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:3.1.1.8 (cholinesterase)
12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The monoclonal antibody (mAb) 2G8 (subclass IgG2a) raised against acetylcholinesterase (AChE, EC 3.1.1.7) from electric organ of Torpedo nacline timilei crossreacted with AChE from Torpedo marmorata, electric eel (Electrophorus electricus), flounder (Platichthys flesus) body muscle, rat brain, bovine brain, and human brain, this suggests that the epitope to which mAb 2G8 bound had been highly conserved during evolution. No crossreaction was found with AChE from human and bovine erythrocytes, nor with butyrylcholinesterase (BtChE, EC 3.1.1.8) from human serum. Binding of mAb 2G8 to the globular G2 form of AChE from T. marmorata strongly decreased enzyme activity, while no significant inhibition was found with either collagen-tailed, asymmetric forms, or with the enzymes from flounder body muscle or mammalian sources. The possibility that mAb 2G8 bound to anionic sites of AChE could be excluded since neither edrophonium chloride nor decamethonium bromide influenced the binding of 2G8 to the enzymes. Enzyme-linked immunosorbent assay and Western blot showed that heat-denatured, diisopropylfluorophosphate-treated, CNBr- and trypsin-digested AChE from T. marmorata still reacted with mAb 2G8; this indicates that the epitope to which 2G8 bound, at least partially, belonged to a continuous determinant. Treatment of cholinesterases with N-glycosidase F abolished crossreaction with 2G8, showing that an essential part of the epitope consisted of N-linked carbohydrates.
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PMID:The monoclonal antibody 2G8 is carbohydrate-specific and distinguishes between different forms of vertebrate cholinesterases. 204 Feb 91

We have successfully demonstrated that exogenously administered acetyl- or butyrylcholinesterase (AChE, BChE respectively) will sequester organophosphates (OPs) before they reach their physiological targets. In addition, a third enzyme, endogenous carboxylesterase is known to be capable of scavenging OPs. In these studies, we have administered AChE and BChE to three different species of animals (mice, marmosets and monkeys) which were challenged with three different OPs (VX, MEPQ and soman). Results obtained from these systematic studies demonstrate that: (a) a quantitative linear correlation exists between blood AChE levels and the protection afforded by exogenously administered ChEs in animals challenged with OP, (b) approximately one mole of either AChE or BChE sequesters one mole of OP, (c) such prophylactic measures are sufficient to protect animals against OPs without the administration of any supportive drugs. Thus the OP dose, the blood-level of esterase, the ratio of the circulating enzyme to OP challenge, and the rate of reaction between them determine the overall efficacy of an enzyme as a pretreatment drug. The biochemical mechanism underlying the sequestration of various OPs by the use of exogenously administered scavenging esterases is the same in all species of animals studied. Therefore, the extrapolation of the results obtained by the use of ChE prophylaxis in animals to humans should be more reliable and effective than extrapolating the results from currently used multidrug antidotal modalities.
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PMID:Enzymes as pretreatment drugs for organophosphate toxicity. 205 84

Neurons dissociated from septal area of fetal (E 18-19) rat brain were grown for 7 days in culture. Cholinergic neurons were identified by cytochemical demonstration of acetyl cholinesterase. Addition of the nerve growth factor to the culture medium (200 u/ml) increases the number of AChE-positive neurons, the size of the cell body and activity of AChE in these neurons.
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PMID:[The effect of nerve growth factor on cholinergic neurons in dissociated cultures of the septum pellucidum]. 205 13

The biochemical changes of the elements of cholinergic neurotransmission (choline acetyltransferase, ChAT; acetylcholinesterase, AChE; butyrylcholinesterase, BuChE; and muscarinic cholinergic receptors, mAChR) as well as the electrolyte content were studied in ischemic lumbar spinal cord segments of newborn pigs. Ischemia was elicited by ligating the aorta for 30 min. Although no significant changes were observed in the sodium, potassium and calcium content of ischemic spinal cords, the calcium content was slightly elevated, to 119.3% of the control value. Whereas significant depletions were observed in both AChE and ChAT activities (to 69.1 and 87.7% of the control value, respectively), there was no significant change in BuChE activity as compared to the control value. The mAChR were also decreased, from 33.25 +/- 2.2 to 27.18 +/- 1.9 fmol/mg protein, while the Kd value was not significantly altered. It is concluded that even a relatively brief interruption of the oxygen supply can cause severe damage in the lumbar spinal cord of the newborn pig, affecting the cholinergic neurotransmission elements. This animal model might be suitable for studying the effects of hypoxia in newborns and children during chest operations involving the descending aorta.
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PMID:Effects of ischemia on cholinergic neurotransmission and electrolyte content in newborn pig lumbar spinal cord. 215 20

A stochastic simulation program was written to study the importance of residue variability in predicting excessive chronic (seasonal) cholinesterase (AChE) inhibition and acute illness among a cohort of agricultural harvesters grouped into crews exposed to AChE-inhibiting insecticides. It was concluded that residue variability can substantially affect the cohort's AChE level only for daily mean AChE inhibitions below 4% per day, increasing end-of-season mean AChE inhibition but actually decreasing the cohort's end-of-season variability. The incidence of acute individual and group (crew) AChE inhibitions in excess of that potentially producing clinical symptoms (assumed herein to be greater than 50% in a day), exhibits a fairly clear boundary as a function of a combination of the residue's mean and deviation. The predicted acute response accurately parallelled reported rates, thus validating the simulation model.
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PMID:Effects of organophosphate insecticide residue variability on reentry intervals. 222 Aug 37

The complete amino acid sequence of a mammalian acetylcholinesterase from fetal bovine serum (FBS AChE) is presented. This enzyme has a high degree of sequence identity with other cholinesterases, liver carboxyesterases, esterase-6, lysophospholipase, and thyroglobulin. The locations of 191 amino acids in 10 regions of the FBS enzyme were compared with corresponding sequences of Torpedo, human, and Drosophila AChEs and human serum butyrylcholinesterase (BChE). In one region there is a marked difference in both the number of amino acids and their sequence between mammalian AChE and other AChEs and the human serum BChE. The amino acid sequence of FBS AChE showed overall homologies of 90% with human AChE, 60% with T. california AChE, 50% with human serum BChE, and 39% with Drosophila AChE in these regions.
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PMID:Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases. 236 60

The monoclonal antibody AE-2 raised against acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) from human erythrocytes is shown to inhibit the enzyme activity. The reaction of the antibody with a structural epitope is investigated further. The epitope resides on monomeric, dimeric and tetrameric species of the enzyme. The rate of phosphorylation of the enzyme by diisopropylfluorophosphate was not affected by the antibody. On the other hand, inhibitors directed towards the anionic site(s) competed with antibody binding, suggesting that one of these is the epitope. The titration with antibody is biphasic and yields about 80% inhibition even in the presence of a large excess of antibody. Inhibition is fully reversible upon dilution, in a time-dependent manner. AE-2 also inhibited human adult and fetal brain acetylcholinesterase (to the same extent). However bovine brain acetylcholinesterase was inhibited to a lesser extent and rat brain acetylcholinesterase did not interact with the antibody. Butyrylcholinesterase (EC 3.1.1.8) also showed no reactivity towards the antibody.
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PMID:An inhibitory monoclonal antibody to human acetylcholinesterases. 243 22

Forty-five well clinically characterized patients with progressive dementia were investigated for lumbar cerebrospinal fluid (CSF) monoamine metabolites and cholinesterase activities. Monoamine concentrations were determined by reverse phase liquid chromatography with electrochemical detection and the cholinergic enzymes were measured photometrically. Firstly, all clinical and CSF parameters were studied in statistical cluster analyses to detect groups of variables which demonstrated a high correlation with respect to each other. The CSF transmitter markers were then used in multiple regression models to explain the variance of clinical variables as chosen from the cluster analyses. The degree of dementia, as assessed by global deterioration score (GDS) and activity in daily life (ADL) status, as well as the Alzheimer-related symptoms dyspraxia and dysphasia, were associated with low AChE activities in CSF. A presumed subgroup of dementia patients clinically characterized by asymmetry of neurological signs, increased unilateral tonus, stepwise progression, and high Hachinski score, showed low HVA concentrations in CSF. These data suggest a coupling of clinical/neurological parameters to different CSF transmitter profils and, thus, that CSF biochemical parameters are of use as antemortem markers in dementia conditions.
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PMID:Monoamine metabolite concentrations and cholinesterase activities in cerebrospinal fluid of progressive dementia patients: relation to clinical parameters. 245 93

The inhibition of human and mammalian red blood cell (RBC) cholinesterase (AChE) in whole blood in the presence of added pyridostigmine has been examined. After the addition of pyridostigmine to animal and human blood, red cells were separated from plasma at varying intervals and their enzyme activity measured. An apparent rate constant (ke) was derived for the reaction sequence in which carbamate is released from AChE inhibited by pyridostigmine. The constant is a complex of the rates of decarbamoylation and reinhibition of AChE in the blood sample. Rate constants were also determined for the spontaneous reactivation (ks) of carbamoylated AChE in the species studied. Values of Ks were greater than Ke in corresponding species but varied little between species. Pretreatment of animals with pyridostigmine is known to be an effective therapy against organophosphorus compounds, including soman. The ranking of ke values in mammalian blood was the same as that for the protection against soman in animals: monkey greater than guinea-pig greater than rabbit greater than rat (ke = 0.15, 0.07, 0.05, 0.02 h-1, respectively). Since ke for human blood (0.20 h-1) was greater than that of monkey, pyridostigmine pretreatment would be expected to be an effective prophylaxis for soman in humans.
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PMID:Carbamoylated enzyme reversal as a means of predicting pyridostigmine protection against soman. 257 9

We report the existence, in Torpedo marmorata tissues, of a cholinesterase species (sensitive to 10(-5) M eserine) that differs from acetylcholinesterase (AChE, EC 3.1.1.7) in several respects: (a) The enzyme hydrolyzes butyrylthiocholine (BuSCh) at about 30% of the rate at which it hydrolyzes acetylthiocholine (AcSCh), whereas Torpedo AChE does not show any activity on BuSCh. (b) It is not inhibited by 10(-5) M BW 284C51, but rapidly inactivated by 10(-8) M diisopropylfluorophosphonate. (c) It does not exhibit inhibition by excess substrate up to 5 X 10(-3) M AcSCh. (d) It does not cross-react with anti-AChE antibodies raised against purified Torpedo AChE. This enzyme is obviously homologous to the "nonspecific" or pseudocholinesterase (pseudo-ChE, EC 3.1.1.8) that exists in other species, although it is closer to "true" AChE than classic pseudo-ChE in several respects. Thus, it shows the highest Vmax with acetyl-, and not propionyl- or butyrylthiocholine, and it is not specifically sensitive to ethopropazine. Pseudo-ChE is apparently absent from the electric organs, but represents the only cholinesterase species in the heart ventricle. Pseudo-ChE and AChE coexist in the spinal cord and in blood plasma, where they contribute to AcSCh hydrolysis in comparable proportions. Pseudo-ChE exists in several molecular forms, including collagen-tailed forms, which can be considered as homologous to those of AChE. In the heart the major component of pseudo-ChE appears to be a soluble monomeric form (G1). This form is inactivated by Triton X-100 within days.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Polymorphism of pseudocholinesterase in Torpedo marmorata tissues: comparative study of the catalytic and molecular properties of this enzyme with acetylcholinesterase. 257 81


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