Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cation-stimulated adenosine triphosphatase (ATPase) activities of erythrocyte ghosts and erythrocyte ghost plasma membrane fragments of patients with Duchenne muscular dystrophy (DMD) were compared with activities in age-matched normal male controls. DMD Mg++-stimulated ATPase activity was within the normal range. The specific activity of DMD erythrocyte ghost Na+,K+-stimulated, Mg++-dependent ATPase was also normal, and was inhibited by 10(-4) M ouabain to an extent comparable with controls. Ca++-stimulated, Mg++-dependent ATPase activity of DMD erythrocyte ghost plasma membrane fragments, assayed at 0.5 mM free Ca++, was 21% above that in age-matched male controls (n = 22, 2-tailed paired t-test, P less than 0.01). Kinetic studies indicated that the DMD erythrocyte Ca++-stimulated, Mg++-dependent ATPase has greater affinity for MgATP than the enzyme in control erythrocytes.
 ...
PMID:Erythrocyte cation-activated adenosine triphosphatases in Duchenne muscular dystrophy. 14 27

The adenosine triphosphatase activity of erythrocyte ghosts from patients with Duchenne muscular dystrophy was inhibited by 10(-4) M ouabain to a smaller extent than in normals, when measured in the presence of either high or low concentrations of sodium or potassium ions. The inhibition by ouabain of the enzyme in normal ghosts, measured with low sodium or potassium ions, was less if the erythrocytes were first incubated with plasma from Duchenne patients than if incubated with normal plasma. Similar results were obtained when the ghosts themselves were incubated with Duchenne or normal plasma before assay.
 ...
PMID:Effect of ouabain upon erythrocyte membrane adenosine triphosphatase in Duchenne muscular dystrophy. 14 73

Rapid advances in the molecular genetics of Duchenne muscular dystrophy (DMD) and the discovery and localization of the gene product dystrophin has brought new hope that successful treatment for this disease may not be too far away. Dystrophin has been postulated to have a mechanical function, helping to resist stress associated with muscle contraction. The presence of dystrophin in low concentrations in muscle cells, its expression in nervous tissue and the observation that hypercontraction of the sarcomeres precedes membrane rupture make the hypothesis unlikely. On the basis of an analogy with a cytoskeletal protein ankyrin, which is associated with the sodium/potassium adenosine triphosphatase (ATPase) in the kidney, it is possible that dystrophin deficiency leads initially to an increased but inefficient calcium-ATPase activity, which pumps calcium out of the cell. Partial failure of the pump would result in intracellular accumulation of calcium, hypercontractions of the sarcomeres, rupture of the cell membrane, massive influx of calcium and cell necrosis.
 ...
PMID:Pathogenesis of Duchenne muscular dystrophy: the calcium hypothesis revisited. 149 54

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.
 ...
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.
 ...
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