Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026837 (muscle rigidity)
 1,077 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The thixotropic properties of single muscle fibres have been investigated. The effect is larger than in whole muscle and although the time course of stiffness recovery is generally similar, there is an indication that two phases may be involved. Rigor, induced chemically, eliminates thixotropic behaviour.
 ...
PMID:Thixotropy in frog single muscle fibres. 231 May 57

Tension responses due to small, rapid length changes (completed within 40 microseconds) were obtained from skinned single frog muscle fiber segments (4-10 mm length) incubated in relaxing and rigor solutions at various ionic strengths. The first 2 ms of these responses can be described with a linear model in which the fiber is regarded as a rod, composed of infinitesimally small, identical segments, containing one undamped elastic element and two or three damped elastic elements and a mass in series. Rigor stiffness changed less than 10% in a limited range, 40-160 mM, of ionic strength conditions. Equatorial x-ray diffraction patterns show a similar finding for the filament spacing and intensity ratio I(11)/I(10). Relaxed fibers became stiffer under low ionic strength conditions. This stiffness increment can be correlated with a decreasing filament spacing and (an increased number of) weakly attached cross-bridges. Under low ionic strength conditions an additional recovery (1 ms time constant) became noticeable which might reflect characteristics of weakly attached cross-bridges.
 ...
PMID:Weakly attached cross-bridges in relaxed frog muscle fibers. 278 23

A study was carried out to investigate the effects of ionic strength and monovalent cations on isometric, Ca2+-activated force and rigor responses in mechanically skinned muscle fibres. Three types of skeletal muscle fibres were used: rat fast- and slow-twitch fibres and toad twitch fibres. The contractile apparatus of rat slow-twitch fibres was affected differently from that of rat fast-twitch and amphibian twitch fibres when changing the ionic strength (expressed either in terms of ionic equivalents as I or formally as gamma/2) and [K+]. Thus, the apparent sensitivity to Ca2+ decreased substantially more in slow-twitch fibres (by a factor of 20) than in the other fibre types (by a factor of 12) when I and [K+] were increased from 94 to 354 mM and from 56 to 316 mM respectively. Maximum Ca2+-activated force, however, declined only by a factor of 2.2 in slow-twitch fibres compared with 4.2 in the other fibre types, when I was increased from 154 to 354 mM. In slow-twitch fibres the force oscillations of myofibrillar origin were found to increase substantially in amplitude, duration and frequency at low values of I and almost disappeared at high ionic strength. At low values of I, it was also discovered that ca. 50% of the fast-twitch fibres responded with myofibrillar force oscillations when submaximally activated. The characteristics of these oscillations were different from those of slow-twitch fibres. Rigor force levels were found to decline markedly with increasing iota and [K+] in all fibre types. Unexpectedly, once rigor force was established in a certain ionic environment, the level of force was stable regardless of further changes in ionic strength and monovalent cation concentration. These results indicate that the rigor cross-bridges can be formed in different stable positions and that the probability of attachment in certain positions (rather than the total number of cross-bridges that can be formed) is influenced by the ionic conditions. Further experimental evidence provided in this study shows that the increase in [K+] is mainly responsible for the decrease of the Ca2+-sensitivity of the contractile apparatus and that ionic strength (expressed as I rather than gamma/2) influences markedly the maximal Ca2+-activated force, the maximum steepness of the pCa-force relations and the oscillatory processes of myofibrillar origin.
 ...
PMID:Potassium and ionic strength effects on the isometric force of skinned twitch muscle fibres of the rat and toad. 308 99

Rigor tension was found to vary significantly with the replacement rate of the relaxing with the rigor solutions. The maximum value of rigor tension (Prig = 130 kN/m2) was obtained under slow (5 microL/sec) replacement of the solutions. The difference in the tensions may reflect variations in the amount of "compliance" taken out from the fibre.
 ...
PMID:[Maximum rigor tension developed in a single rabbit glycerinated skeletal muscle fiber]. 322 19

An account is given of unusual course of a hyperthermic crisis in a 23-year-old male who underwent repeated anesthetics. As yet little has been reported about Isoflurane, which we presume to have been the triggering agent. In this case only the surgically untreated lower extremity developed rigor, with which malignant hyperthermia is associated, whereas the surgically treated extremity, where circulation had been stopped with a tourniquet, remained unaffected. Rigor and contracture of the affected extremity were so severe that they led to a compartment syndrome, necessitating fasciotomy. No observation of this kind has been published before. In addition to a discussion of this dissociated effect in malignant hyperthermia, a detailed account of the course of the crisis is given.
 ...
PMID:[Malignant hyperthermia. An unusual course of a rare disease]. 340 97

1. A technique was developed to generate 2-8 degrees C step temperature perturbations (T-jumps) in single muscle fibres to study the thermodynamics of muscle contraction. A solid-state pulsed holmium laser emitting at 2.065 microns heated the fibre and surrounding solution in approximately 150 mus. The signal from a 100 microns thermocouple fed back to a heating wire maintained the elevated temperature after the laser pulse. 2. Tension of glycerol-extracted muscle fibres from rabbit psoas muscle did not change significantly following T-jumps when the fibre was relaxed. 3. In rigor, tension decreased abruptly on heating indicating normal (not rubber-like) thermoelasticity. The thermoelastic coefficient (negative ratio of relative length change to relative temperature change) of the fibre was estimated to be -0.021 at sarcomere lengths of 2.5-2.8 microns. Rigor tension was constant after the temperature step and returned to the original value on recooling. 4. In maximal Ca2+ activation, tension transients initiated by T-jumps had several phases. An immediate tension decrease suggests that thermoelasticity during contraction is similar to that in rigor. Active tension then recovered to the value before the T-jump with an apparent rate constant of approximately 400 s-1 (at 10-20 degrees C). This rate constant did not have an appreciable dependence on the final temperature. Finally, tension increased exponentially to a new higher level with a rate constant of approximately 20 s-1 at 20 degrees C. This rate constant increased with temperature with a Q10 of 1.4. 5. At submaximal Ca2+ activation the tension rise was followed by a decay to below the value before the T-jump. This decline was expected from the temperature dependence of steady pCa-tension curves. The final tension decline occurred on the 1-5 s time scale. 6. The value and amplitude dependence of the rate constant for the quick recovery following T-jumps were similar to those of the quick recovery following length steps during active contractions. The enthalpy change associated with the quick tension recovery following temperature-step perturbations was estimated to be positive suggesting that the recovery process is an endothermic reaction. Slower reaction steps on the 10-30 ms timescale, as well as reactions corresponding to the quick recovery, may contribute to the cross-bridge power stroke.
 ...
PMID:Transient tension changes initiated by laser temperature jumps in rabbit psoas muscle fibres. 344 91

Small length changes were imposed on pairs of sartorius muscles from Rana temporaria and Rana pipiens in rigor and the mechanical and thermal responses studied. Rigor was induced by soaking the muscles overnight at 0 degrees C in a physiological salt solution containing 1.5 mM sodium azide and 0.4 mM sodium iodoacetate. Tension was measured at both the tibial and the pelvic ends of the preparation. Muscles were held at a steady tension of 20 to 76 kN m-2 and stretches or releases of 0.02 to 0.6 mm applied in pairs, with the initial change reversed several hundred milliseconds later. Single stretches resulted in heat absorption and releases in heat production by the preparation. Net heat production resulted from complete cycles of length changes larger than 0.1 mm, whether the initial change was a stretch or a release. The heat produced by the complete cycle was attributed to the movement of the muscles over the thermopile. It was proportional to the difference in tension between the tibial and pelvic ends of the preparation and increased with the size and speed of the length change. Half the heat produced by a complete cycle of length changes was subtracted from the thermal response recorded in the first half-cycle to obtain the reversible component of the response. The reversible component was linearly related to the tension change for all sizes and speeds of length change which were studied, with the heat:tension ratio ranging from -0.0093 to -0.0179 in eleven muscles (mean -0.0128 +/- 0.0009). The constancy of the heat:tension ratio in rigor muscles over a wide range of mechanical conditions indicates that the source of the thermal changes is the normal elasticity of the preparation. Since the size of the ratio is approximately the same as that measured in active muscles, the tension-dependent component of the thermal response to length changes applied to active muscles is probably also of elastic origin.
 ...
PMID:The thermoelastic effect in rigor muscle of the frog. 348 55

The polarization properties of light diffracted from single-skinned fibers of skeletal muscles have been examined under conditions in which the bathing solution pH and the ionic strength are changed. For fibers in the relaxed state, we observe large decreases in both the total depolarization signal, r, and the total diffraction birefringence signal, delta nT, upon pH change from 7.0 to 8.0 at normal ionic strength. However, if the ionic strength is raised, then the r-value change as the pH changes from pH 7.0 to pH 8.0 is much smaller. If the rigor state is achieved at pH 8.0, and 0 mM ATP under either of the ionic strength conditions, the fiber can still be stretched. Rigor stiffness for this state is only approximately 20% that of the value of the stiffness at pH 7.0 rigor. Electron micrographs obtained under this pH 8.0 rigor state show that the overlap region can be decreased upon stretching the fiber, signifying a different kind of weaker-binding rigor state. Optically, the weaker-binding rigor state has a lower depolarization signal and larger form birefringence than the strong-binding rigor state. To convert from one type of rigor state (pH 7.0) to the other rigor state (pH 8.0), or vice versa, the fiber must first be relaxed. Apparently, either of the rigor states can block the full impact of the pH effect.
 ...
PMID:Optical ellipsometry on the diffraction order of skinned fibers. pH-induced rigor effects. 349 77

Rigor complexes between actin and myosin have been shown to cause increased binding of Ca2+ to troponin C. A similar effect of force-generating crossbridges has been suggested as an explanation for the coupling between load and activation which has been observed in skeletal and cardiac muscle. The goal of this study was to test the hypothesis that Ca2+-troponin affinity during crossbridge cycling is load-dependent. Ca2+-binding to detergent-extracted rabbit psoas fibres was measured during ATP-induced force generation and in the relaxed state. To compare Ca2+ binding in the latter two states it was necessary to establish conditions in which ATP-induced force could be regulated independently of free Ca2+ concentration. Such conditions were obtained by the use of either the ATPase inhibitor sodium vanadate or the substitution of MgITP for MgATP as an energy source. This study showed that in the presence of MgATP (or MgITP) the amount of Ca2+ bound to the myofilaments at a given free Ca2+ concentration was independent of the force generated. Thus force per se is not a determinant of Ca2+-troponin affinity.
 ...
PMID:The binding of calcium to detergent-extracted rabbit psoas muscle fibres during relaxation and force generation. 385 10

Mechanical and biochemical descriptions of the muscle cross-bridge cycle have been correlated. Skinned muscle fibres of rabbit psoas muscle in rigor were incubated in solutions containing approximately equal to 30 microM-Ca2+ ions and P3-1-(2-nitro)phenylethyladenosine-5'-triphosphate, 'caged ATP', an inert photolabile precursor of ATP. ATP was liberated from caged ATP within the fibres by pulses of 347 nm radiation from a frequency-doubled ruby laser. The mechanical responses of muscle fibres to the rapid increase of ATP concentration were monitored. Tension dropped briefly and then rose above the rigor value to the level characteristic of a steady active contraction. Liberation of ATP decreased in-phase stiffness (measured at 500 Hz) from the rigor level to a maintained value intermediate between rigor and relaxed values. Out-of-phase stiffness increased to a maintained level indicating a phase lead of tension with respect to imposed length oscillations. Rigor tension was varied prior to photolysis by slight alterations of fibre length. Tension traces starting at different rigor tensions converged to a common tension level at the same rate, whether or not Ca2+ was included in the medium. These data suggest that the rate of cross-bridge detachment by ATP from the rigor state is not influenced by Ca2+. Analysis of the tension records, in terms of sequential detachment and reattachment reactions, provided a measure of cross-bridge reattachment rate and an alternate measure of the detachment rate. Detachment from the rigor state was approximately proportional to the ATP concentration, with a second-order rate constant of at least 5 X 10(5) M-1 S-1. Reattachment with force generation had no detectable dependence on the concentration of ATP liberated by photolysis. A simple kinetic model of the cross-bridge cycle in terms of chemically defined intermediates was compatible with most of the experimental data. The ATP dependence of cross-bridge detachment, the kinetics of maintained cross-bridge reattachment in the presence of Ca2+, and transient reattachment and final relaxation in the absence of Ca2+ were explained. In this model, reversibility of cross-bridge attachment and the steps leading to force production allow the relatively high observed detachment rate to be accommodated with other data relating to active contraction. These data include the steady ATPase rate of active muscle fibres and the fewer attached cross-bridges in active contractions compared to rigor.
 ...
PMID:Initiation of active contraction by photogeneration of adenosine-5'-triphosphate in rabbit psoas muscle fibres. 648 46


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>