Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0231530 (twitching)
 2,043 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Epidermal growth factor (EGF) and bovine serum albumin (BSA) are both required for serum-free clonal growth of human muscle satellite cells (HMSC). However, neither inhibits differentiation of HMSC, and when both are added to a minimal serum-free differentiation medium, they enhance survival and maintenance of human myotubes. A combination of 10 ng/mL EGF and 0.5 mg/mL BSA, added to MCDB 120 plus 10 micrograms/mL insulin, increases both total protein per dish and total creatine kinase activity, and keeps the myotubes in good condition for a longer period of time. The myotubes become cross-striated and exhibit frequent spontaneous twitching. Substantial amounts of neonatal myosin heavy chain and the MM isozyme of creatine kinase are expressed, together with detectable amounts of adult fast myosin heavy chain. With regular feeding, these cultures can be maintained for at least 3 weeks with no overgrowth by mononucleate cells, and with far less degeneration than with insulin as the only supplement.
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PMID:Improved medium with EGF and BSA for differentiated human skeletal muscle cells. 150 22

The effects of hypothyroidism on structural and functional properties of the actomyosin-ATPase complex of rat fast-twitch gastrocnemius muscle were examined and related to energetic and mechanical parameters. Hypothyroidism resulted in the appearance of a small band of the myosin heavy chain subunit of the slow form (MHCs) 8% of total MHC) which was absent in the euthyroid group. This observation corresponded with lower activities of myofibrillar ATPase (-14%) and Ca-activated myosin ATPase (-9%) in the hypothyroid group, although these changes were not significant. No effect of hypothyroidism on the Ca2+-sensitivity of the myofibrillar-ATPase activity was observed and tetanic force was not changed. Twitch force, however, was significantly increased by hypothyroidism. The degree of myosin P-light chain phosphorylation (percentage of total amount of P-light chain) determined after 5 and 10 s of tetanic stimulation (130 Hz, 35 degrees C), respectively, proved to be significantly lower in the hypothyroid group (5 s: 57%; 10 s: 61%) vs the euthyroid group (5 s: 79%; 10 s: 82%). There was no difference in P-light chain phosphorylation at rest between eu- and hypothyroids. The results suggest that a decreased actomyosin-ATPase activity can only in part contribute to the 30% lower energy turnover during force development found for fast-twitch skeletal muscle of hypothyroid rats. Moreover, the increase in twitch force by hypothyroidism cannot be explained by a change in myosin P-light chain phosphorylation. Isometric twitch tension potentiation after a 2 s tetanus and during low-frequency repetitive stimulation was reduced (up to -60%) in muscles of hypothyroid rats, which may well be related to the lower extent of P-light chain phosphorylation in hypothyroids.
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PMID:Structural and functional aspects of the actomyosin complex from fast-twitch muscle of euthyroid and hypothyroid rats. 296 Sep 52

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

Isoforms of myosin heavy chain (MHC) and myosin light chain (MLC) influence contractile kinetics of skeletal muscle. We previously showed that the four major skeletal muscle fibre types in Rana pipiens (type 1, type 2, type 3 and tonic; amphibian nomenclature) contain four unique MHC isoforms. In the present study we defined the MLCs expressed in each of these R. pipiens fibre types. The MLC composition of single MHC-typed fibres was determined from western blots using a panel of monoclonal MLC antibodies. A total of seven MLCs were identified, including four types of MLC1, two of MLC2 and a single MLC3. Twitch fibre types (types 1, 2 and 3) expressed MLC1(f) and MLC2(f), while tonic fibres contained a unique set of isoforms, MLC1(Ta), MLC1(Tb) and MLC2(T). MLC3 was expressed primarily in type 1, type 1-2 and type 2 fibres. Surprisingly, some frogs displayed a striking pattern of MLC expression where a unique isoform of MLC1 (MLC1(x)) was coexpressed along with the normal MLC1 isoform(s) in all fibre types. MLC1(x) was either expressed in all fibres of a given frog or was completely absent. The intraspecific polymorphism in MLC1 expression is likely to have a genetic basis, but is unlikely to be caused by allelic variation. The ratio of MLC3/MLC1 increased in direct proportion to the percentage of type 1 MHC, but was only weakly correlated. The variability in MLC3/MLC1 within a fibre type was extremely large. Both the MHC isoform and MLC3/MLC1 ratio varied significantly between 1 mm segments along the length of fibres. For all segments combined, MLC3/MLC1 increased with the percentage of type 1 MHC, but the correlation between segments was weaker than between fibres.
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PMID:Identification of myosin light chains in Rana pipiens skeletal muscle and their expression patterns along single fibres. 1181 48

We have studied the contractile properties, structure, fiber-type composition, and myosin heavy chain (MyHC) expression pattern of regenerating and intact soleus muscles of adult CBA/J mice treated with cyclosporin A (CsA) or vehicle solutions (Cremophor, saline). A comparison of muscles after 4-7 weeks drug application with those receiving vehicle showed that the isometric contractile force of intact drug-treated muscles was reduced (tetanus, -21%; twitch, -34%) despite normal mass and muscle cross-sectional area. The frequency of fast-twitch fibers was increased, whereas no innervation deficits, histopathological alterations, or changes in fiber numbers were observed. Regeneration after cryolesion of the contralateral soleus proceeded more slowly in CsA-treated than in vehicle-treated animals. Despite this, when muscle properties reached mature levels (4-7 weeks), muscle mass recovery was better in CsA-treated animals (30% higher weight, 50% more fiber profiles in cross-sections). The force production per unit cross-sectional area was deficient, but not the maximum tension. Twitch time-to-peak and half-relaxation time were shorter than controls correlating with a predominance of fast-twitch fibers (98% Type II fibers versus 16%-18% in control muscles) and fast MyHC isoforms. Partial reversal of this fast phenotype and an increase in muscle force were observed when the animals were left to recover without treatment for 5-8 weeks after CsA application over 7 weeks. The high numbers of fiber profiles in CsA-treated regenerated muscles and increased mass remained unchanged after withdrawal. Thus, CsA treatment has a hyperplastic effect on regenerating muscles, and drug-induced phenotype alterations are much more prominent in regenerated muscles.
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PMID:Contractile properties, structure and fiber phenotype of intact and regenerating slow-twitch muscles of mice treated with cyclosporin A. 1201 14

Activation of either the calcineurin or the extracellular signal-regulated kinase (ERK1/2) pathway increases the percentage of slow fibres in vivo suggesting that both pathways can regulate fibre phenotypes in skeletal muscle. We investigated the effect of calcineurin blockade with cyclosporin A and mitogen-activated protein kinase kinase (MEK1/2) blockade with U0126 upon myosin heavy chain (MHC) isoform mRNA levels and activities of metabolic enzymes after 1 day, 3 days and 7 days of treatment in primary cultures of spontaneously twitching rat skeletal muscle. U0126 treatment significantly decreased MHC Ibeta mRNA levels and significantly increased MHC IIX, MHC IIB, embryonal MHC and perinatal MHC mRNA levels when compared to control. In addition, U0126 treatment significantly increased lactate dehydrogenase, creatine kinase, hexokinase, malate dehydrogenase and beta-hydroxyacyl-CoA dehydrogenase activities above control values while a significant reduction in the percentage of pyruvate dehydrogenase in the active form was also observed. Calcineurin blockade significantly decreased both MHC Ibeta and embryonal mRNA levels below control and significantly increased MHC IIX mRNA levels. Significant increases in the activities of both lactate dehydrogenase and creatine kinase above control values were also seen following cyclosporin A treatment. In conclusion, the results suggest that calcineurin upregulates slow-fibre genes and suppresses fast-fibre genes. Similarly, the ERK1/2 pathway upregulates slow-fibre MHC and suppresses fast-fibre MHC isoforms. However, the effect on enzyme activities is not fibre-type specific. The effect of U0126 on the percentage of pyruvate dehydrogenase in the active form suggests that the ERK1/2 pathway may also be involved in regulation of the phosphorylation state of this enzyme.
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PMID:Blockades of mitogen-activated protein kinase and calcineurin both change fibre-type markers in skeletal muscle culture. 1246 48

The purpose of this study was to determine whether induced expression of the Ca2+ buffering protein parvalbumin (PV) in slow-twitch fibres would lead to alterations in physiological, biochemical and molecular properties reflective of a fast fibre phenotype. Transgenic (TG) mice were generated that overexpressed PV in slow (type I) muscle fibres. In soleus muscle (SOL; 58 % type I fibres) total PV expression was 2- to 6-fold higher in TG compared to wild-type (WT) mice. Maximum twitch and tetanic tensions were similar in WT and TG but force at subtetanic frequencies (30 and 50 Hz) was reduced in TG SOL. Twitch time-to-peak tension and half-relaxation time were significantly decreased in TG SOL (time-to-peak tension: 39.3 +/- 2.6 vs. 55.1 +/- 4.7 ms; half-relaxation time: 42.1 +/- 3.5 vs. 68.1 +/- 9.6 ms, P < 0.05 for TG vs. WT, respectively; n = 8-10). There was a significant increase in expression of type IIa myosin heavy chain (MHC) and ryanodine receptor at the mRNA level in TG SOL but there were no differences in MHC expression at the protein level and thus no difference in fibre type. Whole muscle succinate dehydrogenase activity was reduced by 12 +/- 0.4 % in TG SOL and single fibre glycerol-3-phosphate dehydrogenase activity was decreased in a subset of type IIa fibres. These differences were associated with a 64 % reduction in calcineurin activity in TG SOL. These data show that overexpression of PV, resulting in decreased calcineurin activity, can alter the functional and metabolic profile of muscle and influence the expression of key marker genes in a predominantly slow-twitch muscle with minimal effects on the expression of muscle contractile proteins.
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PMID:Alterations in slow-twitch muscle phenotype in transgenic mice overexpressing the Ca2+ buffering protein parvalbumin. 1256 45

Previous studies show that cessation of resistance training, commonly known as "detraining," is associated with strength loss, decreased neural drive, and muscular atrophy. Detraining may also increase the expression of fast muscle myosin heavy chain (MHC) isoforms. The present study examined the effect of detraining subsequent to resistance training on contractile performance during slow-to-medium velocity isokinetic muscle contraction vs. performance of maximal velocity "unloaded" limb movement (i.e., no external loading of the limb). Maximal knee extensor strength was measured in an isokinetic dynamometer at 30 and 240 degrees/s, and performance of maximal velocity limb movement was measured with a goniometer during maximal unloaded knee extension. Muscle cross-sectional area was determined with MRI. Electromyographic signals were measured in the quadriceps and hamstring muscles. Twitch contractions were evoked in the passive vastus lateralis muscle. MHC isoform composition was determined with SDS-PAGE. Isokinetic muscle strength increased 18% (P < 0.01) and 10% (P < 0.05) at slow and medium velocities, respectively, along with gains in muscle cross-sectional area and increased electromyogram in response to 3 mo of resistance training. After 3 mo of detraining these gains were lost, whereas in contrast maximal unloaded knee extension velocity and power increased 14% (P < 0.05) and 44% (P < 0.05), respectively. Additionally, faster muscle twitch contractile properties along with an increased and decreased amount of MHC type II and MHC type I isoforms, respectively, were observed. In conclusion, detraining subsequent to resistance training increases maximal unloaded movement speed and power in previously untrained subjects. A phenotypic shift toward faster muscle MHC isoforms (I --> IIA --> IIX) and faster electrically evoked muscle contractile properties in response to detraining may explain the present results.
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PMID:Changes in the human muscle force-velocity relationship in response to resistance training and subsequent detraining. 1573 98

Previously, we showed that artificial rearing using the "pup in a cup" model results in decreased tongue activity and caused some minor alterations in the tongue retrusor musculature. However, the artificial rearing time frame previously chosen was brief (11 days). The purpose of the present investigation was to extend the artificial rearing period from postnatal days 3 to 21 (P21) to determine whether significant alterations occur as a result of this reduced tongue use. Several changes in contractile properties due to the artificial rearing process were observed, which fully recovered by postnatal days 41 to 42 (P41-2). These changes included a shorter twitch contraction time, shorter twitch half-relaxation time, and decreased fatigue resistance. Styloglossus muscle exhibited more neonatal myosin heavy chain (MHC) isoform at P21 for the artificially reared (AR) group. Changes that were persistent at P41-2 were also observed. Maximum tetanic tension was lower for the AR group at P21 and P41-2 compared with their dam-reared counterparts. Twitch tension was also lower by P41-2 in the AR group. At P41-2, the AR group exhibited an increase in MHC IIa and a decrease in MHC IIb for the styloglossus muscle. In addition, the AR group exhibited a decreased MHC IIb for the long head of the biceps brachii at P41-2. Our results are similar to other models of hindlimb immobilization and suspension. By extending our artificial rearing period, this reduced tongue activity induced acute changes and alterations in the tongue retrusor musculature that persisted into early adulthood.
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PMID:Contractile properties and myosin heavy chain composition of rat tongue retrusor musculature show changes in early adulthood after 19 days of artificial rearing. 1680 31

Dynamic resistance training increases the force and speed of muscle contraction, but little is known about modifications to the contractile properties of the main physiological types of motor units (MUs) that contribute to these muscle adaptations. Although the contractile profile of MU muscle fibers is tightly coupled to myosin heavy chain (MyHC) protein expression, it is not well understood if MyHC transition is a prerequisite for modifications to the contractile characteristics of MUs. In this study, we examined MU contractile properties, the mRNA expression of MyHC, parvalbumin, and sarcoendoplasmic reticulum Ca2+ pump isoforms, as well as the MyHC protein content after 5 wk of volitional progressive weight-lifting training in the medial gastrocnemius muscle in rats. The training had no effect on MyHC profiling or Ca2+-handling protein gene expression. Maximum force increased in slow (by 49%) and fast (by 21%) MUs. Within fast MUs, the maximum force increased in most fatigue-resistant and intermediate but not most fatigable MUs. Twitch contraction time was shortened in slow and fast fatigue-resistant MUs. Twitch half-relaxation was shortened in fast most fatigue-resistant and intermediate MUs. The force-frequency curve shifted rightward in fast fatigue-resistant MUs. Fast fatigable MUs fatigued less within the initial 15 s while fast fatigue-resistant units increased the ability to potentiate the force within the first minute of the standard fatigue test. In conclusion, at the early stage of resistance training, modifications to the contractile characteristics of MUs appear in the absence of MyHC transition and the upregulation of Ca2+-handling genes.
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PMID:Contractile properties of motor units and expression of myosin heavy chain isoforms in rat fast-type muscle after volitional weight-lifting training. 2753 95


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