between Vmax and myosin ATPase defined here may prove to be predictive of the ability of cardiac muscle to release bond energy.
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PMID:The relationship of mechanical Vmax to myosin ATPase activity in rabbit and marmot ventricular muscle. 15 23

The effect of temperature on the force-sarcomere velocity relation (20 degrees, 25 degrees, and 30 degrees C) and maximum velocity of sarcomere shortening (Vo; range 15 degrees-35 degrees C) was studied in trabeculae from rat heart. Sarcomere length and Vo were measured by laser diffraction techniques. Sarcomere length and sarcomere velocity, determined from each of the first-order diffraction lines, differed by less than 4%. Slack sarcomere length in the trabeculae appeared to be 1.9 microns. Isovelocity release techniques were used to obtain sarcomere velocity and Vo directly. Sarcomere velocity was measured at SL = 1.9-2.0 microns for elimination of contributions of parallel elastic force and restoring force to the external load of the sarcomeres. Peak twitch force development (Fo) was maximal (Fo-max) at 25 degrees C at [Ca2+]o = 1.5 mM. Lowering of the temperature below 25 degrees C led to development of spontaneous sarcomere activity and depression of Fo; both responses could be prevented by the addition of 0.5 mM procaine. Increase of temperature above 25 degrees C reduced twitch duration and Fo. Hill's rectangular hyperbola fitted the force-velocity data if the load during shortening was less than 70% of Fo. Vo appeared to be independent of the level of activation at all temperatures when Fo was maintained above 90% of Fo-max, either by an increase of [Ca2+]o (to 3.0 mM) or by paired pulse stimulation. Vo increased with increasing temperature; the parameter a, calculated from force-velocity relations measured at 20 degrees, 25 degrees, and 30 degrees C, decreased with increasing temperature. The Arrhenius plot of Vo was studied in detail over a wider temperature range (15 degrees-35 degrees C) and in smaller temperature increments. The relation was linear between 18 degrees and 33 degrees C; the observed Q10, defined as the ratio of Vo measured at temperature (T) over Vo at T-10 degrees C, was 4.6 A Q10 of 4.6 for Vo is consistent with the reported temperature dependence of rat cardiac actin-activated myosin ATPase, which suggests that the same reaction step may limit the activity of the enzyme in vitro and during shortening of the cardiac sarcomeres at zero external load.
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PMID:Force and velocity of sarcomere shortening in trabeculae from rat heart. Effects of temperature. 233 24

The dynamic stiffness of excised cardiac muscles that would be likely to have different intrinsic speeds of contraction, as judged by previous biochemical reports of their myosin ATPase rates, was compared. This study included muscles from thyrotoxic rabbits and newborn rabbits, rabbit atria, and normal papillary muscles at different temperatures. The usual excitation-contraction coupling process was bypassed by replacing bathing Ca2+ with Ba2+. The ensuring actively maintained contracture allowed us to focus more specifically on the contractile properties of the myofilaments. Dynamic stiffness was determined by sinusoidally oscillating muscle length at many different frequencies over the range 0.05-50 Hz while holding average muscle length at 95% of the systolic length, thus giving maximal developed force. The form of the stiffness modulus spectrum was similar for all muscles studied: stiffness was fairly constant at low frequencies, decreased to a minimum at an intermediate frequency, and then increased steeply, followed by a milder rate of increase over high frequencies. Differences in contraction speed were evident by shifts in the frequencies at which corresponding portions of the stiffness spectrum appeared. The clearest landmark was the frequency where stiffness became minimum (fmin). This varied strongly with temperature (Q10 = 2.9). Compared to normal adult papillary muscles (fmin = 1.2 Hz), fmin was 2.2 times faster in thyrotoxic myocardium, 1.9 times faster in 1-week-old rabbits, and 3.7 times faster in atrial trabeculae. These ratios of functional speed are similar to the corresponding ratios of myosin Ca2+-ATPase activities reported in the literature.
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PMID:Dynamic stiffness of barium-contractured cardiac muscles with different speeds of contraction. 295 19

We studied the effects of cardiac cooling by 7 +/- 2 degrees C (SD) from 36 degrees C on both contractility index (Emax) and the relation between O2 consumption per beat (VO2) and systolic pressure-volume area (PVA) of the left ventricle in the excised cross-circulated dog heart preparation. PVA represents the total mechanical energy generated by a contraction. The VO2-PVA relation divides measured VO2 into unloaded VO2 and excess VO2. The slope of the VO2-PVA relation represents inversely the efficiency of the contractile machinery to convert chemical energy from the excess VO2 to total mechanical energy. Cooling is known to decrease myosin ATPase activity (Q10 of 2-3), which in turn is expected to increase the chemomechanical efficiency of cross bridges. Therefore, we expected an increase in the efficiency and hence a decreased slope of the VO2-PVA relation with cooling. The cooling increased Emax by 46 +/- 13% and the time to Emax by 45 +/- 27%. Pacing rate was constant or had to be slightly decreased to avoid arrhythmias with cooling. We found that neither the slope of the VO2-PVA relation nor unloaded VO2 significantly (p greater than 0.05) changed with the cooling. This result contradicts the expected increase in the efficiency with cooling. We conclude that cardiac cooling by 7 degrees C from 36 degrees C does not increase the efficiency of the contractile machinery in excised cross-circulated dog left ventricle.
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PMID:Cardiac cooling increases Emax without affecting relation between O2 consumption and systolic pressure-volume area in dog left ventricle. 338 83

We examined the tension change induced by a rapid temperature jump (T-jump) in shortening and lengthening active muscle fibres. Experiments were done on segments of permeabilized single fibres (length (L0) approximately 2 mm, sarcomere length 2.5 microm) from rabbit psoas muscle; [MgATP] was 4.6 mm, pH 7.1, ionic strength 200 mm and temperature approximately 9 degrees C. A fibre was maximally Ca2+-activated in the isometric state and a approximately 3 degrees C, rapid (< 0.2 ms), laser T-jump applied when the tension was approximately steady in the isometric state, or during ramp shortening or ramp lengthening at a limited range of velocities (0-0.2 L0 s(-1)). The tension increased to 2- to 3 x P0 (isometric force) during ramp lengthening at velocities > 0.05 L0 s(-1), whereas the tension decreased to about < 0.5 x P0 during shortening at 0.1-0.2 L0 s(-1); the unloaded shortening velocity was approximately 1 L0 s(-1) and the curvature of the force-shortening velocity relation was high (a/P0 ratio from Hill's equation of approximately 0.05). In isometric state, a T-jump induced a tension rise of 15-20% to a new steady state; by curve fitting, the tension rise could be resolved into a fast (phase 2b, 40-50 s(-1)) and a slow (phase 3, 5-10 s(-1)) exponential component (as previously reported). During steady lengthening, a T-jump induced a small instantaneous drop in tension, followed by recovery, so that the final tension recorded with and without a T-jump was not significantly different; thus, a T-jump did not lead to a net increase of tension. During steady shortening, the T-jump induced a pronounced tension rise and both its amplitude and the rate (from a single exponential fit) increased with shortening velocity; at 0.1-0.2 L0 s(-1), the extent of fibre shortening during the T-jump tension rise was estimated to be approximately 1.2% L(0) and it was shorter at lower velocities. At a given shortening velocity and over the temperature range of 8-30 degrees C, the rate of T-jump tension rise increased with warming (Q10 approximately 2.7), similar to phase 2b (endothermic force generation) in isometric muscle. Results are discussed in relation to the previous findings in isometric muscle fibres which showed that a T-jump promotes an early step in the crossbridge-ATPase cycle that generates force. In general, the finding that the T-jump effect on active muscle tension is pronounced during shortening, but is depressed/inhibited during lengthening, is consistent with the expectations from the Fenn effect that energy liberation (and acto-myosin ATPase rate) in muscle are increased during shortening and depressed/inhibited during lengthening.
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PMID:Force generation examined by laser temperature-jumps in shortening and lengthening mammalian (rabbit psoas) muscle fibres. 1791 9