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)

(1) Cholinesterase activity was investigated in some human lymphatic organs (palatine tonsil, 'normal' spleen, 'bilharzial' spleen, thymus, lymph node and appendix) using GOMORI'S modification of KOELLE and FRIEDENWALD'S thiocholine iodide method, hydrolyzing acetylthiocholine iodide and butyrylthiocholine iodide. (a) Acetyl- and butyrylcholinesterases seemed to be different enzymes; but when they have the same pattern of activity, the latter generally offers a weaker reaction. (b) All the lymphatic follicles of the tonsil, those found in the cortex of the cervical lymph nodes as well as those present in the appendix, were stainable with both acetyl- and butyrylcholinesterase. (c) Acetylcholinesterase activity was not demonstrated in the Malpighian bodies of the 'normal' spleen, but the reaction was strongly present in the blood vessels (including the central arterioles) as well as in the capsule and the different components of the trabecular system. (d) In 'bilharzial' splenomegaly a relatively strong activity started to appear in the Malpighian corpuscles, manifested as a brownish precipitate in their centres. Also some patchy positive areas began to make their appearance in the tissue of the red pulp and had a particular arrangement around the Malpighian corpuscules, in such a way as to 'wall them off' from the tissue of the red pulp. (e) In the thymus no acetylcholinesterase activity was encountered, except in Hassal's corpuscles and in the trabeculae between the thymic lobules. (2) The data obtained in this work were discussed in relation to previous works in other laboratories and it seems that a species difference exists. (3) Cholinesterases may be present in the lymphatic tissue in order to get rid of some potentially toxic esters resulting from the necrobiotic phenomena accompanying the high mitotic activity found especially in the germinal centres of the lymphoid follicles. (4) There are many unanswered questions about the coexistence of the phosphatases and cholinesterases in the same places; their concomitant association in the lymphatic tissue may represent a special case within the framework of a more general mechanism.
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PMID:Cholinesterase activity in some human lymphatic organs. 95 94

A screening aimed at obtaining a cholinesterase inhibitor of microbial origin was carried out using Pseudomonas butyrylcholinesterase. A mycelium-extract of a fungus strain, belonging to the genus Penicillium, was found to produce such an enzyme inhibitor. The inhibitor was purified and crystallized as colorless leaflets. From physical and chemical studies, the inhibitor was identified as being identical with an antibiotic, mycelianamide, though this compound was not known to have enzyme inhibitor activity. The kinetics of the inhibition of Pseudomonas butyrylcholinesterase were also studied. Horse serum cholinesterase and hog liver carboxylesterase were also inhibited by the isolated Penicillium C-81 inhibitor, but lipase and acetylcholinesterase were not.
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PMID:A butyrylcholinesterase inhibitor produced by Penicillium sp. no. C-81 and its identity with mycelianamide. 95 41

The inhibitory effect of 3-diethylaminophenyl-N-methylcarbamate methiodide on rat brain acetylcholinesterase and horse plasma butyrylcholinesterase was studied in vitro. This quaternary carbamate is a more potent inhibitor of acetylcholinesterase than butyrylcholinesterase. Complete inhibition of acetylcholinesterase may be achieved without any inhibition of butyrylcholinesterase, i.e. that 3-diethylaminophenyl-N-methylcarbamate methiodide is a selective inhibitor of acetylcholinesterase. The inhibitory effect of different doses of this compound on plasma and liver butyrylcholinesterase and erythrocyte, brain, heart and diaphragm acetylcholinesterase of the rat was studied in vivo. With increasing doses of carbamate the inhibition of the enzymes in the plasma, erythrocytes, liver, heart, and diaphragm increased while the brain acetylcholinesterase was unaffected. The toxic action of carbamate studied was preferably due to acetylcholin esterase inhibition in the peripheral nervous system and this compound cannot penetrate the blood-brain barrier.
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PMID:Anticholinesterase action of 3-diethylaminophenyl-N-methyl-carbamate methiodide in vitro and in vivo. 97 52

The visual and somatic sensory cortex were investigated. The activity of acetylcholinesterase and lactate dehydrogenase was similar in the pretrigeminal and non-operated cats. The activity of these two enzymes, as well as that of choline acetyltransferase, butyrylcholinesterase and acid phosphatase was similar 3 and 8 h after the pretrigeminal transection. Results support the possibility of utilizing the pretrigeminal cat for investigations of biochemical correlates of learning.
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PMID:Activity of some enzymes in the cortex of the cat with pretrigeminal brainstem transection. 97 Feb 47

Strips of muscle from innervated and denervated rat hemidiaphragm were tested for sensitivity to acetylcholine and to carbachol. For both agonists, denervation (6-8 days) produced notable supersensitivity. However, the increase in sensitivity to acetylcholine (ca. 600-fold) was much greater than that to carbachol (ca. 51-fold). Denervation also produced an increase in [3H]alpha-bungarotoxin binding (ca. 20-fold), presumably indicative of an increase in the number of acetylcholine receptors. In addition to causing increases in tissue sensitivity and receptor number, denervation caused a marked loss of acetylcholinesterase activity (ca. 70%) and a modest loss of butyrylcholinesterase activity (ca. 20%). When innervated muscle was pretreated with eserine (5 X 10(-5) M), there was a loss of acetylcholinesterase activity (ca. 86%) and butyrylcholinesterase activity (ca. 36%). Simultaneously, there was an increase in tissue sensitivity to acetylcholine (ca. 26-fold). When denervated muscle was pretreated with eserine, there was no loss of enzyme activity beyond that caused by denervation. Furthermore, eserine pretreatment did not increase denervated muscle sensitivity to acetylcholine. The data suggest that both an increase in acetylcholine receptors and a decrease in acetylcholinesterase activity contribute to the phenomenon of denervation supersensitivity.
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PMID:The role of acetylcholine receptors and acetylcholinesterase activity in the development of denervation supersensitivity. 97 56

Influence of conditioned electro-defensive training of different duration and intensity on the weight and biochemical characteristics (activity of acetylcholinesterase and butyrylcholinesterase) of different parts of the brain was studied in rats of various genetic lines. It has been shown that the minimal duration of training leading to changes in the investigated characteristics in the experimental rats as compared with the controls, amounted to 30 days. Positive correlation has been found between the capacity for learning, the weight of the cortex and the activity of its acetylcholinesterase. A different degree of changes in the indicated characteristics has been revealed in various lines of rats used in the experiments.
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PMID:[Effect of conditioned reflex defense training on the level of cholinesterase activity and weight of the rat brain]. 101 93

The paper deals with a detailed histochemical mapping of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) in the diencephalon and mesencephalon of Uromastix hardwickii. In AChE in contrast to BChE preparations, most of the nuclei reveal intense activity Interestingly, the hypothalamic nuclei demonstrate positive reactions to AChE but totally negative reactions in BChE preparations. The enzymatic activity in fiber tracts is totally negative for AChE; on the contrary, it is intensely positive for BChE. Neurosecretory substance, in the hypothalamic region, is positive for the two preparations of the enzymes. The role of these enzymes, as related to the functional activities of the various nuclei and fiber tracts, has also been discussed.
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PMID:Histoenzymological mapping of acetylcholinesterase and butyrylcholinesterase in the diencephalon and mesencephalon of Uromastix hardwickii. 101 94

A hydrolysis of suberyldicholine and monocholic ester of suberic acid by butyrylcholinesterase was studied. In the region of Sopt the rates of suberyldicholine hydrolysis were slightly below and under S less than Sopt they were far in excess of the rates of acetylcholine hydrolysis. The following kinetic constants of hydrolysis were obtained: for suberyldicholine--Km=2.3-10(-5)M, V=2.4 mcM/mg. min, Kss=7.2-10(-2)M; for monocholic ester of suberic acid--Km=7.5-10(-4)M, V=1.5 mcM/mg, min, Kss=1.2-10(-2)M (25 degrees, pH 7.5, 0.1 M KCl). Suberyldicholine was shown to be highly active reversible inhibitor of competitive--non-competitive type (Ki=2.3-10(-6)M, alpha=0.5) of acetylcholinesterase from human erythrocytes; the inhibitory effect of monocholic ester of suberic acid was distinctly lower. By biological and indirect biochemical methods it was found that low concentrations of suberyldicholine 10(-5)=10(-6)M (similar to concentrations that were in an organism upon myorelaxation) were hydrolyzed by acetlycholinesterase with the rate, approximately equal to the rate of acetylcholine hydrolysis. The reversible binding and the enzymatic hydrolysis of suberyldicholine by acetylcholinesterase of tissues were likely to be the main factors that determined the effectiveness and prolonged blocking action of suberyldicholine on the nerve-muscle conductivity.
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PMID:[Enzymatic hydrolysis and reversible binding of suberyldicholine by cholinesterases]. 103 Aug 81

Persistent selective suppression of the butyrylcholinesterase (cholinesterase; acylcholine acyl-hydrolase, EC 3.1.1.8) activity of the superior cervical, stellate, and ciliary ganglia of cats by the daily administration of tetramonoisopropyl pyrophosphortetramide, 3.0 mumol/kg, intravenously, for 6 days produced a significant elevation in the levels of ganglionic acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7). When the same procedure was preceded by the inactivation of over 95% of the ganglionic acetylcholinesterase by sarin, 2.0 mumol/kg, intravenously, the rate of regeneration of acetylcholinesterase was decreased. Results are interpreted as evidence that ganglionic butyrylcholinesterase may serve as a precursor to acetylcholinesterase, and that the level of butyrylcholinesterase may regulate the rate of acetylcholinesterase synthesis.
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PMID:Effects of persistent selective suppression of ganglionic butyrylcholinesterase on steady state and regenerating levels of acetylcholinesterase: implications regarding function of butyrylcholinesterase and regulation of protein synthesis. 106 4

The nature of the cholinesterase activity present on the wall of blood vessels in amphibian brain has been studied histochemically. It is concluded that the enzyme involved is acetylcholinesterase rather than butyrylcholinesterase, which more frequently occurs in the blood vessels of the brain of other vertebrates. The histochemical results are in agreement with most biochemical data concerning substrate specificity and inhibitor response for both acetylcholinesterase and butyrylcholinesterase. The two main hypotheses put forward by others in order to explain cholinesterase activity in brain vessels are discussed briefly.
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PMID:Histochemical characterization of cholinesterase activity in the frog brain with special reference to its localization on the wall of blood vessels. 108 70


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