Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The shedding of acetylcholinesterase-enriched vesicles from erythrocytes of various species of animals occurred when cells were treated with C12:0PC. The response was observed shortly after a morphological change of erythrocytes without any accompanying detectable K+ leakage or hemolysis. The vesiculation was inhibited by the presence of serum albumin or by the incorporation of cholesterol into C12:0PC liposomes, indicating that the insertion of C12:0PC into the erythrocyte membrane causes the vesiculation. The ratio of C12:0PC to total phospholipid determined in vesicle fractions was almost the same as that observed in non-hemolyzed cell fractions. This finding suggests that the vesicles were not shed from portions of membranes rich in C12:0PC. The vesicles showed similar characteristics to those generated by ATP depletion; their diameter is 150-200 nm and they are enriched with acetylcholinesterase activity. Erythrocytes became denser when they lost acetylcholinesterase activity on treatment with C12:0PC.
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PMID:Release of vesicles containing acetylcholinesterase from erythrocyte membranes by treatment with dilauroylglycerophosphocholine. 688 44

It has been shown in rat experiments that armin in doses that inhibit blood cholinesterase by 50 and more per cent lowers the content of nicotinamide coenzymes in the myocardium and liver of the animals, primarily at the expense of the diminution of the oxidized forms. In the rat liver, armin decreases the content of adenyl nucleotides, mainly at the expense of ATP. Dipyroxime prevents changes induced by armin, which is accompanied by partial reactivation of cholinesterase. It is suggested that in the mechanism of antidote action of dipyroxime, of importance is its normalizing effect on redox and energy processes in the body.
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PMID:[Effect of armin and dipyroxime on the nicotinamide coenzyme and adenine nucleotide content of the rat myocardium and liver]. 705 78

Quinacrine-fluorescent nerve fibres and nerve cell bodies are described in the right and left atria of the guinea-pig and rabbit. The nerve cells (20 to 35 micrometers in diameter) are found predominantly in the right atrium in both species. The nerve fibres are varicose and innervate both the muscle and many blood vessels. The quinacrine fluorescent neural structures are unaffected by chemical sympathectomy with 6-hydroxydopamine. The distribution of quinacrine-positive nerve fibres and cell bodies are compared to the distribution of adrenergic and acetylcholinesterase-positive nerves in the atrium of both species. Quinacrine fluorescence appears to be selective for non-adrenergic, non-cholinergic nerves and the possibility that it is binding to high contents of ATP discussed.
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PMID:Fluorescent histochemical localisation of quinacrine-positive neurones in the guinea-pig and rabbit atrium. 712 52

Incubation of human erythrocytes with suspensions of sonicated dimyristoyl phosphatidylcholine resulted in dramatic morphological changes of the cells and release of membrane vesicles. The shedding of membrane vesicles was not preceded by ATP depletion and only occurred at temperatures of incubation that were above the phase transition temperature of dimyristoyl phosphatidylcholine. Membrane vesicles were separated from intact erythrocytes and exogenous dimyristoyl phosphatidylcholine by a series of centrifugation steps. The lipid composition of the membrane vesicles was similar to that of the native erythrocyte, and the predominant membrane proteins were band 3, glycophorin and acetylcholinesterase. Spectrin was not detected. Freeze-fracture electron microscopy showed vesicles (150 nm in diameter) with protein particles embedded in the lipid bilayer.
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PMID:Effect of dimyristoyl phosphatidylcholine on intact erythrocytes. Release of spectrin-free vesicles without ATP depletion. 721 19

Nerve showing positive reaction to quinacrine are described in rabbit ileum and stomach during perinatal development and compared to the distribution of nerves revealed by catecholamine fluorescence and by staining for acetylcholinesterase Acetylcholinesterase- and quinacrine-positive neurons were observed on the twenty-third day of gestation in both the ileum and stomach, but catecholamine fluorescence was not detected in nerves until the twenty-fifth and twenty-sixth days of gestation in the stomach and ileum respectively. The possibility that quinacrine is binding to high accumulations of ATP is discussed.
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PMID:Perinatal development of quinacrine-positive neurons in the rabbit gastrointestinal tract. 730 84

A new procedure is described for the preparation of highly purified and stable secretory vesicles from adrenal medulla. Two forms of acetylcholinesterase, a membrane bound form as well as a soluble form, were found within these vesicles. The secretory vesicles, isolated by differential centrifugation, were further purified on a continuous isotonic Percoll gradient. In this way, secretory vesicles were separated from mitochondrial, microsomal and cell membrane contamination. The secretory vesicles recovered from the gradient contained an average of 2.26 mumol adrenaline/mg protein. On incubation for 30 min at 37 degrees C in media differing in ionic strength, pH, Mg2+ and Ca2+ concentration, the vesicles released less than 20% of total adrenaline. Acetylcholinesterase could hardly be detected in the secretory vesicle fraction when assayed in isotonic media. However, in hypotonic media (less than 400 mosmol/kg) or in Triton X-100 (0.2% final concentration) acetylcholinesterase activity was markedly higher. During hypotonic treatment or when secretory vesicles were specifically lyzed with 2 mM Mg2+ and 2 mM ATP, adrenaline as well as part of acetylcholinesterase was released from the vesicular content. On polyacrylamide gel electrophoresis this soluble enzyme exhibited the same electrophoretic mobility as the enzyme released into the perfusate from adrenal glands upon stimulation. In addition to the soluble enzyme a membrane bound form of acetylcholinesterase exists within secretory vesicles, which sediments with the secretory vesicle membranes and exhibits a different electrophoretic mobility compared to the soluble enzyme. It is concluded, that the soluble enzyme found within isolated secretory vesicles is secreted via exocytosis, whilst the membrane-bound form is transported to the cell membrane during this process, contributing to the biogenesis of the cell membrane.
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PMID:Latent acetylcholinesterase in secretory vesicles isolated from adrenal medulla. 731 5

The number of quinacrine-fluorescent nerve cell bodies and the percentage of the ganglion area occupied by this fluorescence within stretch preparations of the myenteric plexus of the stomach and ileum of the guinea-pig, rabbit and rat were assessed. The number of quinacrine-positive cell bodies per cm2 of plexus varied between 1045 in the rabbit ileum to 2633 in the rat stomach, whilst the percentage of the ganglionic area occupied by fluorescence was approximately 10%. The distribution of quinacrine-fluorescent nerve fibres and cell bodies in the myenteric plexus was compared to the distribution of nerves revealed by catecholamine fluorescence and by staining for acetylcholinesterase in the stomach and ileum of all three species. Quinacrine fluorescence appears to be selective for non-adrenergic, non-cholinergic nerves; the possibility that it binds to high levels of ATP is discussed.
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PMID:Comparative studies of quinacrine-positive neurones in the myenteric plexus of stomach and intestine of guinea-pig, rabbit and rat. 731 46

Semi-purified diets supplemented with either a high alpha-linolenate (n - 3) (perilla) oil or a high linoleate (n - 6) (safflower) oil were fed to rats through two generations. Rats fed safflower oil showed a decrease in docosahexaenoic acid (n - 3) and a compensatory increase in docosapentaenoic acid (n - 6) in all the brain regions and organelles examined, when compared with rats fed perilla oil. As reported previously, the safflower oil-fed rats exhibited inferior learning ability compared with the perilla oil-fed rats (N. Yamamoto et al., J. Lipid Res. 28, 144 (1987)). Using brains of rats in these dietary groups, the activities of several enzymes, Na+ , K+-ATPase, Ca2+-ATPase, 5'-nucleotidase, 2',3'-cyclic nucleotide phosphodiesterase, acetylcholinesterase, and choline acetyltransferase in membranes, were compared. The 5'-nucleotidase activity in cortex and hippocampus, and the Na+, K+-ATPase activity in myelin decreased slightly but significantly in the safflower oil group. None of the other membrane-associated enzyme activities in all the brain regions and organelles examined was affected significantly by the dietary fatty acids under optimal assay conditions in vitro. However, in the safflower oil group, the Na+, K+-ATPase activity of synaptosomes at a suboptimal concentration of ATP was 78% that in the perilla oil group. These results suggest that relatively large changes in the proportions of n - 3 and n - 6 polyunsaturated fatty acids in brain membranes caused by dietary manipulation do not provoke significant alterations in most membrane-bound enzyme activities. However, a small but significant change in Na+, K+-ATPase activity at a suboptimal concentration of ATP may be implicated in the altered learning behavior reported earlier.
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PMID:Effect of a high alpha-linolenate and high linoleate diet on membrane-associated enzyme activities in rat brain--modulation of Na+, K+- ATPase activity at suboptimal concentrations of ATP. 749 79

Central administration of galanin in the mouse dose-dependently blocked the hypothermia induced by the muscarinic receptor agonist, 2-ethyl 8-methyl-2,8-diazospiro[4,5]decan-1,3-dion hydrobromide, RS86 (minimum effective dose, MED = 3 nmol) and the acetylcholinesterase inhibitor tetrahydroaminoacridine, (MED = 3 nmol). This inhibitory effect was reversed over the dose range (0.1, 0.3, 1, 3 nmol) by the galanin receptor antagonist galantide (MED = 0.3 nmol). Furthermore, the ATP-sensitive K+ channel blockers glibenclamide (MED = 1 nmol) and gliquidone (10 nmol) both prevented the inhibitory effects of galanin on RS86 induced hypothermia. Glibenclamide (10 nmol) also reversed the inhibitory effects of galanin on tetrahydroaminoacridine induced hypothermia. Preincubation of rat cortical membranes with galanin (10 nM, 1000 nM) in vitro had no effect on binding affinity, receptor number or pharmacology of the rat cortical muscarinic receptor. In contrast to the high affinity of glibenclamide, galanin only weakly displaced [3H]glibenclamide binding in mouse whole brain homogenates (36% at 10 microM). These studies suggest that the inhibitory effect of galanin on cholinergically mediated hypothermia induced by RS86 and tetrahydroaminoacridine may be exerted via an action at ATP-sensitive K+ channels but is unlikely to be acting directly at the site labelled by [3H]glibenclamide.
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PMID:Hypothermia induced by cholinomimetic drugs is blocked by galanin: possible involvement of ATP-sensitive K+ channels. 751 82

The influence of ethanol consumption on acetylcholinesterase (AchE) and Na+, K+ -ATP-ase activities was examined in 14 healthy volunteers after 30 minutes of ethanol treatment at a dose 0.6 g/kg of body weight. It was observed that the activity of both enzymes decreased. The activity of AchE was significantly lower, and that of Na+, K+ -ATP-ase tended to be lower, but the difference was not significant. In vitro experiments showed that ethanol inhibited the AchE and N+, K+ -ATP-ase activities immediately and in proportion to the concentration of ethanol used.
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PMID:Activities of acetylcholinesterase and NA+, K+ -ATP-ase in human erythrocytes after ethanol consumption. 758 49


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