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)

This work was undertaken to study the myelination and cholinesterase activity of the developing white matter of chick embryo spinal cord from the 6th day of incubation until hatching. Myelination of the white matter was always preceeded by the aggregation of neuroglial cells. The sequence of myelination in the cervical and thoracic segments was from before backwards, whereas in the lumbosacral segments it was from behind forewards. Myelination of the ventral column extended craniocaudally, whereas in the posterior column is extended caudocranially. True cholinesterase activity was encountered in the spinal white matter only before and during the process of myelination and was closely associated with the sites of neuroglial aggregations. No pseudocholinesterase activity could be seen in the white matter before myelination. However, during the period of active myelination, enzymatic activity was seen only at the sites of formed myelin and after myelination of all tracts; the whole white matter reacted positive for the enzyme. The significance of these findings is discussed.
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PMID:Myelination and cholinesterase activity of chick embryo spinal cord. 89 12

The distribution and morphologies of neurons containing acetyl cholinesterase (AChE, EC 3.1.1.7) in the thalamus and hypothalamus of the rat were studied by means of a pharmaco-histochemical technique involving staining for AChE (Karnovsky-Roots' procedure) at various times after administration of bis-(u-methylethyl)phosphorofluoridate. This method enables visualization of individual AChE-containing neuronal somata and their processes to a degree not possible with other protocols for the enyzme. The strongest AChE activity occurring at the level of the thalamus is found within the small, round to oval, somata of nucleus anterior dorsalis. Most of the intralaminar nuclei, as well as nucleus reticularis, are composed of medium-sized multipolar neurons displaying moderate to strong AChE activity. Moderately stained AChE neurons are also found in pars ventralis of nucleus geniculatus lateralis and in pars lateralis of nucleus habenularis. Most of the neurons of the lateral and posterior thalamic territories, however, are nearly devoid of AChE. At the level of the hypothalamus, the neurons of nuclei supraoptics and paraventricularis show strong AChE activity. The AChE neurons of nucleus supraopticus are surrounded by numerous AChE-containing processes of some large lateral preoptic area neurons that stain intensely for the enzyme. Numerous intensely stained AChE perikarya occur in the lateral, dorsal, and supra-mammillary hypothalmic areas. These neurons often possess several AChE-containing processes. Nuclei arcuatus and ventomedialis consist mainly of neurons displaying a weak to moderate intensity of AChE staining. At the level of the mamillary bodies most neurons show moderate AChE activity except the neuronal somata of nucleus mammillaris lateralis which stain very strongly for the enzyme.
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PMID:Organization and morphologies of acetylcholinesterase-containing neurons in the thalamus and hypothalamus of the rat. 99 69

The effect of reserpine on acetylcholine synthesis, choline acetylase and cholinesterase activity. Acta Physiol. Pol. 1975, 26 (1): 55-61. Reserpine-induced changes in ACh content in various tissues of white rats (cerebral cortex and brain stem, stomach, lungs, heart, spleen) and the effects of reserpine on the synthesis, enzymatic breakdown of ACh, and ChAc activity were studied. Reserpine administered subcutaneously caused a singificant rise in ACh content of the cerebral cortex and insignificant rise in the heart and spleen. Reserpine (in a concentration of 0.25 mug/ml) had no effect on ACh synthesis in vitro. Reserpine in vivo increased significantly ACh synthesis in the brain. No effect of reserpine on ChAc and AChE activity was demonstrated.
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PMID:The effect of reserpine on acetylcholine synthesis, choline acetylase and cholinesterase activity. 113 Feb 19

Histochemical study of the distribution of cholinesterases in the cat medulla oblongata reveals that all neurones in the dorsal motor nucleus of the vagus (DMV) contain true cholinesterase (AChE) but, while most contain this enzyme alone, a small proportion of cells contain pseudocholinesterase (BuChE) as well. Cervical vagotomy affects the two types of cell to different degrees of severity. The BuChE-containing neurones lose their enzyme completely within 2-3 weeks and they atrophy and disappear as a result of the operation. On the other hand, the reaction is less severe and is reversible in those cells containing AChE only. Vagotomy also causes reduction of AChE and BuChE staining in the nearby area subpostrema; the depletion here is pronounced at 2-3 weeks and recovery occurs within the year. These findings suggest that some cells in the area subpostrema project peripherally via the vagus and that the area is part of the vagal nuclear complex. Moreover, capilllaries in the area contain AChE and BuChE in the endothelial lining and this is one of the few areas of the cat hindbrain to exhibit such vascular enzyme activity. The ependyma of the area postrema, which overlies the area subpostrema, is heavily stained for BuChE but this is unaffected by vagotomy.
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PMID:Effects of vagotomy on the distribution of cholinesterases in the cat medulla oblongata. 119 96

On the basis of structural relationships between 5-hydroxytryptamine (5-HT, serotonine) and eserine, the effect of 5-HT on partially purified brain cholinesterase (ChE) was studied. The addition of 5-HT to brain ChE in vitro resulted in its inhibition, and the constants characterizing this inhibition, namely, the inhibition rate ki (5.44 X 10(2) mol-1/l - min-1), the equilibrium constant K (1.86 X 10(-3), and the rate constant for spontaneous reactivation kr (1.01 min-1) were determined. The inhibition of AChE by 5-HT in vitro was found to be of the competitive type.
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PMID:Inhibition of cholinesterase by 5-hydroxytryptamine. 124 80

Research was conducted upon 28 patients with a diagnosis of endogenous depression after their pharmacological treatment with imipramine or chlorimipramine. The investigation considered the interrelationship between psychophysiological parameters (heart rate, respiration rhythm, postural muscular tension) and the indices of the cholinergic and adrenergic systems (kinetic parameters of choline transport in the blood; Vmax, the activity of plasmic pseudocholinesterase, Che; blood acetylcholinesterase AChE, monoaminoxidase in blood platelets, MAO; and dopamine beta hydroxylase DBH). The results indicate that during relapse of endogenous depression there occurs an imbalance in the cholinergic-adrenergic systems which may be the result of some somatic symptoms typically found in the depression syndrome. The appearance, after pharmacotherapy, of a correlation between the indices of the activity of the cholinergic system with the respiratory rhythm suggest that the part played by the cholinergic mechanism in the regulation of autonomic processes normalizes itself during the course of successful therapy. The appearance of characteristic correlations between the activity of the cholinergic and adrenergic systems and the psychophysiological parameters in the presence of relatively low psychological stress seems to accompany successful treatment with imipramine and chlorimipramine.
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PMID:[Psychophysiological characteristics and metabolic indices of neurotransmitter metabolism in patients ill with endogenous depression]. 130 98

The pattern of molecular forms of acetylcholinesterase (AChE, EC 3.1.1.7) and butyrylcholinesterase (BChE, EC 3.1.1.8) separated by density gradient centrifugation was investigated in the brain and cerebrospinal fluid in Alzheimer's disease (AD), in human embryonic brain and in rat brain after experimental cholinergic deafferentation of the cerebral cortex. While a selective loss of the AChE G4 form was a rather constant finding in AD, a small but significant increase of G1 for both AChE and BChE was found in the most severely affected cases. Both in normal human brain and in AD a significant relationship could be established between the AChE G4/G1 ratio in different brain regions and the activity of choline acetyltransferase (ChAT). A similar decrease of the AChE G4 form as observed in AD can be induced in rat by experimental cholinergic deafferentation of the cerebral cortex. The increase in G1 of both AChE and BChE in different brain regions in AD is quantitatively related to the local density of neuritic plaques which are histochemically reactive for both enzymes. In human embryonic brain, a high abundance of G1 and a low G4/G1 ratio for both AChE and BChE was found resembling the pattern observed in AD. Furthermore, both in embryonic brain and in AD AChE shows no substrate inhibition which is a constant feature of the enzyme in the adult human brain. It is, therefore, concluded that the degeneration of the cholinergic cortical afferentation in AD as reflected by a decrease of AChE G4 is accompanied by the process of a neuritic sprouting response involved in plaque formation which is probably associated with the expression of a developmental form of the enzyme.
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PMID:Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development--a study of molecular forms. 130 64

To establish the chromosomal location of the human ACHE gene encoding the acetylcholine hydrolyzing enzyme acetylcholinesterase (ACHE, acetylcholine acetylhydrolase, E.C. 3.1.1.7), a human-specific polymerase chain reaction (PCR) procedure that supports the selective amplification of ACHE DNA fragments from human genomic DNA was employed with 19 human-hamster somatic cell hybrids carrying one or more human chromosomes. Informative ACHE-specific PCR fragments were produced from two cell lines, both of which include human chromosome 7, but not with DNA from 17 cell hybrids carrying various combinations of all human chromosomes other than 7. Fluorescent in situ hybridization of biotinylated ACHE DNA with metaphase chromosomes from human peripheral blood lymphocytes revealed prominent labeling on the 7q22 position. Therefore, further tests were performed to confirm the chromosome 7 location. DNA samples from the two cell lines including chromosome 7 and the ACHE gene were positive with PCR primers informative for the human cystic fibrosis CFTR gene, known to reside at the 7q31.1 position, but negative for the ACHE-related butyrylcholinesterase (BCHE, acylcholine acylhydrolase, E.C. 3.1.1.8) gene, mapped at the 3q26-ter position, confirming that these lines contain chromosome 7 but not chromosome 3. In contrast, three other cell lines including chromosome 3, but not 7, were BCHE-positive and ACHE-negative. In addition, genomic DNA from a sorted chromosome 7 library supported the production of ACHE- but not BCHE-specific PCR products, whereas with DNA from a sorted chromosome 3 library, the BCHE but not the ACHE fragment was amplified.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Mapping the human acetylcholinesterase gene to chromosome 7q22 by fluorescent in situ hybridization coupled with selective PCR amplification from a somatic hybrid cell panel and chromosome-sorted DNA libraries. 138 Apr 83

The administration of 2-pyridine aldoxime methyl chloride (2-PAM Cl) is a standard part of the regimen for treatment of human overexposure to many organophosphorus pesticides and nerve agents. However, some literature references indicate that poisoning by carbaryl (1-naphthyl N-methyl carbamate), an insecticide in everyday use, is aggravated by the administration of 2-PAM Cl. This effect has been reported in the mouse, rat, dog and man. We have found that the inhibition of both eel acetylcholinesterase (eel AChE, EC 3.1.1.7) and human serum cholinesterase (human BuChE, EC 3.1.1.8) by carbaryl was enhanced by several oximes. Based on 95% confidence limits the rank order of potentiation with eel AChE was TMB-4 = Toxogonin > HS-6 = HI-6 > 2-PAM Cl. By the same criterion, the rank order of potentiation with human BuChE was TMB-4 > Toxogonin > HS-6 = 2-PAM Cl. Carbaryl-challenged mice also reflected a potentiation since TMB-4 exacerbated the toxicity more than 2-PAM Cl. Our hypothesis is that certain oximes act as allosteric effectors of cholinesterases in carbaryl poisoning, resulting in enhanced inhibition rates and potentiation of carbaryl toxicity.
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PMID:Studies of the amplification of carbaryl toxicity by various oximes. 141 99

Purified fetal bovine serum acetylcholinesterase (FBS AChE) and horse serum butyrylcholinesterase (BChE) were successfully used as single pretreatment drugs for the prevention of pinacolyl methylphosphonofluoridate (soman) toxicity in nonhuman primates. Eight rhesus monkeys, trained to perform Primate Equilibrium Platform (PEP) tasks, were pretreated with FBS AChE or BChE and challenged with a cumulative level of five median lethal doses (LD50) of soman. All ChE-pretreated monkeys survived the soman challenge and showed no symptoms of soman toxicity. A quantitative linear relation was observed between the soman dose and the neutralization of blood ChE. None of the four AChE-pretreated animals showed PEP task decrements, even though administration of soman irreversibly inhibited nearly all of the exogenously administered AChE. In two of four BChE-pretreated animals, a small transient PEP performance decrement occurred when the cumulative soman dose exceeded 4 LD50. Performance decrements observed under BChE protection were modest by the usual standards of organophosphorus compound toxicity. No residual or delayed performance decrements or other untoward effects were observed during 6 weeks of post-exposure testing with either ChE.
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PMID:Use of cholinesterases as pretreatment drugs for the protection of rhesus monkeys against soman toxicity. 147 Nov 50


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