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)

Addition of vasoactive intestinal peptide (VIP) to brain homogenates increased the activity of choline acetyltransferase (ChAT) but not that of acetylcholinesterase or glucose-6-phosphate dehydrogenase. Activity of ChAT was increased in the anterior hypothalamus and in the dorsal and ventral hippocampus, but not in the parietal cortex or posterior hypothalamus. Increased activity occurred rapidly after VIP addition to homogenates and was maximal at 10(-7)M concentration. Kinetic analysis indicates that the Vmax of the enzyme is increased and the Km for choline, but not acetyl-coenzyme A, is decreased in the presence of VIP. Results support a possible VIP-cholinergic interaction in the CNS.
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PMID:Activation of choline acetyltransferase by vasoactive intestinal peptide. 632 60

The genetic structure of three Asiatic eskimos subpopulations (402 individuals), five coast chuckchies subpopulations (1793 individuals) and three reindeer chuckchies subpopulations (559 individuals) have been studied for 26 electrophoretic protein systems (33 loci). These are: adenilate-kinase (AK), diaphorase NAD X H (Dia), glyoxalase-1 (GLO-1), glucose-6-phosphate dehydrogenase (6GPT), glutamatpyruvate transaminase (GPT), glutamicoxalate transaminase (GOT), carbonic anhydrase-1 (Ca-1), catalase (Ct), acid phosphatase (AcP), lactate dehydrogenase (loci LDH-A and LDH-B), leucine aminopeptidase (Lap), malatedehydrogenase (MDH), purine nucleoside phosphorylase (PNP), superoxide dismutase (Sod), 6-phosphogluconate dehydrogenase (PGD), phosphoglucomutase (loci PGM1 and PGM2), cholinesterase (loci c1--c5), alkaline phosphatase (Pp), esterase D (EsD), red cell esterase (Est) - 4 loci, albumin (Alb), haptoglobin (Hp), hemoglobine (Hb A and B), group-specific component (Gc), transferrin (Tf), ceruloplasmin (Cp). In addition, AB0 and Rh system blood groups and phenyl thiocarbamide taste sensitivity (PTC) have been studied. 12 of 36 loci are polymorphic (33.33%), heterozygosity for all loci in eskimos, coastal and reindeer chuckchies being 0.118 +/- 0.005, 0.130 +/- 0.002 and 0.120 +/- 0.004, respectively. These estimates do not differ essentially from heterozygosity at these loci for mongoloid groups living further south. The test for interpopulation heterogeneity has permitted to estimate contribution of the loci to the differentiation of these populations. The least heterogeneity has been found at loci where gene frequency distribution is the most specific for these ethnic groups.
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PMID:[Genetic structure of the populations of native inhabitants in the northeastern USSR. III. Asiatic Eskimos and the coast and reindeer Chukchi]. 643 3

n-Butyl mercaptan (nBM) is a breakdown product of S,S,S,-tri-n-butyl phosphorotrithioate (DEF) and S,S,S-tri-n-butyl phosphorotrithioite (merphos) in hens and in the environment. n-Butyl disulfide (nBD) is an oxidation product of nBM. A single 500 mg/kg dose of nBM and nBD was administered in gelatin capsules to groups of five 12-month old laying hens. A third group (five hens) was given gelatin capsules. One day after administration, the hens exhibited weakness which progressed to unsteadiness and inability to stand by the third day. These signs were accompanied by a pale comb 18--24 hr after dosing, which changed to dark color at 48 hr. Treated hens improved with time. Heinz bodies and extensive erythrocyte deformation and lysis were observed in blood smears taken from hens 24 and 48 hr after treatment. Hemoglobin concentration, packed cell volume, erythrocytes, and glucose-6-phosphate dehydrogenase activity were significantly lower than controls, while methemoglobin was significantly higher. As the clinical condition of these hens improved, these hematologic changes disappeared. nBM caused an initial increase in plasma butyrylcholinesterase activity which was dose-dependent and returned to normal by the end of the 28-day experiment. Also, brain acetylcholinesterase activity was not different from that of the control at termination.
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PMID:Heinz body production and hematological changes in the hen after administration of a single oral dose of n-butyl mercaptan and n-butyl disulfide. 687 30

In this communication, the results of applying various histochemical techniques for the localization of oxidoreductases, transferases, hydrolases and isomerases in the human heart are presented. The Purkinje fibres of the atrioventricular conducting system of the human heart differ from the myocardium proper in containing a slightly higher activity of most of the glycolytic and gluconeogenetic enzymes investigated. The relatively higher activity of 6-phosphofructokinase, the key enzyme in anaerobic carbohydrate metabolism, is especially noteworthy. On the other hand, the activities of some of the enzymes that play a part in the aerobic energy metabolism is slightly less than those in the myocardium fibres. As for the activity of the NADPH regenerating enzymes, the activity of 6-phosphogluconate dehydrogenase and malate dehydrogenase (oxaloacetate-decarboxylating) is somewhat higher, and the activity of glucose-6-phosphate dehydrogenase similar, in the Purkinje fibres compared to that in the myocardial fibres. The activity of myosin ATPase is similar for both types of fibre. Likewise, the fibres of the conducting system and of the myocardium show a similar activity of acid phosphatase, beta-glucuronidase, non-specific naphthylesterase and peroxidase. The neurogenic function of the conducting system of the human heart was demonstrated by the high activity of acetylcholinesterase in the Purkinje fibres and in the atrioventricular node. All these histochemical findings in Purkinje fibres are similar at widely differing levels of the conducting system.
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PMID:Enzyme histochemical studies on the conducting system of the human heart. 744 Feb 54

Levels of acetylcholinesterase, non-specific esterases, glutathione-S-transferase and glucose-6-phosphate dehydrogenase in Aedes aegypti (L.) mosquitoes inoculated intrathoracally with Chikungunya virus were elevated, as compared to uninoculated control insects. A number of these enzymes are important in the insects defence mechanism against xenobiotics, such as pesticides. Malathion bioassays indicated a reduction in the susceptibility of experimentally injected insects with virus or virus-free inoculum, compared to non-inoculated controls. However, insects which were mock-inoculated (injected with no inoculum) showed a similar reduction in susceptibility suggesting that the observed effect was due to the mobilization of a defence reaction in the mosquitoes in response to injury during inoculation.
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PMID:Post-inoculation changes in enzyme activity of Aedes aegypti infected with Chikungunya virus. 757 67

1. Endosulfan insecticide is a polychlorinated compound used for controlling a variety of insects; it is practically water-insoluble, but readily adheres to clay particles and persists in soil and water for several years. Its mode of action involves repetitive nerve-discharges positively correlated to increase in temperature. This compound is extremely toxic to most fish and can cause massive mortalities. In fish, it causes marked changes in Na and K concentrations, decrease in blood Ca(2+) and Mg levels and inhibits Na, K and Mg-dependent ATPase (in brain). 2. Bioaccumulation of endosulfan is reported for marine animals; however, freshwater animals (e.g., crayfish) accumulate it to some extent, but they lose the compound rapidly during depuration. Endosulfan is generally less toxic to aquatic invertebrates than fish. However, it causes decreases in adenylate energy charge, oxygen consumption, hemolymph amino acids, succinate dehydrogenase, heart-beat (mussel) and altered osmoregulation. 3. Generally, mammals are less susceptible to endosulfan's toxicity than aquatic animals. The majority of studies conducted on laboratory mammals can be summarized. (a) Neurotoxicity: male rats are more sensitive than females to endosulfan, which decreases brain and plasma acetylcholinesterase activity. Endosulfan I (a metabolite) causes a significant change in norepinephrine, 5-HT and GABA. (b) Renal toxicity: inhibition of MFOs activity was noticed in rats; other effects included changes in proximal convoluted tubules and necrosis of the tubular epithelium. (c) Hepatotoxicity: chemically-induced aminopyrine N-demethylase and aniline hydrolase were found in rat liver, and reduction in the glycogen level occurred. (d) Hematologic toxicity: endosulfan exposure resulted in a significant decrease in the level occurred. (d) Hematologic toxicity: endosulfan exposure resulted in a significant decrease in the erythrocyte glutathione reductase, hemoglobin amount, RBC number and mean corpuscular volume. 4. Respiratory toxicity: involved dyspnea, acute emphysema, cyanosis and hemorrhages in teh interalveolar portions of rat's lungs. 5. Biochemical: in rats, endosulfan caused increased glucose-6-phosphate dehydrogenase activity, blood glucose level, phospholipid contents of the microsomal and surfactant system, and profoundly induced the activity of alcohol dehydrogenase and cytosolic glutathione S-transferases. It also decreased significantly Na+, K+ and Mg(2+) ATPases, plasma calcium level and alkaline phosphatase in the intestinal epithelium. 6. Immunologic toxicity: rat serum antibody titer to tetanus toxin, IgG, IgM and gammaglobulins were significantly reduced. 7. Reproductive toxicity: degenerative changes in the seminiferous epithelium, induction of the rate-limiting enzyme in testosterone production (3beta-hydroxysteroid transferase and 17 beta-hydroxysteroid transferase), histological changes in reproductive organs, testicular atrophy and the occurrence of ovarian cysts were noticed in rat. Reduction in the weight of secondary sex organ was also observed.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Bioaccumulative potential and toxicity of endosulfan insecticide to non-target animals. 790 Sep 59

1. The study has been carried out on Wistar rats. The aim of the present study was to trace the effect of aluminum on enzyme activities and hematological parameters on erythrocytes. 2. Aluminum decreased activities of acetylcholinesterase, glutathione reductase, glucose-6-phosphate dehydrogenase, and lactate dehydrogenase in the erythrocytes of the animals tested. 3. In the peripheral blood, a significant decrease in the erythrocyte count, hemoglobin level and hematocrit index and increased percentage of reticulocytes and polychromatophilic erythrocytes were observed. 4. The increase in the neutrophilic granulocyte and lymphocyte count was significant. 5. An inhibitory effect of aluminum on the phagocytic activity of granulocytes was also observed.
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PMID:Hematological and enzymatic results of aluminum intoxication in rats. 810 93

We previously demonstrated that feeding rats Steenbock and Black's rickets-inducing diet produces remarkable changes in the metabolic pattern of the intestinal mucosa, kidney, and liver and in some membrane transport systems of intestinal mucosa and kidney. 1,25-Dihydroxyvitamin D3 administration to rachitic rats did not always prove to be effective in restoring normal values. We have now investigated the effect of 1,25-dihydroxyvitamin D3 on the levels of some metabolites in rat cerebral cortex, on the activity of some enzymes, and on the transport of 2-deoxy-D-glucose and D-glucose in synaptosomes. Our experiments were carried out on three rat groups: control, rachitic, and rachitic treated with 1,25-dihydroxyvitamin D3. The decrease in phosphorus content and the increase in citrate concentration observed in rachitic rat cerebral cortex were corrected by 1,25-dihydroxyvitamin D3 treatment. The activity of acetylcholinesterase, glucose-6-phosphate dehydrogenase, and acyl phosphatase significantly increased in rachitic rat synaptosomes, as well as NAD(+)-dependent isocitrate dehydrogenase in cerebral cortex mitochondria; the administration of 1,25-dihydroxyvitamin D3 to rachitic rats restored enzyme levels to normal. The transport of 2-deoxy-D-glucose and D-glucose in rachitic rat synaptosomes was lower than in the control group and returned to control values in consequence of 1,25-dihydroxyvitamin D3 treatment. The results reported here support the hypothesis of a participation of 1,25-dihydroxyvitamin D3 in some aspects of cerebral cortex metabolism.
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PMID:Effect of vitamin D deficiency and 1,25-dihydroxyvitamin D3 on metabolism and D-glucose transport in rat cerebral cortex. 839 7

We previously demonstrated that feeding rats the Steenbock and Black rickets-inducing diet produces remarkable changes in the metabolic pattern of intestinal mucosa, kidney, liver, cerebral cortex and heart. We have now determined the levels of calcium, phosphorus and citrate in cerebral cortex and the activity of some enzymes in synaptosomes and cerebral cortex mitochondria of three rat groups: control (Group A), fed a vitamin D-deficient diet (Group B), fed a vitamin D-deficient diet and treated with 1,25-dihydroxyvitamin D3 (Group C). While calcium content increased in Groups B and C, phosphorus concentration increased only in Group C and citrate in Group B in comparison with control. The increase in acetylcholinesterase and citrate synthase registered in Group B was restored to control values by 1,25-dihydroxyvitamin D3 treatment, while, neither the decrease in cytochrome c oxidase, nor the increase in glucose-6-phosphate dehydrogenase, acid phosphatase and NADP+(-)isocitrate dehydrogenase observed in Group B were corrected by 1,25-dihydroxyvitamin D3 supply. Acyl phosphatase showed a remarkable increase in consequence of 1,25-dihydroxyvitamin D3 administration.
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PMID:Vitamin D--related modification of enzyme activities in synaptosomes and mitochondria isolated from rat cerebral cortex. 862 85

We examined a chloride (Cl-)-dependent K+ transport (K(+)-Cl- cotransport) and regulatory volume decrease in dog red blood cells with high K+, low Na+, and high glutathione (GSH) content (HK/HG) due to the presence of an Na(+)-K+ pump. The HK/HG cells were separated according to their density, and the age-marker enzyme activities, such as glucose-6-phosphate dehydrogenase and cholinesterase, were determined. Unexpectedly, we found that young cells were heavier (more dense) and smaller in size compared with the old cells, which were lighter (less dense) and larger. The K(+)-Cl- cotransport was nearly 10-fold higher in the most dense cells, representing a 12% fraction of the total population compared with the lightest cohort. Although K(+)-Cl- cotransport in both the dense and the light cells was activated by N-ethylmaleimide, swelling and depletion of cellular divalent cations and the activation of the transport in the dense cells was greater. Both the dense and light cells regulated their volume when they were isosmotically swollen. Therefore, the lower activity of K(+)-Cl- cotransport might not explain the relative large volume in old HK/HG cells. The concentration of GSH and glutamate was higher in the light cells. Thus the higher the GSH and glutamate concentration, the greater the cell volume and the lower the K(+)-Cl- cotransport.
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PMID:K(+)-Cl- cotransport and volume regulation in the light and the dense fraction of high-K+ dog red blood cells. 932 78


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