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)

Enzyme activities of ATPases and acetylcholinesterase from isolated erythrocyte membranes (ghosts) were investigated before and after incubation with 50 mM glucose. Glucose incubation caused a time dependent loss of ATPase and acetylcholinesterase activities. Ghost enzyme activities in steptozotocin diabetic rats were found only insignificantly diminished.
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PMID:ATPase and acetylcholinesterase activities in erythrocyte membranes after incubation with glucose and in streptozotocin diabetic rats. 283 22

Nerve growth factor (NGF) induced the activities of acetylcholinesterase (AChE) and Na+,K+-ATPase concomitant with neurite outgrowth in PC12h cells, while dibutyryl cyclic AMP (DBcAMP) caused the induction of AChE activity and neurite outgrowth but not Na+,K+-ATPase activity. A nonproteinaceous extract isolated from the inflamed skin of rabbits inoculated with vaccinia virus (Neurotropin) induced neurite outgrowth and cell surface change similar to NGF without affecting AChE activity. The results suggest that NGF, DBcAMP and Neurotropin act on PC12h cells through different mechanisms.
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PMID:Differential action of nerve growth factor, cyclic AMP and neurotropin on PC12h cells. 284 98

An alteration in the enzymatic properties of the erythrocyte membrane acetylcholinesterase (AchE) and Na+,K+-ATPase has been described in experimental diabetes mellitus. We studied erythrocyte membrane fluidity and AchE and Na+,K+-ATPase activities in 15 insulin-dependent diabetic patients and 11 normal subjects. Fluidity was assessed by fluorescence polarization, using 1,6-diphenyl-1,3,5-hexatriene as a probe, and AchE and Na+,K+-ATPase activities were measured enzymatically. We found a significant increase in the enzymatic activity of AchE and a change in its enzymatic properties in diabetic patients compared with those in normal subjects. AchE activity correlated inversely with membrane fluorescence polarization, which was decreased in the diabetic patients, indicating an increase in membrane fluidity. Na+,K+-ATPase activity was reduced in the diabetic patients and correlated positively with the fluorescence polarization values. We hypothesize that the abnormal dynamic properties of the erythrocyte membrane may play a major role in determining the described change in enzymatic activity.
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PMID:Abnormal membrane fluidity and acetylcholinesterase activity in erythrocytes from insulin-dependent diabetic patients. 284 52

Activity of membrane-bound enzymes, passive penetration of ions in dose-dependent loading with cholesterol, effect of cholesterol high concentrations on the metabolic patterns in cytosol, viscosity of cell suspension were studied in erythrocytes. Passive cotransport of H+ and Cl- ions via erythrocyte membrane was increased with augmentation in viscosity of the cell suspension. After loading with cholesterol activity of acetylcholinesterase was increased while ATPase and glyceraldehyde-3-phosphate dehydrogenase activities were decreased. The alteration in the enzymatic activity occurred on those sides of the membranes, where these enzymes were localized. Activity of lactate dehydrogenase was decreased in cytoplasm of erythrocytes. The alterations detected may be important in development of ischemic syndrome in hyperlipoproteinemia.
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PMID:[Activity of membrane-bound enzymes, indices of metabolism in the cytoplasm and various physico-chemical properties of erythrocytes with increased cholesterol level]. 293 99

Experiments were designed to study functional associations of proteins in human red cell membranes as the membranes are induced to undergo the critical membrane events of invagination or evagination followed by constriction and fusion. Three examples were chosen for study: the inside-out vesicle (IOV) produced in white ghosts by hypotonic removal of cytoskeletal proteins; the endocytic vacuole produced in white ghosts by incubation with Mg-adenosine triphosphate; and the exocytic vesicle produced by metabolic depletion of intact red blood cells. The resulting particles were harvested, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis for membrane protein content and by enzymic analysis to detect the presence or absence of the exofacial enzyme acetylcholinesterase (ACE), the cytosol facing enzyme glyceraldehyde phosphate dehydrogenase (GAPD), and the integral protein adenosine triphosphatases (ATPases). Each of the vesicles is variably depleted of spectrin and actin, and each retains the exofacial enzyme ACE as well as Mg-ATPase. These findings suggest that there must be local partial depletion of cytoskeletal proteins before invagination or evagination occurs and that in each case part of the exoface of the membrane containing ACE is carried along into the resulting vesicle. The two forms of endocytosis differ with regard to their ATPase content with the energized endocytic vacuole retaining Ca-Mg-ATPase and actin-activated ATPase. The large amount of hemoglobin present in the exocytic vesicle is best explained by trapping of free cytosol and probably reflects a direct interaction of cytosolic components containing hemoglobin with the phospholipid bilayer.
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PMID:Endo- and exovesiculation and the structure of the human red cell membrane. 294 77

Acetylcholinesterase (AchE: EC 3.1.1.7) was identified and purified from the hemolymph of the scorpion Heterometrus bengalensis. The purity of the enzyme was determined by polyacrylamide gel electrophoresis (PAGE). The molecular weight of the enzyme, determined by sodium dodecyl sulfate-PAGE, was 80,000. The purified AchE hydrolysed acetylthiocholine iodide, but it did not react with butyrylthiocholine iodide. BW284C51, a specific inhibitor of AchE, strongly inhibited the enzyme. The known inhibitor (tetramonoisopropylpyrophosphortetramide) of pseudocholinesterase did not produce any inhibition of the enzyme activity. The purified AchE of scorpion hemolymph was vulnerable to high substrate concentration. The presence of Cu2+ and Ni2+ reduced the enzyme activity, whereas the metal ion, Sn2+, enhanced AchE activity. Ca2+ produced neither inhibition nor activation. (Na+, K+)-ATPase and Mg2+-ATPase activities were greatly enhanced by the purified AchE.
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PMID:Acetylcholinesterase (EC 3.1.1.7), a neurotransmitter enzyme in scorpion hemolymph. 296 37

Trichloroethylene (TCE) is a widely used organic solvent, the most important toxic effect of which is a narcotic central nervous (CNS) effect. In the present study we have used rat erythrocyte membranes as a nerve cell model for studying the changes in membrane integrity caused by TCE treatment. The parameters determined were osmotic resistance and the activities of acetylcholinesterase (AchE) and adenosinetriphosphatase (ATPase), both of which are integral membrane proteins. TCE had a dose-dependent effect on all these parameters. It increased the osmotic resistance at low concentrations and caused a decrease at high concentrations. Enzyme inhibition was only significant at high solvent concentrations. Decrease of temperature potentiated these effects. Our results indicate that changes in membrane proteins may be the initial factor leading to other changes in the membrane, e.g. increased osmotic resistance.
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PMID:Changes in trichloroethylene-treated rat erythrocyte membranes in vitro. 296 51

The mechanism of the anaesthetic effect of toluene on the central nervous system (CNS) was studied by using rat erythrocyte and synaptosome membranes as nerve cell models both in vitro and in vivo. The activities of the membrane-bound integral enzymes acetylcholinesterase (AChE), total adenosine triphosphatase (total ATPase) and magnesium-activated adenosine triphosphatase (Mg2+-ATPase) were determined. A short-term exposure to 2000 p.p.m. of toluene had an inhibitory effect on the enzyme activities studied. The degree of inhibition in erythrocyte membranes in vitro and in vivo, and in synaptosome membranes in vitro were in good correlation. In in vivo conditions, the synaptosome-bound enzymes were, however, significantly more inhibited by toluene, which indicates that membranes in vivo are even more vulnerable to the toxic effects of organic solvents than they are as isolated membranes in vitro. However, our results show that in vitro experiments can be used to predict the toxic nerve cell membrane effects of organic solvents. Toluene caused similar enzyme inhibitions both in neural cell membranes and in erythrocyte membranes. Thus, even peripheral non-excitable cell membranes, like erythrocytes, can be used as nerve cell membrane models in studies on the mechanism of the anaesthesia caused by solvents.
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PMID:The effect of in vitro and in vivo toluene exposure on rat erythrocyte and synaptosome membrane integral enzymes. 296 6

The in vivo effect of dimethoate and deltamethrin on body and organ weights, serum proteins and on plasma acetylcholinesterase (AChE), aromatic esterase and ATPase were examined in growing male rabbits throughout five months period. Both compounds had no significant effect on body weight; however, adrenal, testis & pituitary weights decreased (P less than 0.01); the liver and spleen weights increased (P less than 0.01) in a dose dependent manner. Serum total proteins and globulin decreased (P less than 0.01) in a dose dependent trend, while serum albumin was not greatly affected. AChE activity was increased (P less than 0.01) after 1 month of treatment with the two doses of dimethoate and deltamethrin; thereafter, AChE activity showed 40% inhibition of the control level. The activity of aromatic esterase increased markedly after the first month, then declined gradually until the fifth month. High dose of dimethoate markedly inhibited this enzyme particularly after the 5th month of treatment. Both doses of deltamethrin increased ATPase activity after the first month of treatment, then the ATPase activity was normal. Dimethoate inhibited ATPase particularly at the end of treatment in a dose dependent manner.
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PMID:In vivo chronic effect of dimethoate and deltamethrin on rabbits. 297 91

A rat brain P3 fraction enriched in ER derived microsomes was centrifuged through a 20-40% linear sucrose gradient in a Beckman Ti-14 Zonal rotor and 11 fractions were obtained. The distribution of marker enzyme activities and protein were determined in these 11 subfractions. NADPH-Cytochrome C reductase, choline phosphotransferase were employed for endoplasmic reticulum, Na+,K+-ATPase, 5'-nucleotidase, and acetylcholinesterase were employed for plasma membrane, 2',3'-cyclic nucleotide phosphohydrolase was employed for myelin. The bulk of the protein was recovered in the 24-34% sucrose fractions, Na+,K+-ATPase, 5'-nucleotidase, and acetylcholinesterase were in the 22-38% sucrose fractions while NADPH-cytochrome C reductase and CNPase were enriched in the 20-22% sucrose fractions. The ethanolamine and the serine base exchange activities had a bimodal distribution, with highest specific activities in sucrose fractions 32-34% and 20-24%. Choline base exchange activity was nearly undetectable in all the fractions. The specific activities of CDP-choline phosphotransferase, and phospholipid-N-methyltransferase were highest in the 20-22% sucrose fraction. Phospholipid-N-methyltransferase activity was significantly stimulated in the presence of exogenous phospholipid acceptors as phosphatidylethanolamine or phosphatidylmonomethylethanolamine or phosphatidyldimethylethanolamine, however, the greatest response was with phosphatidylmonomethylethanolamine. The rat brain P3 fraction yielded a population of a membrane at the light end of the sucrose gradient which has a buoyant density similar to myelin but seemed to be enriched with NADPH cytochrome C reductase and phospholipid modifying enzymes. This is in contrast to liver microsomes submitted to a similar fractionation.
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PMID:Distribution of selected phospholipid modifying enzymes in rat brain microsomal subfractions prepared by density gradient zonal rotor centrifugation. 298 22


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