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1.
The interaction between contractile force and in-series compliance was investigated for the intact skeletal muscle-tendon unit (MTU) of Rana pipiens semitendinosus muscles during fixed-end contraction. It was hypothesized that internal sarcomere shortening is a function of the length-force characteristics of contractile and series elastic components. The MTUs (n=18) were dissected, and, while submerged in Ringer's solution, muscles were activated at nine muscle lengths (-2 to +6 mm relative to optimal length in 1 mm intervals), while measuring muscle force and sarcomere length (SL) by laser diffraction. The MTU was clamped either at the bone (n=6), or at the proximal and distal ends of the aponeuroses (n=6). Muscle fibers were also trimmed along with aponeuroses down to 5-20 fibers and identical measurements were performed (n=6). The magnitude of shortening decreased as MTU length increased. The magnitude of shortening ranged from -0.08 to 0.3 microm, and there was no significant difference between delta SL as a function of clamp location. When aponeuroses were trimmed, sarcomere shortening was not observed at L(0) and longer. These results suggest that the aponeurosis is the major contributor to in-series compliance. Results also support our hypothesis but there also appear to be other factors affecting internal sarcomere shortening. The functional consequence of internal sarcomere shortening as a function of sarcomere length was to skew the muscle length-tension relationship to longer sarcomere lengths.  相似文献   

2.
The interaction between the semitendinosus muscle and both hip and knee joint angles was examined in the frog (Rana pipiens) hindlimb. Sarcomere length was measured by laser diffraction in passive muscle during hip and knee rotation. A model was then developed to predict semitendinosus sarcomere length as a function of both hip and knee flexion angle. Based on published frog muscle fiber length-tension [Gordon, A. M. et al., J. Physiol. 184, 170-192 (1966)] and force-velocity [Edman, K. A. P., J. Physiol. 291, 143-159 (1979)] properties, and published joint angles during hopping [Calow, L. J. and Alexander, R. McN., J. Zool. (Lond.) 171, 293-321 (1973)], muscle sarcomere length, force and hip and knee torque during a hop were predicted. The semitendinosus muscle generally operated on the descending limb of the length-tension curve at normal joint angle combinations. The model predicted that, during a single coordinated movement, a period of sarcomere shortening (concentric) was followed by a period of sarcomere lengthening (eccentric). Based on calculated torque profiles at the hip and knee joints, this study suggested that the semitendinosus muscle probably functions more as a hip extensor than a knee flexor. In addition, based on the nature of the shortening-lengthening cycle, the semitendinosus may act to mechanically link the force of knee extension to hip extension.  相似文献   

3.
We attempted to analyze the relationships between the steric structure of the sarcomere and its physiological functions by the use of a sarcomere model of muscle contraction, which includes the geometric arrangement of the thick and thin filaments of the sarcomere, as well as of the cross-bridges and actin sites. Motions of both cross-bridges and myofilaments were considered in terms of our three-state model of the elementary cycle under constraints caused by the steric structure of the sarcomere proposed by Huxley and Brown. Each cross-bridge moves in a molecular potential of our three-state model under the influence of the sliding motions of myofilaments. The sarcomere model described well the tension-velocity relation and isotonic transient processes quantitatively and consistently. In addition, it allowed independence of the no-load shortening velocity upon the overlap of the thick and thin filaments, although the motions of cross-bridges were not independent. Effects of the helical periodicities of the thick and thin filaments and of the number of cross-bridges upon muscle contraction were studied, and the conditions for smooth and efficient contraction of muscle were obtained.  相似文献   

4.
横纹肌肌原纤维的第三肌丝──肌联蛋白   总被引:2,自引:0,他引:2  
实验研究证明,在动物横纹肌肌原纤维中,除包含有粗肌丝、细肌丝外,还有纤肌丝的存在,肌联蛋白(肌巨蛋白)是具有挠性的线状蛋白质,分子量为3000 000,长度约为0.9μm,跨越肌原纤维的M-线和Z-线,形成纤肌丝.其生理功能是在粗肌丝装配中具有分子模板作用,并将粗肌丝稳定于肌原纤维肌小节中央以及可参与肌球蛋白活性的调节.  相似文献   

5.
Single fibers isolated from walking leg muscles of crayfish have 8- to 10-µ sarcomeres which are divided into A, I, and Z bands. The H zone is poorly defined and no M band is distinguishable. Changes in the width of the I band, accompanied by change in the overlap between thick and thin myofilaments, occur when the length of the sarcomere is changed by stretching or by shortening the fiber. The thick myofilaments (ca. 200 A in diameter) are confined to the A band. The thin myofilaments (ca. 50 A in diameter) are difficult to resolve except in swollen fibers, when they clearly lie between the thick filaments and run to the Z disc. The sarcolemma invaginates at 50 to 200 sites in each sarcomere. The sarcolemmal invaginations (SI) form tubes about 0.2 µ in diameter which run radially into the fiber and have longitudinal side branches. Tubules about 150 A in diameter arise from the SI and from the sarcolemma. The invaginations and tubules are all derived from and are continuous with the plasma membrane, forming the transverse tubular system (TTS), which is analogous with the T system of vertebrate muscle. In the A band region each myofibril is enveloped by a fenestrated membranous covering of sarcoplasmic reticulum (SR). Sacculations of the SR extend over the A-I junctions of the myofibrils, where they make specialized contacts (diads) with the TTS. At the diads the opposing membranes of the TTS and SR are spaced 150 A apart, with a 35-A plate centrally located in the gap. It appears likely that the anion-permselective membrane of the TTS which was described previously is located at the diads, and that this property of the diadic structures therefore may function in excitation-contraction coupling.  相似文献   

6.
Optical Diffraction Studies of Muscle Fibers   总被引:8,自引:2,他引:6       下载免费PDF全文
A new technique to monitor light diffraction patterns electrically is applied to frog semitendinosus muscle fibers at various levels of stretch. The intensity of the diffraction lines, sarcomere length change, and the length-dispersion (line width) were calculated by fast analogue circuits and displayed in real time. A heliumneon laser (wavelength 6328 Å) was used as a light source. It was found that the intensity of the first-order diffraction line drops significantly (30-50%) at an optimal sarcomere length of 2.8 μm on isometric tetanic stimulation. Such stimulation produced contraction of half-sarcomeres by about 22 nm presumably by stretching inactive elements such as tendons. The dispersion of the sarcomere lengths is extremely small, and it is proportional to the sarcomere length (less than 4%). The dispersion increases on stimulation. These changes on isometric tetanic stimulation were dependent on sarcomere length. No vibration or oscillation in the averaged length of the sarcomeres was found during isometric tetanus within a resolution of 3 nm; however, our observation of increased length dispersion of the sarcomeres together with detection of the averaged shortening of the sarcomere lengths suggests the presence of asynchronous cyclic motions between thick and thin filaments. An alternative explanation is simply an increase of the length dispersion of sarcomeres without cyclic motions.  相似文献   

7.
Single fibres from the semitendinosus muscle of frog were illuminated normally with a He–Ne laser. The intensity transient and fine structure pattern of light diffracted from the fibre undergoing isometric twitches were measured. During fibre shortening, the intensity decreased rapidly and the fine structure pattern preserved its shape and moved swiftly away from the undiffracted laser beam. The fine structure patterns of the contracting and resting fibre were nearly identical. The ratio of intensities of the contracting and resting fibre of the same sarcomere length was determined as a function of the time elapsed after fibre stimulation. The time-resolved intensity ratio increased with sarcomere length and became unity when sarcomere length was between 3.5 m and 3.7 m. A diffraction theory based on the sarcomere unit was developed. It contained a parameter describing the strength of filament interaction. The comparison between the theory and data shows that the initial intensity drop during contraction is primarily due to filament interactions. At a later stage of contraction, sarcomere disorder becomes the major component causing the intensity to decrease. Diffraction models which use the Debye-Waller formalism to explain the intensity decrease are discussed. The sarcomere-unit diffraction model is applied to previously reported intensity measurements from active fibres.  相似文献   

8.
Bundles of the curarized semitendinosus muscle of the frog were fixed during isotonic (afterload) and isometric contraction and the length of the A and I bands investigated by electron microscopy. The sarcomere length, during afterload contraction initiated at 25 per cent stretch, varied depending on the afterload applied between 3.0 and 1.2 µ, i.e. the shortening amounted to 5 to 50 per cent. The shortening involved both the A and I bands. Between a sarcomere length of 3.0 to 1.7 µ (shortening 5 to 35 per cent) the A bands remained practically constant at about 1.5 µ (6 to 8 per cent shortening); the length of the I bands decreased from 1.4 to 0.3 µ (80 per cent shortening). Below a sarcomere length of 1.7 to 1.2 µ the A bands shortened from 1.5 to 1.0 µ (from 6 to 8 to 25 per cent). At sarcomere lengths 1.6 to 1.2 µ the I band was replaced by a contraction band. During isometric contraction the A bands shortened by about 8 to 10 per cent; the I bands were correspondingly elongated.  相似文献   

9.
Changes in thick filament length in Limulus striated muscle   总被引:4,自引:4,他引:0       下载免费PDF全文
Here we describe the change in thick filament length in striated muscle of Limulus, the horseshoe crab. Long thick filaments (4.0 microns) are isolated from living, unstimulated Limulus striated muscle while those isolated from either electrically or K+-stimulated fibers are significantly shorter (3.1 microns) (P less than 0.001). Filaments isolated from muscle glycerinated at long sarcomere lengths are long (4.4 microns) while those isolated from muscle glycerinated at short sarcomere lengths are short (2.9 microns) and the difference is significant (P less than 0.001). Thin filaments are 2.4 microns in length. The shortening of thick filaments is related to the wide range of sarcomere lengths exhibited by Limulus telson striated muscle.  相似文献   

10.
SYNOPSIS. Electron microscopic studies are reported on glycerinatedskeletal and cardiac muscle of a benthic fish, Coryphaenoidesspecies. In white skeletal muscle, the sarcomeres have a restinglength of approximately 1.8 µ, with thick filaments 1.4µ and thin filaments 0.75 µ in length. These dimensionsare somewhat shorter than filament lengths of oilier vertebratemuscles, possibly due to the elfect of volume increase duringassembly of thick and thin filaments at high hydrostatic pressure.During ATP-induced contraction of Coryphaenoides muscle fromsarcomere lengths of 1.8 µ to 1.6 µ, there is acharacteristic interdigitation of thick and thin filaments,with decrease in I band length and no change in length of thickor thin filaments. However, in sarcomeres contracted to lengthsof 1.5 µ. to 1.2 µ, there is a slight shorteningof the A band, apparently due to shortening of thick filaments,that occurs despite the presence of residual I band in the samesarcomeres. There is no obvious crumpling or distortion of thickfilaments during contraction to sarcomere lengths as low as1.0 µ, but filament organization undergoes extensive disarrayat sarcomere lengths approaching 0.7 µ. Although effectsfrom heterogeneity of filament length cannot be excluded withcertainty, the present evidence does suggest that contractionot Coryphaenoides muscle from 1.6 µ to 1.0 µ sarcomerelengih is accompanied by shortening of thick filaments consequentto a structural change within the thick filament core.  相似文献   

11.
Light diffraction patterns produced by single skeletal muscle fibers and small fiber bundles of Rana pipiens semitendinosus have been examined at rest and during tetanic contraction. The muscle diffraction patterns were recorded with a vidicon camera interfaced to a minicomputer. Digitized video output was analyzed on-line to determine mean sarcomere length, line intensity, and the distribution of sarcomere lengths. The occurrence of first-order line intensity and peak amplitude maxima at approximately 3.0 mum is interpreted in terms of simple scattering theory. Measurements made along the length of a singel fiber reveal small variations in calculated mean sarcomere length (SD about 1.2%) and its percent dispersion (2.1% +/- 0.8%). Dispersion in small multifiber preparations increases approximately linearly with fiber number (about 0.2% per fiber) to a maximum of 8-10% in large bundles. Dispersion measurements based upon diffraction line analysis are comparable to SDs calculated from length distribution histograms obtained by light micrography of the fiber. First-order line intensity decreases by about 40% during tetanus; larger multifibered bundles exhibit substantial increases in sarcomere dispersion during contraction, but single fibers show no appreciable dispersion change. These results suggest the occurrence of asynchronous static or dynamic axial disordering of thick filaments, with a persistence in long range order of sarcomere spacing during contraction in single fibers.  相似文献   

12.
In the present investigation of cross-striated muscle fibers of axolotl, we succeeded in observing in one field of vision of the electron microscope all the stages of myofibril contraction. This allowed us to avoid errors in establishing the sequence of individual contraction stages. Our studies reveal a new contraction stage which appears at the shortening of the sarcomere below 74 per cent of the "resting length" but prior to the formation of typical "maximally shortened" sarcomeres, characterized by strong "contraction bands." At this stage, in the center of the sarcomere, at either side of the M line, a "secondary anisotropic" band arises which widens with further sarcomere contraction. At either side of this band, at the place of the former ("primary") anisotropic band, a "secondary isotropic" band is formed. A scheme of successive stages of contraction of the sarcomere is presented. The mechanisms of contraction for the first stage (from 100 to 79 per cent of the "resting length") and for the last stage (from 74 to 58 per cent of the "resting length") seem to be different. While the sliding of myofilaments with respect to one another can be assumed for the first stage, it is the spiralization of these structures which is the most likely explanation for the last stage. (An Abstract in German also appears at the end of this article.)  相似文献   

13.
Titin, a giant protein spanning half the sarcomere, is responsible for passive and restoring forces in cardiac myofilaments during sarcomere elongation and compression, respectively. In addition, titin has been implicated in the length-dependent activation that occurs in the stretched sarcomere, during the transition from diastole to systole. The purpose of this study was to investigate the role of titin in the length-dependent deactivation that occurs during early diastole, when the myocyte is shortened below slack length. We developed a novel in vitro assay to assess myocyte restoring force (RF) by measuring the velocity of recoil in Triton-permeabilized, unloaded rat cardiomyocytes after rigor-induced sarcomere length (SL) contractions. We compared rigor-induced SL shortening to that following calcium-induced (pCa) contractions. The RF-SL relationship was linearly correlated, and the SL-pCa curve displayed a characteristic sigmoidal curve. The role of titin was defined by treating myocytes with a low concentration of trypsin, which we show selectively degrades titin using mass spectroscopic analysis. Trypsin treatment reduced myocyte RF as shown by a decrease in the slope of the RF-SL relationship, and this was accompanied by a downward and leftward shift of the SL-pCa curve, indicative of sensitization of the myofilaments to calcium. In addition, trypsin digestion did not alter the relationship between SL and interfilament spacing (assessed by cell width) after calcium activation. These data suggest that as the sarcomere shortens below slack length, titin-based restoring forces act to desensitize the myofilaments. Furthermore, in contrast to length-dependent activation at long SLs, length-dependent deactivation does not depend on interfilament spacing. This study demonstrates for the first time the importance of titin-based restoring force in length-dependent deactivation during the early phase of diastole.  相似文献   

14.
We most often consider muscle as a motor generating force in the direction of shortening, but less often consider its roles as a spring or a brake. Here we develop a fully three-dimensional spatially explicit model of muscle to isolate the locations of forces and energies that are difficult to separate experimentally. We show the strain energy in the thick and thin filaments is less than one third the strain energy in attached cross-bridges. This result suggests the cross-bridges act as springs, storing energy within muscle in addition to generating the force which powers muscle. Comparing model estimates of energy consumed to elastic energy stored, we show that the ratio of these two properties changes with sarcomere length. The model predicts storage of a greater fraction of energy at short sarcomere lengths, suggesting a mechanism by which muscle function shifts as force production declines, from motor to spring. Additionally, we investigate the force that muscle produces in the radial or transverse direction, orthogonal to the direction of shortening. We confirm prior experimental estimates that place radial forces on the same order of magnitude as axial forces, although we find that radial forces and axial forces vary differently with changes in sarcomere length.  相似文献   

15.
Electron microscopy was used to study the positional stability of thick filaments in isometrically contracting skinned rabbit psoas muscle as a function of sarcomere length at 7 degrees C. After calcium activation at a sarcomere length of 2.6 micron, where resting stiffness is low, sarcomeres become nonuniform in length. The dispersion in sarcomere length is complete by the time maximum tension is reached. A-bands generally move from their central position and continue moving toward one of the Z-discs after tension has reached a plateau at its maximum level. The lengths of the thick and thin filaments remain constant during this movement. The extent of A-band movement during contraction depends on the final length of the individual sarcomere. After prolonged activation, all sarcomeres between 1.9 and 2.5 micron long exhibit A-bands that are adjacent to a Z-disc, with no intervening I-band. Sarcomeres 2.6 or 2.7 micron long exhibit a partial movement of A-bands. At longer sarcomere lengths, where the resting stiffness exceeds the slope of the active tension-length relation, the A-bands remain perfectly centered during contraction. Sarcomere symmetry and length uniformity are restored upon relaxation. These results indicate that the central position of the thick filaments in the resting sarcomere becomes unstable upon activation. In addition, they provide evidence that the elastic titin filaments, which join thick filaments to Z-discs, produce almost all of the resting tension in skinned rabbit psoas fibers and act to resist the movement of thick filaments away from the center of the sarcomere during contraction.  相似文献   

16.
The extensibility of the myofilaments in vertebrate skeletal muscle was studied by stretching glycerinated rabbit psoas muscle fibers in rigor state and examining the resulting extension of sarcomere structures under an electron microscope. Although stretches applied to rigor fibers produced a successive yielding of the weakest sarcomeres, the length of the remaining intact sarcomeres in many myofibrils was fairly uniform, being definitely longer than the sarcomeres in the control, nonstretched part of rigor fibers. The stretch-induced increase in sarcomere length was found to be taken up by the extension of the H zone and the I band, whereas the amount of overlap between the thick and thin filaments did not change appreciably with stretches of 10-20%. The thick filament extension in the H zone was localized in the bare regions, whereas the thin filament extension in the I band appeared to take place uniformly along the filament length. No marked increase in the Z-line width was observed even with stretches of 20-30%. These results clearly demonstrate the extensibility of the thick and thin filaments. The possible contribution of the myofilament compliance to the series elastic component (SEC) in vertebrate skeletal muscle fibers is discussed on the basis of the electron microscopic data and the force-extension curve of the SEC in rigor fibers.  相似文献   

17.
Basalar and tibial extensor muscle fibers of Achalarus lyciades were examined with light and electron microscopes. Basalar muscle fibers are 100–150 µ in diameter. T-system membranes and sarcoplasmic reticulum make triadic contacts midway between Z lines and the middle of each sarcomere. The sarcoplasmic reticulum is characterized by a transverse element situated among myofilaments halfway between Z lines in every sarcomere. The morphology of Z lines, hexagonal packing of thin and thick myofilaments, and thin/thick myofilament ratios are similar to those of fast-acting insect muscles. Tibial extensor muscle fibers are 50–100 µ in diameter. Except for a lack of the transverse element, the T system and sarcoplasmic reticulum are similar to those of basalar muscle. Wavy Z lines, lack of a hexagonal packing of myofilaments, and larger thin/thick myofilament ratios are similar to those of other postural muscles of insects. The morphology of basalar and tibial extensor muscle is compared to that of other insect muscle with known functions, and reference is made to the possible contribution of the transverse element of sarcoplasmic reticulum in basalar flight muscle to speed and synchrony in this muscle.  相似文献   

18.
The sarcomere length-tension relation in skeletal muscle   总被引:5,自引:0,他引:5       下载免费PDF全文
Tension development during isometric tetani in single fibers of frog semitendinosus muscle occurs in three phases: (a) in initial fast-rise phase; (b) a slow-rise phase; and (c) a plateau, which lasts greater than 10 s. The slow-rise phase has previously been assumed to rise out of a progressive increase of sarcomere length dispersion along the fiber (Gordon et al. 1966. J. Physiol. [Lond.]. 184:143--169;184:170-- 192). Consequently, the "true" tetanic tension has been considered to be the one existing before the onset of the slow-rise phase; this is obtained by extrapolating the slowly rising tension back to the start of the tetanus. In the study by Gordon et al. (1966. J. Physiol. [Lond.] 184:170--192), as well as in the present study, the relation between this extrapolated tension and sarcomere length gave the familiar linear descending limb of the length-tension relation. We tested the assumption that the slow rise of tension was due to a progressive increase in sarcomere length dispersion. During the fast rise, the slow rise, and the plateau of tension, the sarcomere length dispersion at any area along the muscle was less than 4% of the average sarcomere length. Therefore, a progressive increase of sarcomere length dispersion during contraction appears unable to account for the slow rise of tetanic tension. A sarcomere length-tension relation was constructed from the levels of tension and sarcomere length measured during the plateau. Tension was independent of sarcomere length between 1.9 and 2.6 microgram, and declined to 50% maximal at 3.4 microgram. This result is difficult to reconcile with the cross-bridge model of force generation.  相似文献   

19.
A-band shortening in single fibers of frog skeletal muscle.   总被引:1,自引:0,他引:1       下载免费PDF全文
The question of whether A-bands shorten during contraction was investigated using two methods: high-resolution polarization microscopy and electron microscopy. During shortening from extended sarcomere lengths in the passive state, sarcomere-length changes were essentially accounted for by I-band shortening. During active shortening under otherwise identical conditions, the sarcomere length change was taken up approximately equally by A- and I-bands. Several potential artifacts that could give rise to apparent A-band shortening were considered and judged unlikely. Results obtained with polarization microscopy were similar to those obtained with electron microscopy. Thus, modest but significant thick filament shortening appears to occur during active sarcomere shortening under physiological conditions.  相似文献   

20.
The repulsive pressure between filaments in the lattice of skinned rabbit and frog striated muscle in rigor has been measured as a function of interfilament spacing, using the osmotic pressure generated by solutions of large, uncharged polymeric molecules (dextran and polyvinylpyrrolidone). The pressure/spacing measurements have been compared with theoretically derived curves for electrostatic pressure. In both muscles, the major part of the experimental curves (100-2,000 torr) lies in the same region as the electrostatic pressure curves, providing that a thick filament charge diameter of approximately 30 nm in rabbit and approximately 26 nm in frog is assumed. In chemically skinned or glycerol-extracted rabbit muscle the fit is good; in chemically skinned frog sartorius and semitendinosus muscle the fit is poor, particularly at lower pressures where a greater spacing is observed than expected on theoretical grounds. The charge diameter is much larger than the generally accepted value for thick filament backbone diameter. This may be because electron microscope results have underestimated the amount of filament shrinkage during sample preparation, or because most of the filament charge is located at some distance from the backbone surface, e.g., on HMM-S2. Decreasing the ionic strength of the external solution, changing the pH, and varying the sarcomere length all give pressure/spacing changes similar to those expected from electrostatic pressure calculations. We conclude that over most of the external pressure range studied, repulsive pressure in the lattice is predominantly electrostatic.  相似文献   

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