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)

Following the implantation of cobalt-gelatine pellets into the frontal cortex, epileptiform spikes in both primary and secondary foci developed and reached a peak between 7-12 days post implantation. Histological examination showed a necrotic lesion with terminal and fibre degeneration in brain areas connected with the frontal cortex. Golgi staining at 60 days showed a loss of pyramidal cells in the primary focal area. In the lesion and primary focal areas GABA, glutamate and aspartate were significantly reduced between 5--10 days post implantation. No changes in glutamine and glycine were found in either the lesion or pulmonary focus. No changes in amino acid content were found in the secondary focus or in glass implanted controls at any time. In cobalt-treated rats there were significant reductions in the transmitter related enzymes, glutamate decarboxylase, acetylcholinesterase, choline acetyltransferase and aromatic amino acid decarboxylase in the lesion area and primary and secondary foci at 4--8 days post implantation. Levels of these enzymes had recovered to normal by 24 days. Lactate dehydrogenase was reduced only in the lesion area. Beta-Galactosidase was reduced in the lesion area at 4 days but subsequent rose rapidly paralleling increasing gliosis around the lesion. It is concluded that cobalt-induced epilepsy is associated with relatively selective loss of neuronal tissue and provides a useful model for further investigation relevant to clinical epilepsy.
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PMID:Neurochemical and morphological changes during the development of cobalt-induced epilepsy in the rat. 113 20

Serum cholinesterase (ChE) and Lactate dehydrogenase (LDH) activities were estimated in 40 cases of carcinoma breast, 25 cases of benign tumours and compared with healthy controls (30 cases). Significant difference in enzyme activities were obtained between benign and malignant neoplasms of the breast when compared with each other as well as when compared with healthy controls. Also, there were significant enzyme changes between non-metastatic cases and those with metastasis and when Stage I and Stage II cancers were compared with those in Stage III and Stage IV. No difference in enzyme levels were recorded between pre and post-operative cases and in different types of breast cancers. While ChE was depressed in 80 per cent cases of malignancy breast, serum LDH was raised in 73.3 per cent cases.
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PMID:Diagnostic and prognostic significance of serum cholinesterase and lactate dehydrogenase in breast cancer. 175 38

Intoxication with an acute dose of carbofuran (1.5 mg/kg, sc) in male Sprague-Dawley rats evoked severe toxic manifestations characteristic of hypercholinergic preponderance with profound muscle fasciculations and convulsions during 30-60 min, lasting for about 2 h. Lactate dehydrogenase, a "biomarker" cytoplasmic enzyme catalyzing the reversible reaction of lactate-pyruvate, was represented by five electrophoretically distinct isoenzymes in the serum and tissues. The amounts of each isoenzyme in different tissues were widely varied and consequently the patterns were tissue specific. A 24-h time-course following carbofuran administration indicated a two-fold increase in the activity of total LDH in serum and more than 30% in hemidiaphragm and liver. The patterns of LDH isoenzymes in serum revealed a significant (P less than 0.01) increase in all the isoenzymes except LDH-4 (64% decrease). Analysis of each tissue revealed characteristic changes in LDH isoenzyme patterns indicating organ-specific tissue damage. These alterations in LDH and its isoenzymes, in addition to acetylcholinesterase inhibition, may be directly or indirectly related to the mechanism(s) of the toxic action, and also provide insight into the site/organ(s) of toxic injury, thus providing an early prognostic indicator.
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PMID:In vivo alterations in lactate dehydrogenase (LDH) and LDH isoenzymes patterns by acute carbofuran intoxication. 195 80

Some biochemical parameters of liver and liver microsomes were studied in albino rats following administration of cobra and viper venoms at dose of 2 mg/kg body weight. The total protein content in cobra venom treated (CVT) animals and DNA and RNA contents of liver and liver microsomes were almost unaltered in both the venom treated animals while total protein content was significantly reduced in viper venom treated (VVT) animals. Alkaline and acid phosphatases activities of whole liver showed significant increase in both the venom treated animals whereas the rise in cholinesterase activity in CVT animals was not significant. Lactic acid content was significantly higher in CVT animals compared to either VVT animals or controls. The glycolytic enzymes viz., aldolase, phosphohexose isomerase and lactate dehydrogenase measured in hepatic microsomal fraction were significantly reduced while alanine and aspartate aminotransferases and gamma-glutamyl transpeptidase activities of liver microsomes were significantly elevated in both the venom treated animals compared to controls.
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PMID:Biochemical studies of liver & liver microsomes in envenomated rats. 227 76

Ascaridia galli and Heterakis gallinae obtained from the common fowl Gallus gallus were exposed to 10(-2)-10(-5)M levamisole and albendazole; both compounds caused death of the parasites in vitro. The effect of the drugs was investigated on homogenates of the treated worms. Albendazole, at 10(-2)M, inhibited oxaloacetate reduction by 67 and 53% and malate oxidation by 21 and 17% in A. galli and H. gallinae, respectively, whereas 10(-4)M levamisole completely inhibited malate dehydrogenase activity in both directions in the two parasites. Lactate dehydrogenase was not affected significantly by either anthelmintic. Aldolase activity was diminished by 57 and 32% in A. galli and H. gallinae, respectively, with 10(-4)M levamisole. Levamisole at 10(-4)M also inhibited the activity of acid and alkaline phosphomonoesterase and cholinesterase. Albendazole had no significant effect on these enzymes in either parasite. Malate dehydrogenase and cholinesterase activity of the host tissue (intestine and caecum) was also reduced significantly with 10(-2) and 10(-3)M levamisole. These studies indicated a multiple mode of action of levamisole and albendazole.
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PMID:The effect of levamisole and albendazole on some enzymes of Ascaridia galli and Heterakis gallinae. 270 87

The intraperitoneal (IP) treatment of rats with diazinon (40 mg/kg) resulted in a variety of changes in the brain. Glycogen was depleted, but there was an increase in the activities of glycogen phosphorylase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and fructose 1,6 diphosphatase. The activity of glucose-6-phosphatase was unaffected while that of cholinesterase was significantly reduced. Lactic acid content was increased, while that of pyruvate was not altered. Animals developed tremors and convulsions, which were maximal two hours after treatment. The induced changes may be compensatory mechanisms to provide extra energy to cerebral tissue as a result of the stimulatory effects in diazinon-treated animals.
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PMID:Cerebral glucose and glycogen metabolism in diazinon-treated animals. 350 78

Effect of diazinon (10,20 and 40 mg/kg, i.p.) on the level of blood glucose in rats was investigated. Hyperglycaemia peaked 2 h after i.p. treatment with 40 mg/kg diazinon. The cerebral acetylcholinesterase activity was significantly reduced. The blood level of pyruvic acid was unchanged while that of lactic acid was significantly increased. Convulsions and biochemical changes caused by diazinon (40 mg/kg) were prevented by diazepam injected immediately after diazinon. In diazinon-treated hyperglycaemic animals, the glycogen content of the brain was depleted, the activities of glycogen phosphorylase, phosphoglucomutase and hexokinase were significantly increased and the activity of glucose-6-phosphatase remained unchanged. Lactate dehydrogenase activity was also increased by treatment with diazinon. The induced changes may compensate for the energy requirement of stimulatory effects caused by diazinon.
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PMID:Changes in cerebral glycogenolysis and related enzymes in diazinon treated hyperglycaemic animals. 362 68

Isolation of neurons from rat forebrain and cerebellum has been performed by a method including trypsin incubation and tissue disaggregation by filtration through successive nylon meshes with a different pore size. Phase contrast microscopy shows highly purified cell preparations. Lactate dehydrogenase, acetylcholinesterase and (Na+-K+) ATPase activities indicate that neurons possess a high cytosolic content and show a good preservation of the plasmatic membrane.
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PMID:Neurons from rat forebrain and cerebellum. Isolation and biochemical characterization. 608 29

Twenty eight enzymatic activities and four macromolecular substances have been histochemically compared in rat and rabbit aortas, embedded in a common block. The study was carried out at different stages of development: 3 days, 3 months, 7-9 months and 17-19 months. In addition, lipase and cholinesterase were biochemically assayed in adult rat and rabbit aortas. The rat aortas (atheroresistant) had a better supply of aerobic oxidoreductases [linked to the pentose pathway (G6PD, 6PGD) as well as to the Krebs cycle (SD, ICD)], lipolytic enzymes (acid esterases, cholinesterase, lipase), lysosomal enzymes (acid PH/ase, Aryl-sulf/ase - Betaglu/ase), ADPase - ATPase - AlK Ph/ase Alpha GPD and acid lipids. Rabbit aortas (atherosensitive) were richer in metachromatic GAG, UDPGD (GAG Anabolism), glycogen, and related enzymes (phosphorylase, glycogen synthetase) as well as 5'-nucleotidase, Beta HBD, Lactate D and Aldolase. These differences support the hypothesis that arterial atherosensitivity is related to the activity and efficiency of smooth muscle cell energetic and catabolic processes, which govern the behaviour of lipids, proteins and carbohydrates as they penetrate the arterial wall. The factors that determine the proliferative and sclerogenic responses of arterial tissues to aggressions and, in particular, the response to lipids, remain, however, to be determined.
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PMID:A comparative study of the arterial tissue metabolism in atherosensitive and atheroresistant species. I. Comparison between rabbit and rat aortas. 734 89

We designed the present study to examine whether or not the inhibition of acetylcholinesterase modulates cerebral microcirculation in hypotension and improves brain metabolism in ischemia induced by bilateral carotid artery occlusion in hypertensive rats. Blood flow to the parietal cortex was determined by the H2 clearance method. Lactate, pyruvate, and ATP were estimated by enzymatic methods. Acetylcholinesterase inhibitor (AChEI, ENA-713), at 0.05, 0.1, or 0.5 mg/kg, was intravenously injected 10 min before either hemorrhagic hypotension or cerebral ischemia. The levels of acetylcholine in the control were 29.3 +/- 8.1 (mean +/- SD) and 39.5 +/- 8.1 pmol/mg in the cortex and hippocampus, respectively, and they were significantly decreased by 15-19% after 60 min of ischemia in the vehicle-treated rats. AChEI preserved the levels to 93-98% of the control (p < 0.05 versus vehicle). The lower limit of autoregulation was 74 +/- 9% of the resting values. The administration of AChEI helped preserve blood flow and lowered the limit to 64 +/- 6% (p < 0.05 versus control). After 60 min of ischemia, lactate increased 6.5-fold and ATP decreased to 64% of the control value. The administration of AChEI dose-dependently reduced the lactate level 1.9- to 3.9-fold and well preserved the ATP level to 94-97% of the control. The inhibition of acetylcholinesterase activity may preserve cerebral autoregulation during hypotension and protect cerebral metabolism against ischemic insult.
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PMID:Inhibition of acetylcholinesterase modulates the autoregulation of cerebral blood flow and attenuates ischemic brain metabolism in hypertensive rats. 767 77


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