Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Undifferentiated type 2C fibers, which are dark on ATPase staining with both alkaline and acid preincubation, comprised on average 16.1% of the muscle fibers in 12 patients with Duchenne muscular dystrophy (DMD). Many of type 2C fibers had characteristics of regenerating fibers: basophilic cytoplasm, vesicular nuclei with occasional prominent nucleoli, high alkaline phosphatase and nonspecific esterase activity, and also high oxidative enzyme activity at the periphery of the fiber. A localized high acetylcholinesterase activity suggested the presence of a neuromuscular junction in some of the type 2C fibers. In serial sections, histochemical reactions characteristic of the type 2C fiber were present in segments of a single fiber, which in other parts was either a type 1 or a type 2 fiber. Since most of the opaque (hyaline, dark) fibers, which previously have been thought to be precursors of necrotic fibers, behaved as differentiated type 1 or type 2 fibers, the presence of type 2C fibers in DMD may not reflect "dedifferentiation" of fiber type, but rather indicate an active regenerating process. It remains unknown whether the type 2C fiber segments in DMD develop into fully differentiated functional fibers or remain as incompletely regenerated fibers.
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PMID:The significance of type 2C muscle fibers in Duchenne muscular dystrophy. 616 59

Limitations in the ability of the human visual system to assess accurately the relative staining densities of individual fibers in muscle tissue stained for myosin. ATPase can complicate the objective evaluation of fiber type populations. In this study a novel approach is employed which utilizes human visual capabilities to provide accurate fiber classification. Using this approach, the ability of five ATPase staining techniques to discriminate fiber type categories in single samples of human normal and Duchenne dystrophic skeletal muscle is evaluated, as is the consistency of the fiber type classifications between stains. While no major discrepancies in fiber typing were observed in the sample of normal muscle, significant differences in classification, along with a decrease in the ability to discriminate fiber types were noted in the sample of Duchenne muscular dystrophy. For the most part, these discrepancies were resolved by a re-interpretation of the staining characteristics of fibers in one stain.
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PMID:Discrimination and consistency of five myosin ATPase stains in human normal and Duchenne dystrophic muscle. 618 41

Immature fibers in Duchenne muscular dystrophy (DMD) and congenital muscular dystrophies (CMD) were compared with human fetal muscles and experimentally-induced regenerating muscle fibers using the acridine orange (AO) technique on fluorescent microscopy and histochemical methods. Strong AO activity was observed on immature fibers in dystrophies and on experimentally-induced fibers in the early stages of regeneration. These young fibers showed type 2C histochemical reactions on ATPase stains. Human fetal muscles failed to show these fibers which were seen in the muscular dystrophies and the experimental regenerating muscle. From these results it is concluded that immature fibers in muscular dystrophies are early stages of regenerating fibers and not maturationally arrested fetal muscle fibers. In addition, these immature fibers formed small groups composed of 10 to 50 fibers in muscular dystrophies and sometimes large groups in CMD. It is suggested that the investigation of immature fibers and their grouping is quite important for revealing the pathogenesis of the muscular dystrophies.
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PMID:Maturational defect of regenerating muscle fibers in cases with Duchenne and congenital muscular dystrophies. 619 37

Myosin ATPase activity was fine-structurally examined in various skeletal muscle lesions including atrophy, degenerations, necrosis, "deltashaped subsarcolemmal lesion", and apparently normal fibers from seven patients of Duchenne muscular dystrophy (D M D). The enzyme activity was almost completely lost in the foci of necrosis, and more or less markedly diminished in various kinds of degenerations, while it was well preserved in the apparently normal and simply atrophic fibers. The results suggested that there were two different lesions in wasting of the skeletal muscles in D M D; necrotic process with degenerations in which myosin-ATPase activity was affected and simply atrophic process which had little influence on the enzyme activity. The former lesion might be related with direct or indirect damages such as proteolysis, while the latter seemed to be an expression of basically different process such as disuse or denervation, or a more mild expression basically of the same process ultimately resulting in necrosis.
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PMID:Fine structural histochemistry of myosin-ATPase activity in the skeletal muscles of Duchenne muscular dystrophy. 621 29

Erythrocyte flexibility measured by a polycarbonate membrane filtration method showed increased fragility (265 +/- 163 Hb mg/l vs. controls 86 +/- 72 Hb mg/l; mean +/- SD; P less than 0.0025) and increased rigidity (123 +/- 96 mm Hg vs. 79 +/- 19 mm Hg; P less than 0.05) in patients with congenital myotonia, while both parameters were normal in patients with Duchenne muscular dystrophy or with myotonic dystrophy. Erythrocyte ghosts obtained from patients with MyD displayed highly significant increases in both (Na+ + K+)-ATPase and (Ca2+ + Mg2+)-ATPase activities (P less than 0.005) and to a lesser extent in Mg2+-ATPase activity (P less than 0.05), while no difference was seen between patients with DMD and age-matched controls. The efflux of Ca2+ was increased from erythrocytes of patients with DMD as compared to age-matched controls (82 +/- 2% vs. 70 +/- 4%; P less than 0.005), while no difference was detected between patients with MyD and age-matched controls.
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PMID:Erythrocyte flexibility, ATPase activities and Ca efflux in patients with Duchenne muscular dystrophy, myotonic muscular dystrophy and congenital myotonia. 622 Oct 82

Erythrocyte ghost membranes have been prepared by two different methods from patients with Duchenne muscular dystrophy (DMD), carriers of DMD, patients with other neuromuscular diseases, and normal individuals. The susceptibility of the membrane Na+,K+-adenosine triphosphatase (ATPase) to the cardiac glycoside, ouabain, has been investigated using various assay conditions. A stimulation of the enzyme has not been detected under any of the conditions employed. Using either a "high salt" (100 mM NaCl, 20 mM KCl) or a "low salt" (1 mM NaCl, 2 mM KCl) assay in the presence of EGTA a reduced susceptibility of the enzyme to ouabain was observed in preparations from patients with DMD compared with those from normal individuals. This behaviour was not manifest in preparations from NAD carriers or from patients with other neuromuscular diseases. The response of the erythrocyte membrane Na+,K+-ATPase activity to changes in temperature has also been investigated. The temperature response of the enzyme from DMD and DMD carrier preparations was indistinguishable from that of normal preparations. In all cases a break in the Arrhenius plot occurred at 21 degrees C.
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PMID:Erythrocyte ghost Na+,K+-adenosine triphosphatase in Duchenne muscular dystrophy. 624 54

Previous studies in our laboratory had demonstrated alterations in the physical state of membrane proteins in erythrocytes in Huntington's disease. In order to assess the specificity of our findings, the results of electron spin resonance studies of protein and lipid components, scanning electron-microscopic studies, enzymatic analyses of membrane-bound sodium plus potassium stimulated, magnesium-dependent adenosine triphosphatase and protein kinase, and cell deformability studies of erythrocyte membranes have been performed in the neurological disorders, Huntington's disease, Friedreich's ataxia, Alzheimer's disease, amyotrophic lateral sclerosis, and myotonic and Duchenne muscular dystrophy. Comparison of the results revealed that alterations in the biophysical and biochemical states of erythrocyte membranes in each disorder are specific to the particular disease state with the exception of those in Friedreich's ataxia and Alzheimer's disease. In the latter instance, the clinical and pathological alterations suggest that these two diseases have different primary defects. Our studies suggest that the molecular basis of each disease is different. In addition, the results suggest that biophysical and biochemical investigations of extraneural tissue in Huntington's disease and other neurological disordes have the potential of clarifying the molecular mechanisms by which these diseases arise.
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PMID:Specificity of biophysical and biochemical alterations in erythrocyte membranes in neurological disorders--Huntington's disease, Friedreich's ataxia, Alzheimer's disease, amyotrophic lateral sclerosis, and myotonic and duchenne muscular dystrophy. 625 Nov 75

We studied the Na+ + K+ ATPase activity of erythrocyte membranes from patients with Duchenne muscular dystrophy (DMD). Samples from patients and controls were obtained at almost the same time on the same day and processed simultaneously. Difference of anticoagulants, extent of washing the red cells, mechanical or osmotic disruption of the cells, presence or absence of EDTA in the washing solution of the ghosts, intentional removal of the peripheral proteins of the membranes, addition of DMD plasma to the assay system, and different temperatures of membrane storage caused no significant differences between DMD and control in Na+ + K+ ATPase or in response of the enzyme to ouabain.
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PMID:Na+ + K+ ATPase of erythrocyte membranes in Duchenne muscular dystrophy. 625 57

Erythrocyte ghost preparations have been prepared from blood of Duchenne patients (DMD), female carriers of the disease and controls. Arrhenius plots of Na+, K+-ATPase activity of these membrane preparations show a biphasic response for controls. For 75% of DMD and carriers the response is monophasic. This is not an inherent property of the membrane since it can vary over time in the one individual and it can be induced in normal membranes by preincubation with DMD plasma. Arrhenius plots of AChE activity showed no such difference between the three sources of blood.
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PMID:Thermodynamic behaviour of membrane enzymes in Duchenne muscular dystrophy. 630 27

Cores were produced in type 1 muscle fibers by tenotomy of rat soleus muscle. The morphology and histochemistry of the muscle fibers was established by light microscopy on cryostat sections stained for hematoxylin-eosin or myofibrillar ATPase and on semithin plastic sections. The ultrastructure was visualized on thin plastic sections. On 6 micrometers of freeze-dried cryosections, energy dispersive X-ray microanalysis was performed on muscle fibers visualized in the scanning-transmission mode of electron microscopy. This procedure permitted quantification of different intracellular elements such as sodium (Na), chlorine (Cl), potassium (K), magnesium (Mg), sulphur (S), and phosphorus (P). Spectra from core fibers could easily be compared with those of normal fibers. A conspicuous finding was an increased Na and Cl content and a decreased K content in core fibers compared to normal fibers. It is known that core fibers produced after tenotomy exhibit distinct changes in plasma membrane morphology similar to that found in Duchenne muscular dystrophy (DMD). The results in this study point to a change in normal intracellular ion composition which could be a result of a deficiency of mechanisms maintaining normal membrane ion gradients.
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PMID:Changes in elemental composition of single muscle fibers following tenotomy of the rat soleus muscle. 663 62


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