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)

Biochemical studies were performed on blood and lung tissue of squirrel monkeys (Saimiri sciureus) following acute exposure to 0.75 ppm ozone (O3) for 4 h/d for 4 consecutive days. One group of animals was sacrificed at the end of the last exposure day and another group was sacrificed 4 d later after the last exposure. Evidence was sought for oxidation-induced changes known to occur in rodents when high levels of O3 are inhaled. A significant increase in red blood cell membrane fragility was observed, as well as significant decreases in red blood cell glutathione and erythrocyte acetylcholinesterase; however, the red blood cell enzymes, lactic acid dehydrogenase (LDH), and glucose-6-phosphate dehydrogenase (G6PDH) were not changed significantly. Lung tissue analysis showed that lipid peroxidation was markedly increased and tissue vitamin E levels were significantly decreased. The tissue enzymes G6PDH, glutathione reductase, and LDH significantly increased in activity. No significant changes were seen in either superoxide dismutase or malic acid dehydrogenase. The results of this experiment indicate that O3, or reaction products resulting from O3-tissue interaction in the lung, pass the air-blood barrier and are capable of producing biochemical changes in blood as well as in lung tissue.
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PMID:Biochemical response of squirrel monkeys to ozone. 10 43

A congenital erythrocyte pyruvate kinase (PK) deficiency was found in a 72-year old female patient with chronic myelomonocytic leukemia (CMML). Erythrocyte PK deficiency was associated with an increase in the activity of hexokinase, 6-phosphogluconate dehydrogenase and glutathione peroxidase in erythrocytes as well as a decrease in acetylcholinesterase, glutathione reductase and glucosephosphate isomerase activities. The enzymatic abnormalities were accompanied by alterations in hemoglobin and in i antigen content of erythrocyte membrane. In addition, bone marrow ultrastructural studies showed dyshemopoietic changes in all blood cell lines and especially in erythroblasts. The present findings confirm the close relationship between CMML and acquired dyserythropoietic syndromes and constitute a new observation of the infrequent association of hereditary erythrocyte enzymopathies and leukemia. A survey of the literature is presented.
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PMID:Chronic myelomonocytic leukemia associated with hereditary pyruvate kinase deficiency and multiple acquired erythrocyte abnormalities. 10 94

In a patient with paroxysmal nocturnal haemoglobinuria (PNH) enzymatic activities of erythrocytes and leucocytes were studied. Studies of autohaemolysis were also performed. The following erythrocytary enzymes were measured: Glucose-6-phosphate dehydrogenase (G-6-PD), pyruvate kinase (PK), glutathione reductase (GR), and acetylcholinesterase (AcChE). The following enzymes were measured in leucocytes: Adenosine deaminase, purine nucleoside phosphorylase, adenine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase and adenosine kinase. Normal activity of G-6-PD, GR and PK in erythrocytes was found. In leucocytes and lymphocytes activity of purine nucleoside phosphorylase was reduced. Auto-haemolysis in vitro was increased, which could not be compensated by addition of glucose or ATP.
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PMID:Erythrocyte and leucocyte enzymes in a case of paroxysmal nocturnal haemoglobinuria. 10 10

Statistically significant changes (P less than .05) were observed in erythrocytes (RBC) and sera of young adult human males following a single short-term exposure to 0.50 ppm ozone (O3) for 2 3/4 hours. The RBC membrane fragility, glucose-6-phosphate dehydrogenase (G-6-PDH) and lactate dehydrogenase (LDH) enzyme activities were increased, while RBC acetylcholinesterase (AcChase) activity and reduced glutathione (GSH) levels were decreased. The RBC glutathione reductase (GSSRase) activities were not significantly altered. Serum GSSRase activity, however, was significantly decreased while serum vitamin E, and lipid peroxidation levels were significantly increased. These alterations tend to disappear gradually, but were still detectable two weeks following exposure.
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PMID:Ozone and human blood. 110 71

The effects of repeated exposure to N,N-dimethylformamide (DMF) on hepatic microsomal monooxygenase system and glutathione metabolism were investigated. DMF was administered to Wistar male rats by subcutaneous (s.c.) injection at 0.5 ml/kg body weight daily for 1 week. Macroscopically, mild liver swelling was observed and liver weights significantly increased after 1 week of exposure to DMF. Hematological changes were not detected. In exposed rats, glutamic oxaloacetic transaminase, glutamic pyruvic transaminase, cholinesterase and total cholesterol significantly increased. Hepatic microsomal cytochrome P-450 and protoheme decreased by 34% and 24%, respectively, while microsomal protein and cytochrome b5 were not affected. NADH-ferricyanide reductase activity decreased by 24% while NADPH-cytochrome c reductase activity showed no change. Glutathione reductase (GR) activity showed a significant decrease after the first injection and remained depressed throughout the study, with no change in glutathione peroxidase (GPx) activity. Glutathione S-transferase (GST) activity showed a significant increase at 3 days after DMF treatment and gradually increased by 66% at 1 week. In a subsequent experiment with a single administration of DMF (4 ml/kg), reduced glutathione (GSH) in the liver was decreased by 28% at 8 h, but recovered to control levels by 24 h. These results indicate that DMF alters the hepatic microsomal monooxygenase system and glutathione metabolism. These findings may greatly contribute to the elucidation of the pathogenesis of DMF hepatotoxicity.
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PMID:Effects of dimethylformamide on hepatic microsomal monooxygenase system and glutathione metabolism in rats. 153 72

This study was carried out on male Wistar rats. The bone marrow activities of acetylcholinesterase (AchE-EC.3.1.1.7.), glutathione reductase (GR-EC.1.6.4.2.) and glucose-6-phosphate dehydrogenase (G6PD-EC.1.1.1.49.) were determined as affected by aluminium. The present experiments have revealed that within the first days there will be an increase in enzyme activity in the bone marrow. Simultaneously a decline in the activity of bone marrow could be observed which occurred later in the first course of the experiment.
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PMID:The effect of aluminium upon the activity of selected bone marrow enzymes in rats. 170 15

The effect of riboflavin deficiency on the fluidity and function of the red blood cell (RBC) membrane and on the activity of some enzymes involved in antioxidant defense mechanisms was studied. Growing male rats were fed an experimental (riboflavin-deficient) or a control (riboflavin-supplemented) diet. Following 7 wk of feeding, RBC from riboflavin-deficient rats contained higher levels of peroxidation products, most likely due to decreased glutathione reductase activity. An elevation in glutathione peroxidase activity was also observed whereas the activity of catalase and superoxide dismutase was not affected. Membrane fluidity was studied by fluorescence polarization, using 1,6-diphenyl-1,3,5 hexatriene (DPH) as a probe. The fluidity of RBC membranes isolated from riboflavin-deficient rats was significantly lower than that of the controls. This decreased fluidity was accompanied by an increase in the activity of the membrane-bound enzyme acetylcholinesterase. This study demonstrated that a decrease in cells' ability to cope with peroxidative damage as a result of riboflavin deficiency may lead to changes in the fluidity and function of membranes.
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PMID:Riboflavin deficiency and the function and fluidity of rat erythrocyte membranes. 238 Jul 93

The aim of this study was to determine the changes of the basic parameters of the erythrocyte system and the activity of some red blood cell (RBC) enzymes prior to and after a single physical effort leading to exhaustion. The study was carried out on male Wistar rats subjected to running on an electric rotating drum at a speed of 25 m/min. A single exercise caused a decrease in the RBC count, haemoglobin concentration (Hb) and haematocrit (Hct) by 21.9, 16.7 and 16.1%, respectively, and an increase in the reticulocyte count (Ret) by 661.5%. The exercise triggered also changes in the activities of some erythrocytic enzymes: pyruvate kinase (PK) activity increased by 12.4%, glucose-6-phosphate dehydrogenase (G6PD) by 37.8%, glutathione reductase (GR) by 30.8% and acetylcholinesterase (AChE) by 248.7%. These increases in the activities of RBC enzymes can be explained by an increase in the red cells turn-over.
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PMID:Metabolism of red blood cells after short-term exercise in rats. 248 9

Erythrocyte membrane (EM) abnormalities in a 16-yr-old boy with hypoalphalipoproteinemia resembling fish eye disease (FED-LS) were investigated. The proband's erythrocytes had markedly decreased osmotic fragility with target cells observed in the peripheral film. Analysis of his EM lipids revealed normal cholesterol and phospholipid content but a marked increase in phosphatidylcholine with concomitant decreases in phosphatidylethanolamine and sphingomyelin. Of the EM enzymes examined, acetylcholinesterase and superoxide dismutase activities were decreased while those of Na+-K+ ATPase, catalase and glutathione reductase were normal. 51Cr erythrocyte survival in the patient was slightly decreased. The observed changes in a number of structural and functional properties of erythrocytes in this disorder are indistinguishable from those previously described in homozygotes for familial lecithin:cholesterol acyltransferase (LCAT) deficiency. Thus, it is possible that in both of these disorders an abnormality of plasma LCAT activity causes, either directly or indirectly, functional and structural changes in the erythrocyte membrane.
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PMID:Erythrocyte abnormalities in a hypoalphalipoproteinemia syndrome resembling fish eye disease. 341 11

The effect of tris-(2-chloroethyl)-amine (HN-3) on RNA and DNA was investigated spectrophotometrically. The shift in the absorbance spectrum caused by the addition of HN-3 was used to test a variety of compounds for their ability to inhibit RNA alkylation. The effect of HN-3 on the activity of several enzymes was also investigated. The activities of ribonuclease A, desoxyribonuclease I, acetylcholinesterase, diaphorase, glutathione reductase, adenosine desaminase, glyoxalase I, 3-hydroxyacyl-CoA-dehydrogenase, xanthine oxidase, glucose-6-phosphate dehydrogenase, hexokinase and the microsomal N-oxygenation of aniline were not changed by HN-3, whereas the activity of cytochrome-c-reductase exhibited a dose dependent diminution in the presence HN-3. Of 105 compounds tested only 14, namely, sodium thiosulfate, dithioxanthine, thiosalicylic acid, 1,2,4-triazole-5-thiol, 2-thiocytosine, 2-thiohistadine, 2,3-dithiosuccinic acid, thioglycolic acid, 3-mercapto-D-valine,6-amino-2-thiouracil, thionicotine amide, dithiothreitol, sodium sulfite, and ergothioneine prevented the alkylation of RNA. All of them also reacted with HN-3 in absence of RNA. No correlation was found between the reaction constant of the reaction compound:HN-3 in the absence of RNA and the concentration of the compound which inhibited RNA alkylation by 50%. The compounds which were effective in vitro were also tested in mice for their ability to reduce HN-3 toxicity in vivo. Only sodium thiosulfate, d-penicillamine, and dithiosuccinic acid were effective. A 3.9fold increase in the LD50 of HN-3 was achieved in mice treated with sodium thiosulfate 3330 mg/kg i.p., a 1.7fold with 2125 mg dithiosuccinic acid/kg, and a 2fold increase with 2500 mg/kg d-penicillamine. The compound tested was injected i.p. 0.5 to 1 min after the s.c. injection of HN-3.
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PMID:Effect of various compounds on the reaction of tris-(2-chloroethyl)amine with ribonucleic acid in vitro and on its toxicity in mice. 617 33


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