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:3.1.1.7 (acetylcholinesterase)
28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to determine the effect of Alzheimer's disease on the relative distribution of soluble and membrane-bound molecular forms of acetylcholinesterase (AChE) in the brain, postmortem samples (delay interval less than 12 h) were obtained from parietal cortex (Brodmann area 40) and hippocampus as well as the areas containing their respective projection nuclei, i.e., substantia innominata and septal nucleus, in 9 patients with Alzheimer's disease (AD) and 4 normal controls. The monomer (G1), dimer (G2), and tetramer (G4) forms of AChE were examined. In AD compared to controls, significant changes occurred in area 40 and hippocampus but not in the areas containing projection nuclei, and included loss of mean total AChE activity, decrease in the relative percentage of membrane-bound G4, and increase in the relative percentage of soluble G1-G2. Percent of soluble G4 was unaffected in AD brain. In area 40 but not hippocampus a large increase in percent membrane-bound G1-G2 occurred. Thus, these results emphasize that the selective decrease in membrane-bound G4 accounts for the decrease in total G4 activity in AD brain.
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PMID:Soluble and membrane-bound forms of brain acetylcholinesterase in Alzheimer's disease. 149 35

Radio-frequency electromagnetic radiation (RFR) at 915 and 147 MHz, when sinusoidally amplitude modulated (AM) at 16 Hz, has been shown to enhance release of calcium ions from neuroblastoma cells in culture. The dose-response relation is unusual, consisting of two power-density "windows" in which enhanced efflux occurs, separated by power-density regions in which no effect is observed. To explore the physiological importance of these findings, we have examined the impact of RFR exposure on a membrane-bound enzyme, acetylcholinesterase (AChE), which is intimately involved with the acetylcholine (ACh) neurotransmitter system. Neuroblastoma cells (NG108), exposed for 30 min to 147-MHz radiation, AM at 16 Hz, demonstrated enhanced AChE activity, as assayed by a procedure using 14C-labeled ACh. Enhanced activity was observed within a time window between 7.0 and 7.5 h after the cells were plated and only when the exposure occurred at power densities identified in a previous report as being effective for altering the release of calcium ions. Thus RFR affects both calcium-ion release and AChE activity in nervous system-derived cells in culture in a common dose-dependent manner.
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PMID:Dose dependence of acetylcholinesterase activity in neuroblastoma cells exposed to modulated radio-frequency electromagnetic radiation. 151 Jul 40

The activity of acetylcholinesterase (AChE) in acetylcholine receptor (AChR)-enriched membrane vesicles isolated from electric organ of Torpedo californica exhibited a biphasic response to ethanol action. Below an ethanol concentration of 35 mM, AChE activity increased with increasing concentration of ethanol. At ethanol concentrations greater than 35 mM, the activity was found to decrease montonically. In contrast, ethanol (35-400 mM) increased the activity of soluble AChE. This biphasic behavior was consistent with the proposed important role of ethanol-membrane interaction. Microcalorimetric measurements revealed that the enthalpy change in acetylcholine (ACh) hydrolysis reaction was 586 J/mol in association with membrane-bound AChE in AChR-enriched membrane vesicles, as compared to -544 J/mol with the isolated soluble AChE. This discrepancy was attributed to the presence of membranes. Unlike its action on the enzyme activity, ethanol did not affect enthalpy change in ACh hydrolysis reaction catalyzed by either membrane-bound or soluble AChE. Comparison of results on activity and heat measurements suggested that the interaction of ethanol with membrane vesicles was nonspecific with no ethanol-induced membrane structural or conformational change.
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PMID:Acetylcholine receptor-enriched membrane vesicles in response to ethanol: activity and microcalorimetric studies. 163 58

Denervated fast-twitch rabbit muscles were progressively losing their fresh weight and the yield of sarcotubular protein was increasing. The activity of Ca(2+)-ATPase was affected but very slightly, the basal Mg(2+)-ATPase and the Mg(2+)-ATPase/Ca(2+)-ATPase ratio however increased together with a simultaneous depression of the membrane-bound acetylcholinesterase activity. We did not observe any differences in density properties of sarcotubular fractions between control and denervated muscle. However, a relative enrichment in SM and H fraction could be seen after denervation with small changes in the content of the Ca(2+)-pump protein, increased levels of calsequestrin and cholesterol, mostly in the heavy and the SM fraction. After denervation the binding sites for 3H-PN-200-110 did not show any changes in receptor affinity, but the number of putative Ca(2+)-channels increased twice along with a depression of 3H-ouabain binding sites. We suggest that the denervation of fast-twitch muscle leads to the hypertrophy of the junctional sarcoplasmic reticulum and the T-system. Changes in the cholesterol content, in the number of putative Ca(2+)-channels and in Na+, K(+)-ATPase can affect the muscle contraction.
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PMID:Effects of denervation on the contents of cholesterol and membrane systems involved in muscle contraction in rabbit fast-twitch sarcotubular system. 165 Jul 29

1. The specific activities of erythrocyte membrane-bound acetylcholinesterase (EC 3.1.1.7.) and soluble hexokinase (EC 2.7.1.1.) in vitamin E deficient and vitamin E sufficient rabbits were investigated. 2. Acetylcholinesterase specific activities values of 43.4 in deficient and 57.4 in sufficient vitamin E rabbits were obtained. Hexokinase specific activity was not modified, and values of 3.31 in deficient and 3.6 in controls were found. 3. No peroxidation process was detected by us on vitamin E deficient diets. 4. These observations would suggest that the membrane stabilizing effect of vitamin E may be accomplished by a mode of action not necessarily related to its ability to prevent lipid peroxidation.
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PMID:Erythrocyte membrane-bound acetylcholinesterase in vitamin E deficient rabbits. 168 4

The immunochemical and immunocytochemical reactivity of an anti-carbohydrate monoclonal antibody (Elec-39), obtained against acetylcholinesterase from Electrophorus electricus electric organ, was followed during the postnatal development of the rat cerebellum. The specificity of this antibody resembles that of a family of anti-carbohydrate antibodies that includes HNK-1, L2, NC-1 and NSP-4, as well as IgMs that occur in some human neuropathies. As revealed by immunoblotting techniques, the reactivity of Elec-39 is maximum around postnatal days 10-12. At this age, the antibody reveals eight major proteins of mol. wt ranging between 14 and 150 kDa. Some of them (with mol. wts of 14, 18, 28 and 31 kDa) are transiently expressed. They correspond to previously identified glycoproteins binding to the plant lectin concanavalin A and binding also to the endogenous mannose-binding lectin CSL and endogenous membrane-bound mannose-binding lectin. In young animals, an important staining with the Elec-39 antibody can be observed on postmitotic precursors of granule cells, on astrocyte processes in the external granular layer, on newly formed parallel fibres and on unmyelinated axons of the white matter. In adult animals, the labelling is localized essentially in myelin and also in the cytoplasm of astrocytes. These results are discussed in relation to ontogenetic phenomena occurring during cerebellar development and the potential role of the carbohydrate epitope revealed with Elec-39 as a determinant in cell adhesion processes.
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PMID:Expression and localization in the developing cerebellum of the carbohydrate epitopes revealed by Elec-39, an IgM monoclonal antibody related to HNK-1. 171 52

Previous studies in this laboratory showed an age-related decline of acetylcholinesterase (AChE) activity in the cerebral cortex of rats. In the present study the age-related differences in enzymatic activity were evaluated in terms of individual molecular forms. Extracts containing total, soluble and membrane-bound AChE were analyzed both by ultracentrifugation in sucrose gradient and by non-denaturing gradient polyacrylamide gel electrophoresis. By ultracentrifugation two molecular forms, namely 10S and 4S (corresponding to tetrameric-G4 and monomeric-G1 forms, respectively) were separated in extracts of total and soluble AChE, while only 10S forms were present in extracts of membrane-bound AChE. Electrophoresis of soluble AChE extracts revealed slowly- and fast-migrating bands, grouped in two clusters of at least three bands each; membrane-bound AChE contained only a single slowly-migrating band. Electrophoresis of the single forms isolated by ultracentrifugation showed that slowly- and fast-migrating bands corresponded to G4 and G1 forms, respectively. Therefore, in soluble AChE no one-to-one relationship between charge- and size-isomers was observed; on the contrary, such relationship has been shown for membrane-bound AChE. This implies that soluble G4 forms and membrane-bound-G4 forms are electrophoretically different, being heterogeneous the former and homogeneous the latter. The age-related decline of total AChE, accompanied by a decrease of G4/G1 ratio, depended mainly on a decrease of membrane-bound AChE while soluble AChE and its G4/G1 ratio was unchanged. The qualitative pattern of charge isomers was not modified by aging.
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PMID:Size and charge isomers of acetylcholinesterase in the cerebral cortex of young and aged rats. 175 33

The effects of monocrotophos and its newly synthesized analogues, RPR-II and RPR-V, on hematology and blood chemistry 24 hr post-treatment were studied in rats given doses of 0.96, 1.23, and 3.0 mg/kg po, respectively. It was found that monocrotophos caused a significant increase in the mean WBC count. RPR-V, a significant decrease in hematocrit and RBC count, whereas RPR-II did not alter any hematological parameter. The activities of membrane-bound enzymes in serum were not significantly changed by all three compounds except for a statistically significant increase of 38% in SGOT activity by RPR-II. Only monocrotophos caused a significant inhibition of the brain acetylcholinesterase activity. In vitro studies with partially purified preparations of rat brain cholinesterase revealed that monocrotophos was the most potent anticholinesterase agent, followed by RPR-II and RPR-V. All three compounds caused inhibition of rat brain cholinesterase by decreasing the Vmax and increasing the Km values, indicating a mixed type of inhibition. The two analogues appeared to be less neurotoxic than monocrotophos.
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PMID:A comparative study of blood changes and brain acetylcholinesterase inhibition by monocrotophos and its analogues in rats. 186 85

Decarbamylation rate of membrane-bound methyl- and dimethyl-carbamylated acetylcholinesterase of human erythrocytes and bovine brain is reliably 1.1-1.6 times lower than that of the soluble enzyme. Such reversible inhibitors as tacrine (of non-competition action), ambenonium (mixed action) and galanthamine (competitive type of action) decelerate the decarbamylation rate of acetylcholinesterase. At pH 6 tacrine inhibits the reduction rate of soluble acetylcholinesterase activity of human erythrocytes more intensively than that of membrane-bound acetylcholinesterase. No differences in decarbamylation rate were found for the both forms of the enzyme at pH 8. Tacrine, a non-competitive inhibitor in concentrations below the inhibition constant (Ki = 1.4 x 10(-7) M) exerts the most intensive effect on the decarbamylation rate of methyl- and dimethylcarbamylated acetylcholinesterase of the mouse brain, while ambenonium and galanthamine in concentrations much (tens times) exceeding their Ki (3.1 x 10(-10) M and 4.4 x 10(-7) M, respectively) provide a decrease of the decarbamylation rate.
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PMID:[The effect of pH and reversible inhibitors on decarbamylation of acetylcholinesterase]. 192 83

The properties of acetylcholinesterase (AChE) in axolemma-enriched fractions (AEF) from bovine splenic nerve were investigated to see if they differed in any way from those of the AChE in diaphragm muscle. The axolemmal enzyme had a low Km for acetylthiocholine (ca. 90 microM), exhibited substrate inhibition, and had a well-defined optimum of substrate concentration of 1 mM. The rate of hydrolysis of substrate decreased with increasing acyl chain length (acetyl- greater than propionyl- greater than butyryl-). The AChE inhibitors eserine and hexamethonium were competitive inhibitors of the membrane-bound enzyme, whereas lidocaine was a noncompetitive inhibitor; these results were comparable to the effect of these inhibitors on diaphragm muscle AChE. The axolemmal enzyme was more efficiently solubilized and more stable in nonionic detergents such as Triton X-100 and Tween 20 than charged detergents such as lysolecithin and zwitterionic detergents. These results indicate that the AChE present in bovine splenic nerve AEF is identical to the previously characterized AChE from other sources.
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PMID:Properties of acetylcholinesterase in axolemma-enriched fractions isolated from bovine splenic nerve. 197 53


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