The effect of preload and Ca++-ions on the time-course of the isometric force and on the force-velocity relation: Is Vmax dependent on the number of activated cross-bridges?

1977 ◽  
pp. 10-16
Author(s):  
R. W. Gülch
Keyword(s):  
Time Course ◽  
Isometric Force ◽  
Velocity Relation ◽  
Ca Ions ◽  
Force Velocity ◽  
Cross Bridges

scholarly journals The effects of inorganic phosphate on muscle force development and energetics: challenges in modelling related to experimental uncertainties

2019 ◽  
Author(s):  
Alf Månsson
Keyword(s):  
Inorganic Phosphate ◽  
Muscle Force ◽  
Isometric Force ◽  
Shortening Velocity ◽  
Apparent Contradiction ◽  
Sequence Of Events ◽  
Velocity Relationship ◽  
Force Velocity ◽  
Cross Bridges ◽  
Experimental Findings

Abstract Muscle force and power are developed by myosin cross-bridges, which cyclically attach to actin, undergo a force-generating transition and detach under turnover of ATP. The force-generating transition is intimately associated with release of inorganic phosphate (Pi) but the exact sequence of events in relation to the actual Pi release step is controversial. Details of this process are reflected in the relationships between [Pi] and the developed force and shortening velocity. In order to account for these relationships, models have proposed branched kinetic pathways or loose coupling between biochemical and force-generating transitions. A key hypothesis underlying the present study is that such complexities are not required to explain changes in the force–velocity relationship and ATP turnover rate with altered [Pi]. We therefore set out to test if models without branched kinetic paths and Pi-release occurring before the main force-generating transition can account for effects of varied [Pi] (0.1–25 mM). The models tested, one assuming either linear or non-linear cross-bridge elasticity, account well for critical aspects of muscle contraction at 0.5 mM Pi but their capacity to account for the maximum power output vary. We find that the models, within experimental uncertainties, account for the relationship between [Pi] and isometric force as well as between [Pi] and the velocity of shortening at low loads. However, in apparent contradiction with available experimental findings, the tested models produce an anomalous force–velocity relationship at elevated [Pi] and high loads with more than one possible velocity for a given load. Nevertheless, considering experimental uncertainties and effects of sarcomere non-uniformities, these discrepancies are insufficient to refute the tested models in favour of more complex alternatives.

Effect of hindlimb unloading on rat soleus fiber force, stiffness, and calcium sensitivity

1995 ◽  
Vol 79 (5) ◽  
pp. 1796-1802 ◽  
Author(s):  
K. S. McDonald ◽  
R. H. Fitts
Keyword(s):  
Time Course ◽  
Fiber Diameter ◽  
Isometric Force ◽  
Calcium Sensitivity ◽  
Cross Sectional Area ◽  
Hindlimb Unloading ◽  
Sectional Area ◽  
Cross Sectional ◽  
Control Value ◽  
Cross Bridges

The purpose of this study was to examine the time course of change in soleus muscle fiber peak force (N), tension (Po, kN/m2), elastic modulus (Eo), and force-pCa and stiffness-pCa relationships. After 1, 2, or 3 wk of hindlimb unloading (HU), single fibers were isolated and placed between a motor arm and a transducer, and fiber diameter, peak absolute force, Po, Eo, and force-pCa and stiffness-pCa relationships were characterized. One week of HU resulted in a significant reduction in fiber diameter (68 +/- 2 vs 57 +/- 1 microns), force (3.59 +/- 0.15 vs. 2.19 +/- 0.12 x 10(-4) N), Po (102 +/- 4 vs. 85 +/- 2 kN/m2), and Eo (1.96 +/- 0.12 vs. 1.37 +/- 0.13 x 10(7) N/m2), and 2 wk of HU caused a further decline in fiber diameter (45 +/- 1 microns), force (1.31 +/- 0.06 x 10(-4) N), and Eo (0.96 +/- 0.09 x 10(7) N/m2). Although the mean fiber diameter and absolute force continued to decline through 3 wk of HU, Po recovered to values not significantly different from control. The Po/Eo ratio was significantly increased after 1 (5.5 +/- 0.3 to 7.1 +/- 0.6), 2, and 3 wk of HU, and the 2-wk (9.5 +/- 0.4) and 3-wk (9.4 +/- 0.8) values were significantly greater than the 1-wk values. The force-pCa and stiffness-pCa curves were shifted rightward after 1, 2, and 3 wk of HU. At 1 wk of HU, the Ca2+ sensitivity of isometric force, assessed by Ca2+ concentration required for half-maximal force, was increased from the control value of 1.83 +/- 0.12 to 2.30 +/- 0.10 microM. In conclusion, after HU, the decrease in soleus fiber Po can be explained by a reduction in the number of myofibrillar cross bridges per cross-sectional area. Our working hypothesis is that the loss of contractile protein reduces the number of cross bridges per cross-sectional area and increases the filament lattice spacing. The increased spacing reduces cross-bridge force and stiffness, but Po/Eo increases because of a quantitatively greater effect on stiffness.

The biophysics and biochemistry of smooth muscle contraction

1992 ◽  
Vol 70 (4) ◽  
pp. 515-531 ◽  
Author(s):  
N. L. Stephens ◽  
C. Y. Seow ◽  
A. J. Halayko ◽  
H. Jiang
Keyword(s):  
Smooth Muscle ◽  
Muscle Contraction ◽  
Light Chain ◽  
Time Course ◽  
Myosin Light Chain ◽  
Isometric Force ◽  
Smooth Muscle Contraction ◽  
Cytoskeletal Proteins ◽  
Contractile Element ◽  
Force Velocity

In this review the biophysics and biochemistry of smooth muscle contraction are dealt with. We describe a new model for the study of bronchial smooth muscle, which facilitates study of cellular contractile mechanisms. A new concept emerging is that study of steady-state mechanical parameters such as maximal isometric force (Po) velocity is inadequate because two types of crossbridges (normally cycling (NBR) and latch) seem to be sequentially active during smooth muscle contraction. Thus quick-release techniques are required to characterize the force–velocity properties of the two types of bridges. Pathophysiological processes that affect the muscle's shortening ability seem to affect the early NBRs only. With respect to maximal shortening capacity of the smooth muscle, the role of loading is very important. The differences between isotonic, elastic, and viscous loading are considerable. Ultimately, the time course and magnitude of loading should exactly resemble that operative in vivo. Once again, it is the characteristic of loading in the early phase of contraction that is crucial, as most of the shortening in smooth muscle occurs early in the contraction. While the maximum force developed by smooth muscle per unit cross-sectional area is the same as for striated muscle, the velocity is 50 times less. The properties of the series and parallel elastic elements of smooth muscle are described. The latter, when in compression mode, acts as an internal resistance to shortening and probably limits it. Isotonic relaxation has therefore not been studied in smooth muscle. We have developed a shortening parameter that is independent of the load on the muscle and of the initial length of the muscle's contractile element. We report the novel observation that isotonically relaxing smooth muscle reactivates itself, resulting in terminal slowing of the relaxation process. With respect to the biochemistry of smooth muscle contraction, contractile (actin isoforms, myosin heavy and light chains and their isoforms), regulatory (calmodulin–4 Ca2+, myosin light chain kinase, myosin light chain and its phosphorylation, tropomyosin, caldesmon, and calponin), and cytoskeletal (chiefly desmin and vimentin) proteins are discussed. While the kinase activates the contractile system, caldesmon and calponin modulate the activity downward. The cytoskeletal proteins desmin, vimentin, and α-actinin could constitute the muscle cell's internal resistor.Key words: smooth muscle mechanics, force–velocity, smooth muscle, internal resistor, smooth muscle retardation, contractile proteins, regulatory proteins.

Oxytocin-mediated recruitment of slowly cycling cross bridges and isometric force in rat myometrium

1996 ◽  
Vol 270 (2) ◽  
pp. E203-E208
Author(s):  
A. L. Ruzycky ◽  
B. T. Ameredes
Keyword(s):  
Isometric Force ◽  
Additional Stress ◽  
Shortening Velocity ◽  
Cycling Rate ◽  
Quick Release ◽  
Cross Bridge ◽  
Cross Bridges ◽  
Unit Stress ◽  
Release Method ◽  
The Relationship

The relationship between cross-bridge cycling rate and isometric stress was investigated in rat myometrium. Stress production by myometrial strips was measured under resting, K+ depolarization, and oxytocin-stimulated conditions. Cross-bridge cycling rates were determined from measurements of maximal unloaded shortening velocity, using the quick-release method. Force redevelopment after the quick release was used as an index of cross-bridge attachment. With maximal K+ stimulation, stress increased with increased cross-bridge cycling (+76%; P < 0.05) and attached cross bridges (+112%; P < 0.05). Addition of oxytocin during K+ stimulation further increased stress (+30%; P < 0.05). With this force component, the cross-bridge cycling rate decreased (-60%; P < 0.05) similar to that under resting conditions. Attached cross-bridges did not increase with this additional stress. The results suggest two distinct mechanisms mediating myometrial contractions. One requires elevated intracellular calcium and rapidly cycling cross bridges. The other mechanism may be independent of calcium and appears to be mediated by slowly cycling cross bridges, supporting greater unit stress.

Scientific contributions of A. V. Hill: exercise physiology pioneer

2002 ◽  
Vol 93 (5) ◽  
pp. 1567-1582 ◽  
Author(s):  
David R. Bassett
Keyword(s):  
World War Ii ◽  
Heat Production ◽  
Time Course ◽  
Exercise Physiology ◽  
Frog Muscle ◽  
World War ◽  
Academic Assistance ◽  
Physiological Adaptations ◽  
Velocity Equation ◽  
Force Velocity

Beginning in 1910, A. V. Hill performed careful experiments on the time course of heat production in isolated frog muscle. His research paralleled that of the German biochemist Otto Meyerhof, who measured the changes in muscle glycogen and lactate during contractions and recovery. For their work in discovering the distinction between aerobic and anaerobic metabolism, Hill and Meyerhof were jointly awarded the 1922 Nobel Prize for Physiology or Medicine. Because of Hill's interest in athletics, he sought to apply the concepts discovered in isolated frog muscle to the exercising human. Hill and his colleagues made measurements of O2 consumption on themselves and other subjects running around an 85-m grass track. In the process of this work, they defined the terms “maximum O2 intake,” “O2requirement,” and “steady state of exercise.” Other contributions of Hill include his discoveries of heat production in nerve, the series elastic component, and the force-velocity equation in muscle. Around the time of World War II, Hill was a leading figure in the Academic Assistance Council, which helped Jewish scientists fleeing Nazi Germany to relocate in the West. He served as a member of the British Parliament from 1940 to 1945 and as a scientific advisor to India. Hill's vision and enthusiasm attracted many scientists to the field of exercise physiology, and he pointed the way toward many of the physiological adaptations that occur with physical training.

Force-velocity and force-power properties of single muscle fibers from elite master runners and sedentary men

1996 ◽  
Vol 271 (2) ◽  
pp. C676-C683 ◽  
Author(s):  
J. J. Widrick ◽  
S. W. Trappe ◽  
D. L. Costill ◽  
R. H. Fitts
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Power Output ◽  
Peak Power ◽  
Isometric Force ◽  
Peak Force ◽  
Peak Power Output ◽  
Type I ◽  
Shortening Velocity ◽  
Force Velocity

Gastrocnemius muscle fiber bundles were obtained by needle biopsy from five middle-aged sedentary men (SED group) and six age-matched endurance-trained master runners (RUN group). A single chemically permeabilized fiber segment was mounted between a force transducer and a position motor, subjected to a series of isotonic contractions at maximal Ca2+ activation (15 degrees C), and subsequently run on a 5% polyacrylamide gel to determine myosin heavy chain composition. The Hill equation was fit to the data obtained for each individual fiber (r2 > or = 0.98). For the SED group, fiber force-velocity parameters varied (P < 0.05) with fiber myosin heavy chain expression as follows: peak force, no differences: peak tension (force/fiber cross-sectional area), type IIx > type IIa > type I; maximal shortening velocity (Vmax, defined as y-intercept of force-velocity relationship), type IIx = type IIa > type I; a/Pzero (where a is a constant with dimensions of force and Pzero is peak isometric force), type IIx > type IIa > type I. Consequently, type IIx fibers produced twice as much peak power as type IIa fibers, whereas type IIa fibers produced about five times more peak power than type I fibers. RUN type I and IIa fibers were smaller in diameter and produced less peak force than SED type I and IIa fibers. The absolute peak power output of RUN type I and IIa fibers was 13 and 27% less, respectively, than peak power of similarly typed SED fibers. However, type I and IIa Vmax and a/Pzero were not different between the SED and RUN groups, and RUN type I and IIa power deficits disappeared after power was normalized for differences in fiber diameter. Thus the reduced absolute peak power output of the type I and IIa fibers from the master runners was a result of the smaller diameter of these fibers and a corresponding reduction in their peak isometric force production. This impairment in absolute peak power production at the single fiber level may be in part responsible for the reduced in vivo power output previously observed for endurance-trained athletes.

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