Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rats were exposed to a simulated altitude of 25,000 ft for 4 h in a decompression chamber, and the activity of some tissue enzymes estimated. Succinate dehydrogenase activity was significantly decreased and cholinesterase activity significantly elevated in the brain homogenates of the hypoxic rats, succinic dehydrogenase activity was significantly increased. There was no change in the activity of Mg+2-ATPase and Na+-K+-ATPase in the microsomal fractions of liver or brain homogenates of the hypoxic animals.
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PMID:Effect of acute hypoxia on the enzymes involved in the metabolic and nervous functioning of rat brain. 12 97

A study in the enzymatic properties of muscle membranes established that sarcolemma of the rabbit skeletal muscles contains the Ca2+-ATPase system which does not require Mg2+ for manifestation of ions activity. By some kinetic properties it differs from ATPase of myosin. The complex Ca-ATP2+ is a substrate of Ca2+-ATPase. Ions of a series of bivalent metals inhibit the latter as well as the passive transport of Ca2+, that may evidence for a definite relation of Ca2+-ATPase with Ca+2 transport in skeletal muscles. Acetyl cholinesterase and AMP-aminohydrolase are strongly bound with the sarcolemma. The sarcolemma structural organization is shown to play a certain role in manifestation of their activity. On the basis of the data obtained when studying the activity in the ATPase systems and dynamics of formation and decay of the intermediate phosphorylated product in the microsomal fraction of cow and rabbit myometrium certain peculiarities are established for the active mechanisms of Ca2+ transport in smooth muscles. A problem is under discussion on the possible active participation of sarcolemma in regulation of Ca2+ concentration in the smooth muscle cells. Two ATPase systems, Mg2+-dependent and Mg2+-dependent Ca2+ activated are found in nuclei; the role of lipids of the skeletal muscles in manifestation of their activity is studied. AMP-amino hydrolase properties are characterized for different areas of the sarcoplasmatic reticulum membranes. The model of E-avitaminous muscular distrophy was used to show disturbances in the structure of sarcolemma and membranes of the sarcoplasmatic reticulum which are accompanied by changes in their ATPase and Ca2+-transporting properties.
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PMID:[Enzymatic properties in muscle membranes]. 12 74

Exposure of rat brain Na+ + K+-ATPase (ATP phosphohydrolase E.C. 3.6.1.3) to concentrations of cassaine greater than 1 x 10(-4) M resulted in a poorly reversible inhibition of this enzyme. Inhibition did not require the presence of ATP and developed rapidly, but the final amount of inhibition observed was independent of time. The amount of inhibition observed at a given concentration of cassaine was reduced by increasing the concentration of membranes in the system. The inhibition of Na+ + K+-ATPase activity was associated with equivalent inhibition of the phosphorylation and (3H)-ouabain binding reactions of this enzyme, while the uninhibited enzyme was apparently kinetically normal. Concentrations of cassaine which produced this stable inhibition of Na+ + K+-ATPase had no effect on the Mg2+-activated ATPase or the NADH cytochrome-c-reductase activities of crude rat brain microsomal preparations. Cassaine inhibited the cholinesterase activity of rat brain microsomes with a Ki of about 5 x 10(-5) M, but his inhibition was fully reversible. The poorly reversible inhibitory actions of cassaine, thus, appeared specific for Na+ + K+-ATPase. Because this stable pattern of inhibition of the Na+ + K+-ATPase by cassaine required drug concentrations at least one hundred-fold greater than those which produce positive inotropic effects, it appears unlikely that this pattern of Na+ + K+-ATPase inhibition is involved in the cardiotonic actions of this drug.
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PMID:Studies on the stable inhibition of Na+ + K+-ATPase by cassaine. 13 Feb 44

The effect of tricresylphosphate (TCP) was studied in vitro and in vivo on the rat liver and brain enzymes acetylcholinesterase (ACC), butyrylcholinesterase (CHE), arylesterase (ARE), aliesterase (ALI), and the microsomal nicotinamide-adenine dinucleotide phosphate oxidase (NADPH2-oxidase) system. The results show that, in the male rat, TCP given intraperitoneally induces an increase in liver microsomal ARE AND NADPH2-oxidase and a decrease in ALI and cholinesterase; no activation of ARE and NADPH2-oxidase is observed in female rats.
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PMID:Effects of tricresylphosphate on esterase activity of rat serum and tissues. 46 77

Glutamate oxaloacetate transminase (GOT), glutamate dehydrogenase (GDH), sorbitol dehydrogenase (SDH), pseudo-cholinesterase (ChE) and various blood constituents were measured in the plasma of Japanese quail fed 1,1-di(p-chlorophenyl)-2-chloroethylene (DDMU) at low levels for periods ranging from 2 to 32 days. Previous work has shown that DDMU is a potent inducer of hepatic microsomal enzymes causing marked structural changes in the liver. A rapid increase in plasma GOT was observed within 4 days accompanied by an increase in relative liver weight. Plasma GDH and SDH increased to a maximum between 16 and 24 dyas which seems to be associated with hepatic cell proliferation. Plasma ChE showed a steady increase over the time course of DDMU administration. The level of plasma lipid was reduced after 4 days whereas the hepatic lipid content was substantially increased suggesting that the fatty liver condition may be caused by decreased release of triglyceride from the liver. Plasma glucose was reduced at 8 days but there was no evidence of a hyperglycaemic state. The changes noted after 2 days of DDMU diet were confirmed by measurements on birds 18 h after oral dosing the DDMU. The study demonstrates the value of plasma enzyme measurements for the early detection of toxic effects and indicates that DDMU administration leads to extrahepatic effects in addition to those previously described in the liver.
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PMID:The effects of 1,1-di(p-chlorophenyl)-2-chloroethylene on plasma enzymes and blood constituents in the Japanese quail. 46 32

Pretreatment of rats with 10 mg of ethylestrenol (17alpha-ethylestr-4-en-17beta-ol) by force feeding twice daily for three days and once on the fourth day decreased the severity of parathion (0,0-diethyl 0-4-nitrophenyl phosphorothioate) toxicity and caused a 150% increase in the parathion LD50 in male animals. It decreased by 51% cholinesterase inhibition in the brain caused by i.p. injection of 2 mg of parathion/kg body weight but not that of an equitoxic dose (0.5 mg/kg) of its active metabolite, paraoxon (0,0-diethyl 0-4-nitrophenyl phosphate). It decreased by 29% cholinesterase inhibition in plasma following i.p. administration of parathion but caused only a 16% decrease in cholinesterase inhibition following administration of the equitoxic dose of paraoxon. It did not protect against brain cholinesterase inhibition by 4 mg/kg of parathion given i.v.; however, brain parathion levels were 16% lower in rats pretreated with ethylestrenol than in control rats. It increased the rate of inactivation of both parathion and paraoxon by liver microsomal enzyme preparations. Thus enzyme induction seems to account for the protection afforded by ethylestrenol to toxicity following poisoning by organophosphates.
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PMID:The protective effects of ethylestrenol against acute poisoning by organophosphorus cholinesterase inhibitors in rats. 63 20

The subcellular distribution of cholinesterase (ChE) was studied in the gastrocnemius muscle of rats after strong or weak nerve crushing. The ChE activities of muscle were decreased to a greater extent by strong crushing than by weak crushing. In particular, the ChE activity of the fraction containing sarcoplasmic reticulum was most greatly decreased. These results suggest that the change in the ChE activity of the microsomal fraction most finely reflects the strength of nerve crushing.
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PMID:Changes in cholinesterase activity of muscle after crushing the sciatic nerve of rats. 65 90

In an analysis of the gastrocnemius muscle, the microsomal fraction showed the highest cholinesterase (ChE) activity. The ChE activity of all fractions decreased to a greater extent after strong nerve crushing than after weak crushing. This change in the activity in the microsomal fraction was the most marked change observed. Although in the analysis of the soleus muscle the ChE activity was measured only in the homogenate and in the microsomal fraction, the results were the same as those obtained with the gastrocnemius. A preparation of vitamins B1, B2, and B12 (B complex) had little effect on the ChE activity in the gastrocnemius muscle. In the soleus muscle on the lesion side, the B complex increased the ChE activity to some extent after nerve crushing, but such was not significant. However, the B complex signifiicantly increased this activity in the soleus on the intact side. In the soleus muscle, strong nerve crushing induced more marked muscle atrophy than weak crushing. On the other hand, no significant difference was found in the gastrocnemius. Effects of the B complex on muscle atrophy were found in the soleus, but not in the gastrocnemius. These results suggest that the ChE activity in the microsomal fraction containing sarcoplasmic reticulum reflects the nervous disorders clearly, and that the B complex increases the ChE activity and muscle weight in the soleus, but not in the gastrocnemius muscle.
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PMID:[Changes in cholinesterase activity of gastrocnemius and soleus muscles of the rat after crush of the sciatic nerve, and effects of a vitamin B complex on those changes (author's transl)]. 75 Mar 31

A number of commercial and candidate flame retardants were studied with regard to their toxicity to goldfish, inhibition of cholinesterase, inhibition of acetyl choline binding to its receptor and insecticidal properties. Several of the flame retardants were notably toxic to fish. Some of the compounds showed modest inhibition of cholinesterase and/or microsomal oxidases, but none inhibited acetyl choline receptor binding. Whereas several of the flame retardants showed little or no insecticidal properties when added alone to a housefly diet, piperonyl butoxide greatly synergised their toxicity to houseflies.
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PMID:Further toxicologic studies with commercial and candidate flame retardant chemicals. Part II. 88 Mar 89

The exposure of adult male rats to 200 ppm of tetrachlorethylene t hours daily for 4 days resulted in a marked sequestration of solvent in perirenal fat 17 hours after the last exposure period. Similar exposure of similar rats to 500 ppm of dichlormethane led to a lesser accumulation of the solvent in fat as studied at the same time. Further exposures on the fifth day increased promptly the solvent contents of various organs. The exposure to tetrachlorethylene caused a diminished brain RNA content on the fifth day with simultaneous increase in the activity of non-specific cholinesterase. Similar changes in the RNA content were not seen in experiments with dichlormethane while the activity of acid proteinase increased above the control level in brain. Observations on the performance of the same animals in an open-field situation revealed that ambulation was affected in experiments with tetrachlorethylene immediately after exposure while preening pattern was changed after exposure to dichlormethane. Analysis on liver microsomal cytochrome P-450 content displayed slight increases in the hemochrome content in both experiments. The present data indicated that a rather modest exposure to both solvents could cause significant solvent accumulation in the fat and brain with marked effects on rat behaviour and protein metabolism in brain while changes in liver cytochrome P-450 content might not reflect the magnitude of these changes.
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PMID:Biochemical and behavioural effects of inhalation exposure to tetrachlorethylene and dichlormethane. 92 19


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