scholarly journals ATPase Activity of Myosin Correlated with Speed of Muscle Shortening

1967 ◽  
Vol 50 (6) ◽  
pp. 197-218 ◽  
Author(s):  
Michael Bárány
Keyword(s):  
Atpase Activity ◽  
Myosin Atpase ◽  
Actin Binding ◽  
Contraction Time ◽  
Lower Vertebrates ◽  
Maximal Speed ◽  
Series Of Experiments ◽  
Isometric Twitch ◽  
Q10 Values ◽  
Speed Of Shortening

Myosin was isolated from 14 different muscles (mammals, lower vertebrates, and invertebrates) of known maximal speed of shortening. These myosin preparations were homogeneous in the analytical ultracentrifuge or, in a few cases, showed, in addition to the main myosin peak, part of the myosin in aggregated form. Actin- and Ca++-activated ATPase activities of the myosins were generally proportional to the speed of shortening of their respective muscles; i.e. the greater the intrinsic speed, the higher the ATPase activity. This relation was found when the speed of shortening ranged from 0.1 to 24 muscle lengths/sec. The temperature coefficient of the Ca++-activated myosin ATPase was the same as that of the speed of shortening, Q10 about 2. Higher Q10 values were found for the actin-activated myosin ATPase, especially below 10°C. By using myofibrils instead of reconstituted actomyosin, Q10 values close to 2 could be obtained for the Mg++-activated myofibrillar ATPase at ionic strength of 0.014. In another series of experiments, myosin was isolated from 11 different muscles of known isometric twitch contraction time. The ATPase activity of these myosins was inversely proportional to the contraction time of the muscles. These results suggest a role for the ATPase activity of myosin in determining the speed of muscle contraction. In contrast to the ATPase activity of myosin, which varied according to the speed of contraction, the F-actin-binding ability of myosin from various muscles was rather constant.

Maximum shortening speed of motor units of various types in cat lumbrical muscles

1993 ◽  
Vol 69 (2) ◽  
pp. 442-448 ◽  
Author(s):  
J. Petit ◽  
M. Chua ◽  
C. C. Hunt
Keyword(s):  
Motor Unit ◽  
Inverse Correlation ◽  
Motor Units ◽  
Maximum Speed ◽  
Single Motor Units ◽  
Maximal Speed ◽  
Contraction Times ◽  
Isometric Twitch ◽  
Lumbrical Muscles ◽  
Speed Of Shortening

1. Isotonic shortening of cat superficial lumbrical muscles was studied during maximal tetanic contractions of single motor units of identified types. For each motor unit, the maximal speed of contraction, Vmax, was determined by extrapolating to zero the hyperbolic relation between applied tension and speed of shortening. 2. The maximal speeds of shortening of motor units formed a continuum with the highest velocities observed for the fast fatigable motor units and the lowest for the slow motor units. 3. On average, the maximum speed of shortening increased with the tetanic tension developed by the motor units. 4. In motor units with isometric twitch contraction times less than 35 ms, these times showed a significant inverse correlation with Vmax. Progressively longer contraction times were associated with rather small changes in Vmax. 5. The implications of these findings on the speed of muscle shortening during motor-unit recruitment are discussed.

Uncoupling of actin-activated myosin ATPase activity from actin binding by a monoclonal antibody directed against the N-terminus of myosin light chain 1

Biochemistry ◽  
1992 ◽  
Vol 31 (16) ◽  
pp. 4090-4095 ◽  
Author(s):  
Wylinn Boey ◽  
Alan W. Everett ◽  
John Sleep ◽  
John Kendrick-Jones ◽  
Cristobal G. Dos Remedios
Keyword(s):  
Monoclonal Antibody ◽  
Atpase Activity ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Myosin Atpase ◽  
Actin Binding ◽  
Myosin Atpase Activity ◽  
N Terminus

Isometric contractile properties and velocity of shortening during avian myogenesis

1982 ◽  
Vol 243 (3) ◽  
pp. C177-C183 ◽  
Author(s):  
P. J. Reiser ◽  
B. T. Stokes ◽  
J. A. Rall
Keyword(s):  
Atpase Activity ◽  
Myosin Atpase ◽  
Contractile Properties ◽  
In Ovo ◽  
Tetanic Force ◽  
Time To Peak ◽  
Myosin Atpase Activity ◽  
Velocity Of Shortening ◽  
Isometric Twitch ◽  
Force Time

Isometric twitch and tetanic contractile properties and velocity of unloaded shortening (V0) of whole avian posterior latissimus dorsi muscle (PLD) were examined between embryonic day 15 and the first 2 wk after hatching. The time to peak twitch force, time to half-relaxation of the twitch response, and time to half-peak tetanic force all change significantly during the final week in ovo but do not change during the first 2 wk ex ovo. Comparisons with previously published reports by others indicate that the twitch half-relaxation time at hatching is approximately the same as that of the adult PLD. The velocity of unloaded shortening increases 2.3-fold during the period studied. It has previously been shown by other that the velocity of shortening is well correlated with a muscle's myosin ATPase activity. Therefore, the observed changes in V0 suggest that the myosin ATPase activity of the avian PLD increases between embryonic day 15 and the first 2 wk posthatching, and this change could account, at least in part, for some of the changes in the isometric properties that were measured.

scholarly journals Inhibition of acanthamoeba actomyosin-II ATPase activity and mechanochemical function by specific monoclonal antibodies.

1984 ◽  
Vol 99 (3) ◽  
pp. 1024-1033 ◽  
Author(s):  
D P Kiehart ◽  
T D Pollard
Keyword(s):  
Monoclonal Antibodies ◽  
Atpase Activity ◽  
Conformational Changes ◽  
Binding Sites ◽  
Polyclonal Antibodies ◽  
Myosin Ii ◽  
Antigenic Site ◽  
Actin Binding ◽  
Filamentous Form ◽  
Antibody Effects

Monoclonal and polyclonal antibodies that bind to myosin-II were tested for their ability to inhibit myosin ATPase activity, actomyosin ATPase activity, and contraction of cytoplasmic extracts. Numerous antibodies specifically inhibit the actin activated Mg++-ATPase activity of myosin-II in a dose-dependent fashion, but none blocked the ATPase activity of myosin alone. Control antibodies that do not bind to myosin-II and several specific antibodies that do bind have no effect on the actomyosin-II ATPase activity. In most cases, the saturation of a single antigenic site on the myosin-II heavy chain is sufficient for maximal inhibition of function. Numerous monoclonal antibodies also block the contraction of gelled extracts of Acanthamoeba cytoplasm. No polyclonal antibodies tested inhibited ATPase activity or gel contraction. As expected, most antibodies that block actin-activated ATPase activity also block gel contraction. Exceptions were three antibodies M2.2, -15, and -17, that appear to uncouple the ATPase activity from gel contraction: they block gel contraction without influencing ATPase activity. The mechanisms of inhibition of myosin function depends on the location of the antibody-binding sites. Those inhibitory antibodies that bind to the myosin-II heads presumably block actin binding or essential conformational changes in the myosin heads. A subset of the antibodies that bind to the proximal end of the myosin-II tail inhibit actomyosin-II ATPase activity and gel contraction. Although this part of the molecule is presumably some distance from the ATP and actin-binding sites, these antibody effects suggest that structural domains in this region are directly involved with or coupled to catalysis and energy transduction. A subset of the antibodies that bind to the tip of the myosin-II tail appear to inhibit ATPase activity and contraction through their inhibition of filament formation. They provide strong evidence for a substantial enhancement of the ATPase activity of myosin molecules in filamentous form and suggest that the myosin filaments may be required for cell motility.

Alterations in diaphragm contractility after nandrolone administration: an analysis of potential mechanisms

1999 ◽  
Vol 86 (3) ◽  
pp. 985-992 ◽  
Author(s):  
Michael I. Lewis ◽  
Mario Fournier ◽  
Amelia Y. Yeh ◽  
Paul E. Micevych ◽  
Gary C. Sieck
Keyword(s):  
Atpase Activity ◽  
Maximum Velocity ◽  
Interstitial Space ◽  
Myosin Atpase ◽  
Fiber Types ◽  
Intact Male ◽  
Cross Sectional ◽  
Myosin Atpase Activity ◽  
Relative Contribution

The aim of this study was to evaluate the potential mechanisms underlying the improved contractility of the diaphragm (Dia) in adult intact male hamsters after nandrolone (Nan) administration, given subcutaneously over 4 wk via a controlled-release capsule (initial dose: 4.5 mg ⋅ kg−1 ⋅ day−1; with weight gain, final dose: 2.7 mg ⋅ kg−1 ⋅ day−1). Control (Ctl) animals received blank capsules. Isometric contractile properties of the Dia were determined in vitro after 4 wk. The maximum velocity of unloaded shortening ( V o) was determined in vitro by means of the slack test. Dia fibers were classified histochemically on the basis of myofibrillar ATPase staining and fiber cross-sectional area (CSA), and the relative interstitial space was quantitated. Ca2+-activated myosin ATPase activity was determined by quantitative histochemistry in individual diaphragm fibers. Myosin heavy chain (MHC) isoforms were identified electrophoretically, and their proportions were determined by using scanning densitometry. Peak twitch and tetanic forces, as well as V o, were significantly greater in Nan animals compared with Ctl. The proportion of type IIa Dia fibers was significantly increased in Nan animals. Nan increased the CSA of all fiber types (26–47%), whereas the relative interstitial space decreased. The relative contribution of fiber types to total costal Dia area was preserved between the groups. Proportions of MHC isoforms were similar between the groups. There was a tendency for increased expression of MHC2B with Nan. Ca2+-activated myosin ATPase activity was increased 35–39% in all fiber types in Nan animals. We conclude that, after Nan administration, the increase in Dia specific force results from the relatively greater Dia CSA occupied by hypertrophied muscle fibers, whereas the increased ATPase activity promotes a higher rate of cross-bridge turnover and thus increased V o. We speculate that Nan in supraphysiological doses have the potential to offset or ameliorate conditions associated with enhanced proteolysis and disordered protein turnover.

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