UMLS:C0231530 - FACTA Search

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Query: UMLS:C0231530 (twitching)
2,043 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of a single voluntary contraction of the quadriceps muscle group on phosphate incorporation into the phosphorylatable light chains (P-light chains) of fast and slow myosin isolated from the vastus lateralis muscle and potentiation of the electrically stimulated twitch tension was studied in intact human muscle. Twitch potentiation was maximal 20 s after the voluntary contraction. Thereafter, twitch potentiation declined, but was still significantly higher than pre-contraction values 2 min after the voluntary contraction. Phosphate incorporation into the P-light chain of fast myosin followed a similar time course to twitch potentiation, but no phosphate was incorporated into slow myosin P-light chains. These observations suggest that myosin light chain kinase activity is mainly associated with fast-twitch muscle fibers and, in agreement with previous studies, suggests that twitch potentiation associated with P-light chain phosphorylation is confined to the fast-twitch fibers of human muscle.
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PMID:Myosin light chain phosphorylation and isometric twitch potentiation in intact human muscle. 383 3

1. Cat soleus (slow twitch) was cross-reinnervated with nerve to flexor hallucis or digitorum longus muscle (fast twitch). More than 3 years later motor unit isometric contractions and muscle immunohistochemistry and histochemistry were investigated. All muscles differed from normal fast or slow muscle.2. The motor units could be divided into two groups: one with fast twitches and low tetanic tension, the other with slow twitches and high tension. This is the reverse of the relation between motor unit twitch time and tetanic tension in normal muscle (fast or slow).3. Motor unit twitch time to peak decreased with axonal conduction velocity, as in normal muscle, but so did tetanic tension, which is abnormal.4. Twitch-tetanus ratio increased with twitch time to peak in the group of slow units but not in the fast group (although the range of ratios was as great).5. A tetanus depressed the twitch tension of slow motor units and potentiated fast ones as in normal muscle but the potentiation was often accompanied by an abnormal prolongation of the twitch.6. The mean conduction velocity of axons was slightly higher than at 6 months' reinnervation but below the normal value for fast muscle.7. Antibody to slow myosin was bound strongly to Type I fibres but not to Type II fibres, confirming the histochemical division of fibres into Types I and II.8. More than 95% of the fibres were oxidative, with Type I predominating over Type II a in the ratio of about 2:1.9. The higher tension of the slow motor units was the result of three factors: the number of fibres per motor unit was at least three times that in the fast; Type I fibres had cross-sectional areas little less than Type II (a and b together) and were estimated to develop more tension per unit area. All three findings were different from those in normal fast muscle.10. One flexor hallucis longus muscle was self-reinnervated and examined histochemically. This muscle was abnormal in that a large majority of the fibres were Type I.
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PMID:Motor units and immunohistochemistry of cat soleus muscle after long periods of cross-reinnervation. 621 65

Fast-twitch muscles of the hindlimb of dystrophic (dy2J) mice show a prolongation of both the contraction and relaxation phases of the isometric twitch. Comparable muscles of the forelimb of these mice exhibit relatively little increase in time to peak tension but time to half-relaxation is as severely affected as in the hindlimb. When examined with an immunohistochemical technique to demonstrate the presence of "slow" myosin it was apparent that there were no fibers containing the "slow" isoenzyme in either hindlimb or forelimb muscles of 6-month control mice. In dy2J mice hindlimb muscles contained many fibers with "slow" myosin whereas forelimb muscles did not. It is suggested that the spontaneous twitching activity produced in the hindlimbs, as a result of amyelination of the spinal roots, induces synthesis of "slow" myosin, which in turn leads to prolongation of time to peak twitch tension.
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PMID:Slowing of twitch of dystrophic mouse muscle in partially due to altered activity pattern. 622 47

1. Isometric contractions of motor units, isolated functionally by ventral root splitting in vivo, were recorded from mouse soleus muscle. 2. Motor unit tensions varied over a narrow symmetrical range and averaged 4.7% of whole muscle tension, corresponding to twenty-one motor units per muscle. 3. There was considerable variation between muscles in isometric twitch times-to-peak and even greater variation for the motor units. The distribution of motor unit times-to-peak was apparently unimodal and could be fitted by a single normal population. A slightly better fit was, however, obtained with two normal populations, as suggested by the histochemistry. 4. Twitch time-to-peak decreased in proportion to axonal conduction velocity in individual animals. The whole population of motor units could be fitted by a linear relation between time-to-peak and the reciprocal of conduction time in the motor axon. Motor unit tension was also linearly related to the reciprocal of conduction time. 5. Histochemistry showed clear division between Type I and Type IIa fibres. Type I fibres reacted strongly with antibody against slow myosin of cat soleus muscle; Type IIa gave a reaction no stronger than the background. The division was as clear as in the cat or rat.
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PMID:Isometric contractions of motor units and immunohistochemistry of mouse soleus muscle. 705 Mar 45

The extent to which treatment with low doses of the nonfluorinated steroid methylprednisolone affects diaphragm contractility and morphology is unknown. In the present study, we compared the effects of equipotent doses of methylprednisolone and deflazacort, an oxazoline derivate of prednisolone with less systemic side-effects on bone structure and carbohydrate metabolism. Twenty six male adult rats were randomized to receive daily saline (control), methylprednisolone 0.4 mg.kg-1 or deflazacort 0.5 mg.kg-1 i.m. Contractile properties and histopathology were measured after a 6 week treatment period. During treatment, body weight increased in control and methylprednisolone-treated animals, but decreased by 4.2 +/- 1.1% (mean +/- SD) in the deflazacort group. Similarly, diaphragm mass in the deflazacort group was decreased compared to control and methylprednisolone groups. Twitch tension and twitch characteristics of isolated diaphragm bundles were similar in the three groups. Maximal tetanic tension was decreased in the deflazacort group. The force-frequency curve of the deflazacort bundles shifted downwards compared to control. Fatigue occurring during this protocol was greatest in the methylprednisolone- and deflazacort-treated animals. Microscopic examination revealed no gross abnormalities in the three groups. Histochemical analysis after staining for myosin adenosine triphosphatase (ATP-ase) showed that in the deflazacort group cross-sectional area of type I, IIa and IIb fibres were decreased. We conclude that low doses of methylprednisolone caused subtle and negligible changes in rat diaphragm contractile properties without affecting fibre dimensions, while deflazacort at an equipotent dose induced generalized fibre atrophy and changes in diaphragm contractility.
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PMID:Rat diaphragm contractility and histopathology are affected differently by low dose treatment with methylprednisolone and deflazacort. 765 57

This work studies the dynamic metabolic changes of the rabbit masseter muscle during post-natal development. The composition and proportion of oxidative and glycolytic muscle fibers alter during maturation. The masseter muscle, as most muscles of the craniofacial region, exhibits unusual development in composition of isoforms of myosin. The effect of this unusual composition on the dynamic metabolic properties of the masseter muscle have not been assessed. The metabolism of the rabbit masseter muscle was studied by means of 31P-nuclear magnetic resonance (NMR) spectroscopy. Contraction was elicited by electrical stimulation of the muscle in the anesthetized animal. Five animals were studied at 8 weeks and 24 weeks so that both the juvenile and adult stages could be evaluated. The dynamic biochemical changes in the masseter muscle were studied by the analysis of NMR spectra. A single-turn surface coil (copper) was used, and the original signal was treated with Fourier transforms to obtain 31P spectra. The low signal-to-noise ratio required averaging 16 acquisitions (acquisition time = 400 msec, repetition rate = 1.8 sec) in 30 sec and then obtaining continuous spectra for 27 min. Each averaged spectrum demonstrated five peaks: inorganic phosphate (Pi), creatine phosphate (PCr), and three peaks related to adenosine triphosphate (ATP). The protocol involved recording an initial three-minute rest period, stimulating the muscle at 5 Hz for 3 min twice, separated by three-minute rest periods, and stimulating the muscle at 50 Hz twice for 3 min separated by rest periods. The Pi/PCr ratio increased significantly in the adult masseter during both 5-Hz stimulations, evoking twitching, and the first 50-Hz stimulation, evoking tetany (repeated ANOVA, P < 0.05). The resting pH (6.96 +/- 0.13) was significantly lowered during both twitching (6.85 +/- 0.10; P < 0.0038) and tetany (6.55 +/- 0.13; P < 0.0001), but only in the adult masseter muscle. These finding suggest that the adult masseter muscle possesses more glycolytic fibers as it modifies its metabolism during postnatal development.
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PMID:Effect of maturation on 31P magnetic resonance spectroscopy of the rabbit masseter muscle. 860 Jan 82

Studies of skinned fibers suggest that the rate of ATP turnover in skeletal muscle is depressed by acidosis. To examine whether this occurs in intact muscles, the ATP cost of isometric contractions was measured in ex vivo, arterially perfused cat biceps (predominantly fast-twitch) and soleus (slow-twitch) muscles under normocapnic (5% CO2) and hypercapnic (70% CO2) conditions. Hypercapnia decreased extracellular pH from 7.4 to 6.7 and intracellular pH from 7.1 to 6.5 (soleus) or 6.6 (biceps) but had no significant effect on the phosphocreatine (PCr)-to-ATP ratio in muscles at rest. The ATP cost of contraction was estimated from PCr changes, measured by gating the acquisition of 31P-nuclear magnetic resonance spectra to times before and after brief tetani (1 s at 100 Hz and 2 s at 25 Hz for biceps and soleus, respectively) or 10-s trains of twitches (2 and 1 Hz, respectively). Peak isometric force and the ATP cost of tetanic contraction (PCr/force x time integral) were not significantly different under hypercapnic compared with normocapnic conditions in either muscle (mean: 7.97 and 2.44 micromol x kg(-1) x s(-1) for biceps and soleus, respectively). Twitch force and the ATP cost per twitch decreased by nearly 50% during hypercapnic perfusion in both muscle types. The results indicate that hypercapnic acidosis has no significant effect on the ATPase rate per active myosin head in intact mammalian skeletal muscle.
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PMID:Acidosis has no effect on the ATP cost of contraction in cat fast- and slow-twitch skeletal muscles. 912 91

Goldfish (Family Cyprinidae, Carassius auratus) and killifish (Family Cyprinodontidae, Fundulus heteroclitus) were acclimated to 10, 20 and 35 °C for 4 weeks. The thermal acclimation of C-start (escape swimming) performance and the physiological properties of fast twitch muscle fibres that underlie it were investigated in these species at the molecular (myosin isoform expression), biochemical (myofibrillar ATPase activity), cellular (contractile kinetics) and organismal levels of organisation. Peptide maps were obtained for fast muscle myosin heavy chains, isolated from 10 °C- and 35 °C-acclimated fish. Different myosin heavy chain isoforms were expressed in response to a change in acclimation temperature in goldfish, but myosin heavy chain isoform expression was unaffected by acclimation temperature in killifish. Compared with fish acclimated to 35 °C, acclimation to 10 °C increased the activity of fast muscle myofibrillar ATPase assayed at 10 °C fivefold in goldfish and only 50 % in killifish. Muscle twitch contraction time at 10 °C decreased significantly in response to acclimation to 10 °C in both species; however, the magnitude of this response was much greater in goldfish (100 %) than in killifish (30 % or less). In goldfish, these changes in the physiological properties of fast twitch fibres during 10 °C acclimation resulted in a six- to eightfold increase in the speed and turning velocity of fish performing C-starts at 10 °C. By comparison, the somewhat smaller acclimatory response of killifish fast muscle properties was accompanied by only a minor (50 % or less) adjustment in locomotor performance. Thermal acclimatory responses of fast muscle at the molecular, biochemical and cellular levels of organisation are clearly reflected in alterations in organismal escape performance.
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PMID:The thermal acclimation of burst escape performance in fish: an integrated study of molecular and cellular physiology and organismal performance 932 80

Twitch potentiation and fatigue in skeletal muscle are two conditions in which force production is affected by the stimulation history. Twitch potentiation is the increase in the twitch active force observed after a tetanic contraction or during and following low-frequency stimulation. There is evidence that the mechanism responsible for potentiation is phosphorylation of the regulatory light chains of myosin, a Ca2+-dependent process. Fatigue is the force decrease observed after a period of repeated muscle stimulation. Fatigue has also been associated with a Ca2+-related mechanism: decreased peak Ca2+ concentration in the myoplasm is observed during fatigue. This decrease is probably due to an inhibition of Ca2+ release from the sarcoplasmic reticulum. Although potentiation and fatigue have opposing effects on force production in skeletal muscle, these two presumed mechanisms can coexist. When peak myoplasmic Ca2+ concentration is depressed, but myosin light chains are relatively phosphorylated, the force response can be attenuated, not different, or enhanced, relative to previous values. In circumstances where there is interaction between potentiation and fatigue, care must be taken in interpreting the contractile responses.
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PMID:Coexistence of potentiation and fatigue in skeletal muscle. 1077 80

The effect of aging on the in vitro contractile properties of the patagialis (PAT) muscle of 35 young adult (YA; 8 weeks of age) and 35 aged adult (AA, 110 weeks of age) Coturnix quails was examined after 0-30 days of stretch-overload. Overload was achieved by placing a weight equivalent to 12% of the birds' body weight on one wing. The contralateral wing served as the intra-animal control. Overload increased the weight of the PAT by 45.1+/-2.1% in YA, and 24.1+/-2.6% in AA. Twitch contraction time increased with loading from 43.2+/-1.2 to 67.3+/-2.2 ms in YA birds and 57.2+/-1.7 to 77.4+/-1.9 ms in AA birds. Unloaded shortening velocity (Vo) decreased by 40.1+/-2.2 and 38.8+/-3.2% in YA and aged birds, respectively. The decrease in fast myosin expression was greater in overloaded muscles of YA (20%) as compared to AA birds (12%). However, this was accompanied by a greater decrease in total muscle ATPase activity in aged birds (61%) compared to YA birds (40%). Myosin isozyme Ca(2+)-ATPase activity was 26% lower in FM1 but not other fast myosins in YA birds, but it was approximately 30% lower in all fast myosins in PAT muscles of aged birds. These data show that the reduction of Vo and the increase in twitch duration with aging may be due in part to reductions in ATPase activity in all myosin isoforms, as compared to myosin isoforms isolated from YA birds.
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PMID:Attenuation of Ca(2+)-activated ATPase and shortening velocity in hypertrophied fast twitch skeletal muscle from aged Japanese quail. 1190 84

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