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 embryonic development of total specific activities as well as of molecular forms of acetylcholinesterase (AChE, EC 3.1.1.7) and of butyrylcholinesterase (BChE, EC 3.1.1.8) have been studied in the chick brain. A comparison of the development in different brain parts shows that cholinesterases first develop in diencephalon, then in tectum and telencephalon; cholinesterase development in retina is delayed by about 2-3 days; and the development in rhombencephalon [not studied until embryonic day 6 (E6)] and cerebellum is last. Both enzymes show complex and independent developmental patterns. During the early period (E3-E7) first BChE expresses high specific activities that decline rapidly, but in contrast AChE increases more or less constantly with a short temporal delay. Thereafter the developmental courses approach a late phase (E14-E20), during which AChE reaches very high specific activities and BChE follows at much lower but about parallel levels. By extraction of tissues from brain and retina in high salt plus 1% Triton X-100, we find that both cholinesterases are present in two major molecular forms, AChE sedimenting at 5.9S and 11.6S (corresponding to G2 and G4 globular forms) and BChE at 2.9S and 10.3S (G1 and G4, globular). During development there is a continuous increase of G4 over G2 AChE, the G4 form reaching 80% in brain but only 30% in retina. The proportion of G1 BChE in brain remains almost constant at 55%, but in retina there is a drastic shift from 65% G1 before E5 to 70% G4 form at E7.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Quantitative development and molecular forms of acetyl- and butyrylcholinesterase during morphogenesis and synaptogenesis of chick brain and retina. 358 28

Rats were administered the organophosphorus insecticide acephate at 1.0 or 10.0 mg/kg.day for 15 weeks. Blood and brain samples were collected at the end of the treatment and analyzed for cholinesterase, acetylcholinesterase, and glutamic acid decarboxylase activities and catecholamine and amino acid levels. No significant inhibition in the activity of brain AChE was noted at doses of 1.0 or 10.0 mg/kg.day. Low levels of acephate exposure (1.0 mg/kg.day), which did not alter plasma cholinesterase or RBC acetylcholinesterase activity levels, resulted in a significant elevation of plasma epinephrine and norepinephrine levels. Decreased GABA, dopamine, and tyrosine levels and glutamic acid decarboxylase activity were observed in brains of these rats. Similar changes occurred in rats exposed to 10 mg of acephate/kg.day; however, plasma cholinesterase and RBC acetylcholinesterase activities were inhibited. These observations suggest that chronic exposure to acephate altered the activity of the noncholinergic system without altering the cholinergic activity, and that low-level chronic exposure to organophosphorous compounds cannot be predicted by measuring the ChE or AChE enzyme activities.
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PMID:Neurotoxic effects of low-level chronic acephate exposure in rats. 360 37

Aganglionosis of large bowel (Hirschsprung's disease; HD) is associated with higher acetylcholinesterase activity (AChE activity). Occasionally, especially in the neonatal period, the AChE activity may not be of diagnostic value. The authors previously reported that simultaneous estimation of butyrylcholinesterase activity (BChE activity) and the determination of AChE/BChE ratio may have discriminatory diagnostic value. They extended this finding to 31 cases of HD, in 16 of which resected tissue was available for study. All cases had histologic confirmation of aganglionosis. The AChE/BChE ratio was found to be higher than 2.0, with the exception of a case in which the biopsy weight was low (i.e., less than 3 mg), even when the AChE activity was normal or borderline. The estimation of AChE/BChE ratio is easy, rapid, and, in the author's experience, of discriminatory diagnostic value.
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PMID:The diagnostic value of acetylcholinesterase/butyrylcholinesterase ratio in Hirschsprung's disease. 366 99

Dissociated single cells from chicken retina or tectum kept in rotation-mediated cell culture aggregate, proliferate and establish a certain degree of histotypical cell-to-cell relationships ("sorting out"), but these systems never form highly laminated aggregates ("nonstratified" R- and T-aggregates). In contrast, a mixture of retinal plus pigment epithelial cells forms highly "stratified" aggregates ("RPE-aggregates", see Vollmer et al. 1984). The present comparative study of "stratified" and "nonstratified" aggregates enables us to investigate the process of cell proliferation uncoupled from that of tissue stratification. Here we try to relate these two basic neurogenetic processes with patterns of expression of cholinesterases (AChE, BChE) during formation of both types of aggregates. During early aggregate formation, in both "stratified" and "nonstratified" aggregates an increased butyrylcholinesterase activity is observed close to mitotically active cells. Quantitatively both phenomena show their maxima after 2-3 days in culture. In contrast, AChE-expression in all systems increases with incubation time. In nonproliferative areas, in the center of RPE-aggregates, the formation of plexiform layers is characterized initially by weak BChE- and then strong AChE-activity. These areas correspond with the inner (IPL) and outer (OPL) plexiform layers of the retina in vivo. Although by sucrose gradient centrifugation we find that the 6S- and the fiber-associated 11S-molecules of AChE are present in all types of aggregates, during the culture period the ratio of 11S/6S-forms increases only in RPE-aggregates, which again indicates the advanced degree of differentiation within these aggregates.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cholinesterases and cell proliferation in "nonstratified" and "stratified" cell aggregates from chicken retina and tectum. 369 Jun 29

Three distinct patterns of AChE localization have been observed in relation to cat abducens motor neurons and internuclear neurons labelled by retrograde transport of horseradish peroxidase. First, AChE was localized predominantly within cisternae of granular endoplasmic reticulum and agranular reticulum of motor neuron somata, dendrites and axons, but was absent from internuclear neurons. AChE was also associated with saccules of the Golgi apparatus in the motor neurons, but was was absent from all other cytoplasmic organelles. Second, AChE was observed on the soma-dendritic and axonal surface membrane of the motor neurons, particularly at sites of apposition of synaptic endings of all morphological types, but was usually absent from the surface membranes of internuclear neurons. Third, AChE was associated both extracellularly and intracellularly with certain synaptic endings that contained spheroidal synaptic vesicles and that contacted both motor neurons and internuclear neurons. A similar pattern of staining of synaptic endings was observed at the neuromuscular junctions in the lateral rectus muscle. Axotomy of the VIth nerve resulted in loss of intracellular AChE associated with the Golgi apparatus and extracellular AChE on the somatic surface membrane of the motor neurons. The patterned localization of AChE contrasted with the localization of butyrylcholinesterase, which was associated predominantly with astrocytes. The findings suggest different roles of AChE as a function of the different patterns of localization.
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PMID:Histochemical localization of acetylcholinesterase in relation to motor neurons and internuclear neurons of the cat abducens nucleus. 372 44

To substantiate reported data and improve the properties of anticholinesterase drugs in blood-brain barrier (B-BB) research, 7-(methylethoxyphosphinyloxy) 1-methyl-quinolinium iodide (MEPQ) was prepared and evaluated as an inhibitor of both acetyl- and butyrylcholinesterase (AChE and BuChE, respectively) from various sources. The second-order rate constants for the inhibition of cholinesterase from eel, mice brain and horse serum at 25 degrees were found to be 5.3 X 10(8), 1.3 X 10(8) and 5.4 X 10(7) M-1 min-1 respectively. The inhibited enzyme could be reactivated by 1-methyl-2-hydroxy iminomethylpyridinium iodide (2-PAM). The two enantiomers of the racemic mixture MEPQ inhibited AChE at similar rates. Low concentrations of AChE could be determined by the residual enzyme activity and by fluorescence measurements of the leaving group, thus suggesting the application of MEPQ as a sensitive titrant of cholinesterase, as well as a potential tool in studying B-BB permeability changes.
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PMID:Synthesis and in vitro properties of a powerful quaternary methylphosphonate inhibitor of acetylcholinesterase. A new marker in blood-brain barrier research. 375 44

Acetylcholinesterase, pseudocholinesterase and their molecular forms were measured in the CSF of patients affected by Alzheimer's disease and of matched neurological controls. Three different molecular forms of ChE were found in the CSF of both groups of patients, but only two of them belonged to 'true' AChE. No differences were found between Alzheimer's disease patients and neurological controls in all the examined parameters.
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PMID:Molecular forms of cholinesterases in CSF of Alzheimer's disease/senile dementia of Alzheimer type patients and matched neurological controls. 394 78

Acetylcholinesterase (AChE; EC 3.1.1.7) extracted in 1% Triton X-100 from rabbit brain was purified 2,000-fold by chromatography on agarose conjugated with a monoclonal antibody directed against human red blood cell cholinesterase. After elution from the immunoadsorbent with pH 11 buffer, the preparation was purified further by affinity chromatography on phenyltrimethylammonium-Sepharose 4B with decamethonium elution. Overall yield of purified enzyme was 37% of the AChE originally solubilized, with a specific activity of 2,950 units/mg protein. Electrophoresis under reducing conditions in 7.5% sodium dodecyl sulfate polyacrylamide gels revealed only one silver-staining polypeptide band. A streamlined purification procedure enabled the isolation of electrophoretically homogeneous AChE to be completed in fewer than 7 days, at yields exceeding 50%. Electrophoretic analysis of purified AChE indicated an apparent MW of 71,000 for the monomeric subunit. Gel filtration and sucrose density gradient centrifugation in the presence of Triton X-100 showed little difference between the properties of the native and the purified enzyme. The molecular mass of the main species was estimated from the gel filtration and sedimentation data to be 280,000 daltons. Kinetic parameters of the purified protein (Km = 0.16 +/- 0.01 mM) were close to those of the native enzyme (Km = 0.12 +/- 0.01 mM) when examined with acetylthiocholine iodide as substrate. The two-step immunopurification procedure presented in this communication offers a convenient route to homogeneous neural AChE in quantities useful for detailed biochemical and immunochemical study.
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PMID:Two-step immunoaffinity purification of acetylcholinesterase from rabbit brain. 396 30

To test the usefulness of immunotherapy in organophosphate poisoning, two mouse monoclonal antibodies were prepared to the chemical warfare agent soman. The antibodies bound reversibly to soman and afforded considerable protection to acetylcholinesterase in vitro. However, they were only marginally effective in preventing the consequences of soman poisoning in mice (these data have been published elsewhere). Since potential for immunotherapeutic usefulness resides in antibody affinity and specificity, we conducted experiments to define these parameters to enable us to maximize them in the production of later antibodies. Interaction of the antibodies (CC1 and BE2) in affinity-purified form with a series of soman analogs in a competitive inhibition enzyme immunoassay was used to assess the contribution to binding affinity of each functional group on the soman molecule. Neither antibody interacted with the -P = S analog of soman or methylphosphonic acid. A decrease in the number of methyl groups on the pinacolyl side chain reduced or eliminated binding with both antibodies while increasing the size of this group had a mixed result. The major metabolite of soman, its basic hydrolysis product, interacted weakly with BE2 and failed to interact with CC1. Alkyl ester group substitution at the fluorine position increased antibody binding up to the symmetrical dipinacolyl analog. Stereochemical specificity was determined by measuring the apparent decrease in the rate of inhibition of cholinesterases (acetylcholine acetylhydrolase, EC 3.1.1.7, or acylcholine acylhydrolase, EC 3.1.1.8) by pure soman stereoisomers in the presence of increasing concentrations of each antibody. CC1 demonstrated specificity that varied as C(+)P(+) less than C(-)P(+) less than C(-)P(-) less than C(+)P(-). Although affinities were much lower, BE2 also showed a preference for the more toxic P(-) isomers.
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PMID:Structural and stereochemical specificity of mouse monoclonal antibodies to the organophosphorous cholinesterase inhibitor soman. 402 95

A methodology was developed to determine the proportion of acetyl- (AChE) and butyrylcholinesterase (BuChE) in the albino and pigmented rabbit eye. It was found that BuChE contributed over 75% of the cholinesterase activity in all the ocular tissues but the corneal epithelium of the albino rabbit. This esterase was principally responsible for the parabolic chain length dependence of ocular hydrolysis of model naphthyl ester prodrugs reported previously. In contrast, when incubated with AChE, the rate of hydrolysis of these esters decreased monotonically with increasing ester chain length. Together these findings suggest that esters whose chain length exceeds 4 carbons will be hydrolyzed primarily by BuChE. It is suggested that the dominance of BuChE in ocular tissues is another factor which merits consideration in the design and evaluation of ocular ester prodrugs.
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PMID:Ocular esterase composition in albino and pigmented rabbits: possible implications in ocular prodrug design and evaluation. 407 17


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