Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have reported that the maximal velocity of shortening and myofibrillar adenosine triphosphatase (ATPase) activity of antigen-sensitized airway smooth muscle are higher than that of nonsensitized airway smooth muscle (Kong, S. K., R. P. C. Shiu, and N. L. Stephens. J. Appl. Physiol. 60: 92-94, 1986). To extend these studies, we attempted to determine whether the increased myofibrillar ATPase activity from sensitized airway smooth muscle was associated with either a change in distribution of two myosin heavy chain isozymes or an increase in myosin light chain phosphorylation. Myosin heavy chain isozymes from both control and sensitized airway smooth muscle were separated by 4% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Gels were analyzed by densitometry, which indicated that isozyme band pattern of sensitized airway smooth muscle was not different from that of the control. The maximal levels of phosphorylated myosin light chain from whole cell homogenates of sensitized and control tracheal smooth muscles were 0.65 +/- 0.029 (n = 6) and 0.40 +/- 0.025 mol Pi/mol light chain (n = 6), respectively. The degree of phosphorylation of myosin light chain of sensitized airway smooth muscle was significantly higher than that of the control (P less than 0.05). This study also indicated that increased myofibrillar ATPase activity in sensitized tracheal smooth muscle was correlated with phosphorylation of myosin light chain.
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PMID:Increased myosin phosphorylation in sensitized canine tracheal smooth muscle. 214 57

The spontaneous contractions of cultured chick skeletal muscle fibers were abolished by growth of cultures in the presence of tetrodotoxin (TTX). Inhibition of the contractile activity of cultured myofibers was associated with a marked reduction in the rate of azide-insensitive, ATP-dependent Ca2+ uptake by the total particulate fraction of cell homogenates and by purified sarcoplasmic reticulum. Myosin heavy chain (MHC) accumulation and azide-insensitive, ATP-dependent Ca2+ uptake into a total cell membrane fraction were measured simultaneously in the same culture dish. A decrease in the activity of the ATP-dependent Ca2+ uptake system preceded a significant reduction in MHC content of contraction-inhibited cultures. The reduced rate of Ca2+ uptake observed in the sarcoplasmic reticulum from TTX-treated cultures paralleled a decrease in the amount of enzymatically active Ca2+-transport ATPase. The cellular concentration of the ATPase was estimated from a measurement of the concentration of the Ca2+-dependent, hydroxylamine-sensitive, steady state level of phosphorylated intermediate formed in culture microsomes. In contrast to the changes observed in activity of the sarcoplasmic reticulum ATPase and MHC content of TTX-treated cultures, neither the specific activity of creatine kinase nor the accumulation of the MM isoenzyme were affected. It is therefore concluded that the contractile activity of muscle has a selective effect on the maintenance of the adult skeletal muscle phenotype.
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PMID:Effect of tetrodotoxin relaxation of cultured skeletal muscle on the sarcoplasmic reticulum Ca2+-transport ATPase. 622 Sep 16

Myosin heavy chain isoforms of the ventricular myocardium from crucian carp (Carassius carassius L.) hearts were analyzed in different times of the year by gradient sodium dodecyl sulfate-polyacrylamide gel electrophoresis [K. A. Esser, M. O. Boluyt, and T. P. White, Am. J. Physiol. 255 (Heart Circ. Physiol. 24): H659-H663, 1988]. In winter only one myosin heavy chain type was present, but in summer about one-half of the winter myosin was replaced by more slowly moving summer myosin. The occurrence of summer myosin correlated with seasonal changes in water temperature of the pond, where the fish were caught. Furthermore, the heavy chain composition of the heart was altered by temperature acclimation in the laboratory: cold-acclimated (2 degrees C) fish had only winter myosin, but warm-acclimated (22 degrees C) fish had both summer and winter myosin in about equal amounts. Myosin adenosinetriphosphatase activity of the hearts containing both summer and winter myosin was higher than that of hearts containing only winter myosin. Functionally, changes in myosin heavy chain composition were associated with inverse thermal acclimation in the heart rate. Warm-acclimated fish had higher in vitro heart rate and shorter contraction duration than cold-acclimated animals. Present findings suggest that changes in myosin heavy chain composition together with concomitant changes in Ca2+ activation of contraction make possible large seasonal alterations in the activity of crucian carp hearts. These adjustments are needed to adapt the cardiovascular system to winter hibernation and summer activity, which are dictated by seasonally bound changes in environmental conditions.
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PMID:Seasonal and temperature-induced changes in myosin heavy chain composition of crucian carp hearts. 781 Jul 67

1. Myosin heavy chain (HC) and light chain (LC) isoforms are expressed in a tissue-specific and developmentally-regulated manner in human skeletal muscle. 2. At least seven myosin HC isoforms are expressed in skeletal muscle of the adult. 3. Histochemically-delineated fibre types (based on the stability of myofibrillar actomyosin adenosine triphosphatase activity) in limb muscles correlate with the myosin HC content. 4. Alterations in the phenotypic expression of myosin provides a mechanism of adaptation to stresses placed upon the muscle (e.g. increased and decreased usage).
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PMID:Myosin polymorphism and differential expression in adult human skeletal muscle. 828 47

1. ATP consumption and force development were determined in single skinned muscle fibres of the rat at 12 degrees C. Myofibrillar ATPase consumption was measured photometrically from NADH oxidation which was coupled to ATP hydrolysis. Myosin heavy chain (MHC) and light chain (MLC) isoforms were identified by gel electrophoresis. 2. Slow fibres (n = 14) containing MHCI and fast fibres (n = 18) containing MHCIIB were compared. Maximum shortening velocity was 1.02 +/- 0.63 and 3.05 +/- 0.23 lengths s-1, maximum power was 1.47 +/- 0.22 and 9.59 +/- 0.84 W l-1, and isometric ATPase activity was 0.034 +/- 0.003 and 0.25 +/- 0.01 mM s-1 in slow and in fast fibres, respectively. 3. In fast as well as in slow fibres ATP consumption during shortening increased above isometric ATP consumption. The increase was much greater in fast fibres than in slow fibres, but became similar when expressed relative to the isometric ATPase rate. 4. Efficiency was calculated from mechanical power and free energy change associated with ATP hydrolysis. Maximum efficiency was larger in slow than in fast fibres (0.38 +/- 0.04 versus 0.28 +/- 0.03) and was reached at a lower shortening velocity. 5. Within the group of fast fibres efficiency was lower in fibres which contained more MLC3f. We conclude that both MHC and essential MLC isoforms contribute to determine efficiency of chemo-mechanical transduction.
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PMID:Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibres of the rat. 926 23

The aim of this study was to evaluate the potential mechanisms underlying the improved contractility of the diaphragm (Dia) in adult intact male hamsters after nandrolone (Nan) administration, given subcutaneously over 4 wk via a controlled-release capsule (initial dose: 4.5 mg. kg-1. day-1; with weight gain, final dose: 2.7 mg. kg-1. day-1). Control (Ctl) animals received blank capsules. Isometric contractile properties of the Dia were determined in vitro after 4 wk. The maximum velocity of unloaded shortening (Vo) was determined in vitro by means of the slack test. Dia fibers were classified histochemically on the basis of myofibrillar ATPase staining and fiber cross-sectional area (CSA), and the relative interstitial space was quantitated. Ca2+-activated myosin ATPase activity was determined by quantitative histochemistry in individual diaphragm fibers. Myosin heavy chain (MHC) isoforms were identified electrophoretically, and their proportions were determined by using scanning densitometry. Peak twitch and tetanic forces, as well as Vo, were significantly greater in Nan animals compared with Ctl. The proportion of type IIa Dia fibers was significantly increased in Nan animals. Nan increased the CSA of all fiber types (26-47%), whereas the relative interstitial space decreased. The relative contribution of fiber types to total costal Dia area was preserved between the groups. Proportions of MHC isoforms were similar between the groups. There was a tendency for increased expression of MHC2B with Nan. Ca2+-activated myosin ATPase activity was increased 35-39% in all fiber types in Nan animals. We conclude that, after Nan administration, the increase in Dia specific force results from the relatively greater Dia CSA occupied by hypertrophied muscle fibers, whereas the increased ATPase activity promotes a higher rate of cross-bridge turnover and thus increased Vo. We speculate that Nan in supraphysiological doses have the potential to offset or ameliorate conditions associated with enhanced proteolysis and disordered protein turnover.
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PMID:Alterations in diaphragm contractility after nandrolone administration: an analysis of potential mechanisms. 1006 14

In the present study we have investigated the role of actin-myosin interactions in regulating focal adhesion assembly in Xenopus XR1 glial cells. Actin-myosin interactions, stress fiber formation, and focal adhesion assembly are thought to allow cells to exert tension in the surrounding extracellular matrix, a process essential during morphogenesis and wound healing. Immunocytochemical analysis has revealed that myosin heavy chain-A (MHC-A), the predominant isoform in XR1 cells, was distributed in a filamentous pattern in the central region but was more diffuse towards the cell periphery. Myosin heavy chain-A-like immunoreactivity (IR) partially colocalized with phalloidin stained F-actin microfilaments in XR1 cells but not with microtubules. Furthermore, MHC-A-IR colocalized with immunoreactivity for beta1 integrin receptors and vinculin at focal adhesions located more centrally along the ventral surface of the cells. The partial colocalization of MHC-A with the F-actin cytoskeleton, as well as at focal adhesions, provides evidence that actin-myosin interactions may be involved in regulating focal adhesion assembly and stabilization. To examine this possibility, we have used drugs shown to inhibit cell contractility: the kinase inhibitors H7 and HA100, and 2,3-butanedione 2-monoxime (BDM), which inhibits muscle and nonmuscle ATPase activity. Compared to control cultures, those treated with the inhibitors exhibited a dose-dependent decrease in the percentage of cells that displayed focal adhesions. In addition, these cells also displayed disrupted actin cytoskeletons and a similar disruption in myosin filaments. Taken together, these results provide evidence for an important role of actin-myosin generated forces during focal adhesion assembly in glial cells.
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PMID:Disruption of actin-myosin interactions results in the inhibition of focal adhesion assembly in Xenopus XR1 glial cells. 1034 Jul 65

Myosin heavy chain (MHC) isoform composition and Ca2+ Mg2+ dependent ATPase activity were determined in myofibrils prepared from skeletal muscles (diaphragm, soleus, plantaris and tibialis anterior) of euthyroid (C), hypothyroid (Tx) and hyperthyroid (T3) rats. Direct comparison between T3 and Tx gave an indication of the maximal effect of thyroid hormones. Significant differences in MHC-1 and MHC-2B proportions and in ATPase activity were found in all muscles. The difference in MHC-2A/X proportion was significant only in soleus, diaphragm and plantaris. When T3 and C were compared, significant variations in MHC isoform composition were found only in plantaris and diaphragm. The comparison between Tx and C showed significant differences in MHC isoform distribution and in ATPase activity in most muscles. The differences in ATPase activity among muscles and among thyroid states were consistent with those in MHC isoform distribution. From the correlations between ATPase activity and MHC isoform distribution the enzymatic activities of individual MHC isoforms were calculated. The results indicate that MHC isoform distribution is controlled by thyroid state in all skeletal muscles and that changes in MHC isoforms distribution are accompanied by proportional changes in ATPase activity.
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PMID:Thyroid hormone regulation of MHC isoform composition and myofibrillar ATPase activity in rat skeletal muscles. 1041 57

The impact of a targeted disruption of the Igf1 gene, encoding the insulin-like growth factor I (IGF-I), on diaphragm (DIA) cellularity was studied in 2-mo-old homozygous mutant [IGF-I(-/-)] mice and their wild-type [WT; i.e., IGF-I(+/+)] littermates. DIA fiber types were classified histochemically. DIA fiber cross-sectional areas (CSA) were determined from digitized muscle sections, and fiber succinate dehydrogenase (SDH) activity was determined histochemically using a microdensitometric procedure. An acidic ATPase reaction was used to visualize capillaries. Myosin heavy chain (MyHC) isoforms were identified by SDS-PAGE, and their proportions were determined by scanning densitometry. The body weight of IGF-I(-/-) animals was 32% that of WT littermates. DIA fiber type proportions were unchanged between the groups. The CSAs of types I, IIa, and IIx DIA fibers of IGF-I(-/-) mutants were 63, 68, and 65%, respectively, those of WT animals (P < 0.001). The DIA thickness and the number of fibers spanning its entire thickness were reduced by 36 and 25%, respectively, in IGF-I(-/-) mice (P < 0. 001). SDH activity was significantly increased in all three types of DIA fibers of IGF-I(-/-) mutants (P < 0.05). The number of capillaries per fiber was reduced approximately 30% in IGF-I(-/-) animals, whereas the capillary density was preserved. The proportions of MyHC isoforms were similar between the groups. Muscle hypoplasia likely reflects the importance of IGF-I on cell proliferation, differentiation, and apoptosis (alone or in combination) during development, although reduced cell size highlights the importance of IGF-I on rate and/or maintenance of DIA fiber growth in the postnatal state. Reduced capillarity may result from both direct and indirect influences on angiogenesis. Improved oxidative capacity likely reflects DIA compensatory mechanisms in IGF-I(-/-) mutants.
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PMID:Influences of IGF-I gene disruption on the cellular profile of the diaphragm. 1075 Dec 6

Myosin heavy chain (MHC) expression was determined immunohistochemically in individual muscle fibre types characterised by activities of ATPase and the key oxidative and glycolytic enzymes in rat ocular medial rectus (MR) muscles. In the global layer (GL), glycolytic activity of muscle fibres was higher and oxidative activity lower, than in the orbital layer (OL). Muscle fibres in the former displayed rosette-like organisation with a slow fibre surrounded by several fast fibres, which expressed either MHCIIa or MHCIIb, but many co-expressed both isoforms. In the OL some slow fibres co-expressed MHCIIa. Extraocular MHC isoform (MHCeom) could not be determined immunohistochemically and no pure MHCIIx/d containing fibres were found, suggesting that these isoforms, demonstrated electrophoretically, are co-expressed with others. Slow muscle fibres in both layers co-expressed MHCbeta slow, MHCalpha cardiac and MHC-slow tonic. Neonatal isoform (MHCneo) was co-expressed in several fast and slow muscle fibres in the orbital, but not global layer. Slow fibres in the GL displayed very low oxidative activity. Electrophoretic analysis of ocular MR muscle homogenates revealed that about 50% of total MHC was MHCIIb, MHCeom was quite prominent (25%), and MHCIIa, MHCIIx/d and MHCI contributed each about 8%. MHCneo, MHCslow tonic and MHCalpha cardiac could not be identified as separate bands.
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PMID:Fibre types and myosin heavy chain expression in the ocular medial rectus muscle of the adult rat. 1139 57


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