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At least 19 recordsLinked to original sources
PubMed1998

cDNA cloning, in vitro expression, and biochemical characterization of cholinesterase 1 and cholinesterase 2 from amphioxus--comparison with cholinesterase 1 and cholinesterase 2 produced in vivo.

We have isolated cDNAs coding for the complete amino acid sequences of cholinesterase 1 (ChE1) and cholinesterase 2 (ChE2) from amphioxus. Both ChE transcripts have the characteristics of H-type catalytic subunits, which are inserted in the membrane via an ethanolamine-glycan-phosphatidylinositol anchor. The members of the catalytic triad of ChEs, the three pairs of cysteine residues involved in intrachain disulfide bonding, a cysteine near the carboxy terminal of both sequences, which could mediate interchain disulfide bonding, and 11 of the 14 aromatic amino acids that line the catalytic gorge of AChE are conserved. A remarkable difference between the two enzymes is in the region of the acyl-binding pocket, which plays an important role in determining substrate specificity in cholinesterases. ChE2 contains a sequence that resembles the acyl pocket of invertebrate ChE, while the acyl-binding site of ChE1 is novel. There are also differences between the two enzymes in the peripheral anionic site, which mediates inhibition by certain ligands. In vitro expression in COS-7 cells demonstrates that ChE2 hydrolyzes acetylthiocholine almost exclusively, while ChE1 hydrolyzes both acetylthiocholine and butyrylthiocholine. Both enzymes are inhibited comparably by BW284c51, but ChE1 is considerably more resistant to inhibition by propidium, ethopropazine, and eserine than is ChE2. Velocity sedimentation indicates that ChE1 and ChE2 are present as amphiphilic and nonamphiphilic G2 forms in vivo and in vitro. Another molecular form, which sediments at 17 S, is also present in vivo. Nondenaturing gel electrophoresis in conjunction with digestion by phosphatidylinositol-specific phospholipase C demonstrates that the vast majority of ChE1 and ChE2 is present as ethanolamine-glycan-phosphatidylinositol-anchored G2 forms in vivo. ChE1 also possesses an ethanolamine-glycan-phosphatidylinositol-anchor in vitro; however, ChE2 produced in vitro could not be detected on nondenaturing gels.

Acetylthiocholine↗
PubMed1997

Red cell acetyl cholinesterase and plasma cholinesterase activity and genetic variants of plasma cholinesterase in northwest Indian adults.

The plasma cholinesterase (PChE) and red cell acetyl cholinesterase (AChE) activities are indicators of exposure to organophosphates. We studied their distribution in unexposed Northwest Indian adults by measuring them in 120 men and 111 women by Ellman's and Kalow's method, respectively. We also determined genetic variability of plasma cholinesterase in 193 subjects (male = 111, female = 82). The mean +/- (SD) AChE levels in population, men and women, were 34.97 +/- 13.66, 35.05 +/- 12.42, 34.88 +/- 14.89 nmol/mg Hb/min, whereas PChE was 0.448 +/- 0.173, 0.435 +/- 0.163, 0.462 +/- 0.183 ku/l, respectively. When compared for sex, no significant difference could be found for red cell AChE and PChE activity. However, on 2-way analysis of variance (ANOVA) adjusted for age classification, the levels of both AChE and PChE were significantly higher in groups above the age of 30 years as compared to below 30 years (t = 3.08, p < 0.01, t = 2.82, p < 0.05), respectively. Seven genetic variants of PChE could be detected in males, whereas in females 6 genetic variants were found.

Acetylcholinesterase↗
PubMed1982

Inhibitory effect of acephate (N-acetyl O, S-dimethyl thiophosphoramide) on serum cholinesterase--effect of acephate on cholinesterase.

The Lineweaver-Burk plot of the activity of human serum cholinesterase against the concentration of butyrylthiocholineiodide was shown by two intersecting lines. The Hill plot of cholinesterase activity was linear over the entire range of the substrate concentration. The n value, an interaction coefficient, was less than 1.0 (about 0.8). These results suggest that cholinesterase has multiple substrate binding sites. Acephate, one of the organophosphorous insecticides, inhibited the activity of cholinesterase. Acephate at concentration under 1.25 mM (about 230 ppm in serum) did not inhibit the activity of cholinesterase. The minimum concentration of acephate inhibition of cholinesterase activity was at 2.5 mM. An equilibrium constant(K) can be used as an indicator of inhibitory effect on cholinesterase. The serum cholinesterase activity of workers who were exposed to acephate is not affected when the concentration of acephate in serum is less than 200 ppm. This result suggests that the activity of serum cholinesterase is not an accurate indicator of the exposure of the low toxic insecticides, e.g. acephate. The inhibitory effect of acephate on cholinesterase decreased after the incubation with S-9 mixture. This result suggests that a part of acephate is metabolized to inactive substances in the liver.

Cholinesterase Inhibitors↗
PubMed1994

Interlaboratory cholinesterase determinations and the effect on the results of statistical evaluation of cholinesterase inhibition.

Cholinesterase activity is often a key parameter in the regulatory assessment of cholinesterase-inhibiting agents such as organophosphorous and carbamate pesticides. Thus, the nature and characteristics of the methodology involved in the measurement of plasma (PChe), erythrocyte (R Che), and brain (BChe) cholinesterase activity takes on a heightened degree of importance. In this study an interlaboratory comparison of cholinesterase activity as determined by various laboratories was conducted in order to assess the influence that different methodologies may have on the results of statistical evaluation of cholinesterase inhibition. RChe, PChe, and BChe from animals exposed to fenthion, a known cholinesterase inhibitor, were determined at 8 different laboratories with experience in cholinesterase determination. Seven different instruments and 5 different assay procedures were employed. Marked differences in both the magnitude of inhibition measured and its designation as a statistically significant difference often occurred between laboratories using both the same as well as different methods of cholinesterase analysis. These findings illustrate the importance of considering not only the sensitivity of a given method of analysis, but also the influence of inter- and intra-laboratory variation on statistically responsive aspects of the data profile itself (i.e., precision, sample size, etc.) when establishing regulatory levels (i.e., Reference Doses (RfDs), Health Advisory Levels (HALs), etc.) on the basis of a cholinesterase no-observed- or lowest-observed-effect level (NOEL, LOEL).

Analysis of Variance↗
PubMed1990

Immunoreactive plasma cholinesterase (EC 3.1.1.8) substance concentration, compared with cholinesterase activity concentration and albumin: inter- and intra-individual variations in a healthy population group.

Substance concentrations of plasma cholinesterase (EC 3.1.1.8) were measured in 94 healthy individuals without occupational exposure to known inhibitors (six samples from each individual). Immunoreactive cholinesterase substance concentrations showed an inter-individual variation corresponding to CVtotal = 22% (mean: 5.01 mg/l, SD: 1.11 mg/l). Intra-individual variations of immunoreactive cholinesterase substance concentration were correlated (r = 0.36) to intra-individual variation of albumin. Estimated by a repeated-measures analysis of variance, the observed intra-individual variation of cholinesterase substance concentration corresponded to CV = 8.8% (SD: 0.44 mg/l), which together with a CVerror = 6% (within and between runs), implies a biological intra-individual variation of cholinesterase substance concentration corresponding to CVintra = 6.4%. Specific catalytic activity (kU/mg immunoreactive cholinesterase) was influenced by the ChE-1 phenotype (phenotype U: 1.58 kU/mg, phenotype UA: 1.22 kU/mg), but not by body weight, height, age, and sex. Observed intra-individual variation of specific catalytic activity corresponded to 6.4% (SD: 0.10 kU/mg), which together with an estimated CVerror = 6.2% implies the biological intra-individual variations of specific catalytic cholinesterase activity to be insignificant. The insignificant CVintra makes specific catalytic cholinesterase activity a rational quantity for evaluation of unexpected fluctuations of cholinesterase activity concentrations.

Adult↗
PubMed1980

A reliable way of estimating cholinesterases from whole blood in the presence of anti-cholinesterases.

A method for the determination of cholinesterases [1] has been adapted to monitor these enzymes in the presence of anti-cholinesterase insecticides. The cholinesterases in blood samples, which were dried on filter papers, could be eluted with water (plasma cholinesterase) and with 1% Triton X-100 (erythrocyte acetylcholinesterase) with complete recovery of the enzyme activity. The samples could be stored at room temperature for at least two weeks and in a refrigerator more than six weeks without a decreased efficiency of elution from the filter paper. It was found that if blood samples to which the two insecticides, used to test the validity of the method, had been added, were stored on filter paper at room temperature or deep frozen for at least one week, there was the same inhibition of the cholinesterases as at the start of the experiment. The samples stored at room temperature in tubes, recovered maximally within a day. This modified method of cholinesterase determination will be especially suitable when samples have to be mailed to laboratories making the analysis.

Cholinesterase Inhibitors↗
PubMed1999

Inhibition of neurite outgrowth from chick sympathetic neurons by cholinesterase inhibitors is not mediated by binding to cholinesterases.

Several studies have suggested a role for cholinesterases in regulating neurite outgrowth. Some acetylcholinesterase (AChE) inhibitors can inhibit neurite outgrowth, but it is unclear if this is due to inhibition of AChE. In this study, the effect of cholinesterase inhibitors on neurite outgrowth from chick sympathetic neurons was examined. Very high (micromolar) concentrations of tacrine and BW284c51 were needed to inhibit neurite outgrowth. In contrast, nanomolar concentrations were required to block cholinesterase activity. No correlation was found between the type of inhibitor or potency of cholinesterase inhibition and inhibition of neurite outgrowth. Both tacrine and BW284c51 were neurotoxic at concentrations that inhibited outgrowth. Therefore, the action of cholinesterase inhibitors on neurite outgrowth may be due to non-specific toxicity rather than to cholinesterase binding.

Animals↗
PubMed1983

Plasma cholinesterase and trophoblastic disease. Gestational trophoblastic disease and reduced activity of plasma cholinesterase.

A case of prolonged action of suxamethonium in a patient with gestational trophoblastic disease is reported. Postoperatively the patient was found to have markedly reduced plasma cholinesterase activity (363 IU/litre) with a normal cholinesterase phenotype. Consequently plasma cholinesterase activity and phenotype were measured in six other patients with the condition and these results compared with those of 22 patients with normal first trimester pregnancies undergoing therapeutic abortion. Plasma cholinesterase phenotype was normal in all patients studied. The activity was significantly decreased (p less than 0.05) from the normal range (620-1370 IU/litre) in all patients with trophoblastic disease. In the 22 patients with normal pregnancies, 14 had activity values in the abnormal range (less than 620 IU/litre) while the mean cholinesterase activity of the group as a whole was significantly decreased (561.8 IU/litre, p less than 0.05) below the normal range. These results confirm the presence of a decrease in plasma cholinesterase activity in early pregnancy and provide new evidence for a decrease in activity in a pseudopregnancy state.

Adult↗
PubMed1990

The effect of bambuterol on plasma cholinesterase activity and suxamethonium-induced neuromuscular blockade in subjects heterozygous for abnormal plasma cholinesterase.

Bambuterol is a new bronchodilator which is also a reversible inhibitor of plasma cholinesterase. In patients with normal plasma cholinesterase genotype, bambuterol prolongs suxamethonium-induced neuromuscular blockade. In the present study, we investigated the interaction of bambuterol and suxamethonium in nine patients heterozygous for abnormal plasma cholinesterase during anaesthesia with fentanyl, thiopentone, halothane and nitrous oxide in oxygen. The patients (seven E1uE1a and two E1uE1s) were given 20 mg of bambuterol orally 2 h before anaesthesia. Suxamethonium 1 mg.kg-1 was given for tracheal intubation. The neuromuscular function was monitored using train-of-four (TOF) stimulation of the ulnar nerve and a force displacement transducer. Plasma cholinesterase activity decreased in all patients following bambuterol (P less than 0.001). In patients with genotype E1uE1a, median time to 90% recovery of twitch height and TOF ratio greater than or equal to 0.7 (37.5 min) was prolonged compared to 28 E1uE1a patients not treated with bambuterol (14.0 min) (P less than 0.001). Four of these patients developed a phase II block apparently not correlated to plasma cholinesterase activity. In the E1uE1s; patients, full recovery was seen after 22.0 and 31.4 min, respectively. It is concluded that in patients heterozygous for abnormal plasma cholinesterase, bambuterol 20 mg taken 2 h before anaesthesia causes a 2-3 times prolongation of the neuromuscular blockade following suxamethonium 1 mg.kg-1 and in some patients a phase II block.

Adult↗
PubMed1980

Hen's egg yolk cholinesterase. Purification, characterization and comparison with hen's liver and blood plasma cholinesterase.

The cholinesterase (acylcholine acylkhydrolase, EC 3.1.1.8) of chicken egg yolk was partly purified and characterized. It was compared to homologous enzymes of liver and blood plasma of laying hens. During gel filtration, yolk and liver cholinesterase were resolved into two fractions. Blood plasma cholinesterase showed one form only, identical with yolk and liver cholinesterase 1 *** (EC 3.1.1.8). This form has an Mr of 440 000 and may be a tetramer of a cholinesterase form present in yolk and liver (Mr 104 000). Substrate specificity, pH optima, Km values, the influence of effectors (ammonium derivatives, choline, eserine, fluoride), gel filtration, gel electrophoresis, isoelectric focusing and affinity chromatography, all point to a very close similarity, if not identity, of the corresponding forms.

Animals↗
PubMed1990

Plasma cholinesterase activity in a healthy population group with no occupational exposure to known cholinesterase inhibitors: relative influence of some factors related to normal inter- and intra-individual variations.

Inter-individual variations of plasma cholinesterase were analysed in 193 apparently healthy volunteers (122 males, 71 females) with no known occupational exposure to cholinesterase inhibitors. Multiple regression analysis and analysis of variance showed statistically significant effects on the individual plasma cholinesterase activity by body weight, height, sex, and ChE-1 phenotype (but not by age or electrophoretic phenotype). Varying body weight explained one-fourth of the observed biological variance (s2total). The intra-individual variations during an 8-month period varied substantially from one individual to another (3% to 41% of the subject's mean activity); a repeated-measures analysis of variance showed a within-person variance (s2intra) = 5% of s2total. Intra-individual variation was uninfluenced by the variables that influence the inter-individual variance. A model for a 'standardized' plasma cholinesterase in which the combined effects of the four significant variables, ChE-1 phenotype, sex, body weight, and height are eliminated, is proposed for comparisons of plasma cholinesterase activities in unmatched population groups, e.g. within environmental or occupational medicine.

Adult↗
PubMed1992

Poisoning from oral ingestion of carbofuran (Furadan 4F), a cholinesterase-inhibiting carbamate insecticide, and its effects on cholinesterase activity in various biological fluids.

A case is presented of a fatal ingestion of Furadan (carbofuran), a cholinesterase-inhibiting carbamate insecticide. A 26-year-old white male was found dead with a partially filled 1-gal (3.8-L) container of Furadan 4F insecticide-nematocide (44.9% carbofuran). The individual had ingested approximately 345 mL of the mixture. Analysis of cholinesterase activity in various biological fluids was performed spectrophotometrically using propionylthiocholine and 5,5'-dithiobis-2-nitrobenzoic acid [Sigma Diagnostics, cholinesterase procedure No. 422 (PTC)] which was measured at 405 nm and 30 degrees C in a Gilford Stasar III Spectrophotometer. The cholinesterase activities were as follows: plasma, 245 units (U)/L (93% inhibition/7% normal activity); serum, 208 U/L (95.3% inhibition/4.7% normal activity); whole blood, 297 U/L (92.8% inhibition/7.2% normal activity); erythrocytes, 58 U/L (99% inhibition/1% normal activity); vitreous humor, 7 U/L; and bile, 148 U/L. Carbofuran was detected in the blood and gastric contents by thin-layer chromatography. No alcohol or other drugs were detected in the blood, urine, or gastric contents. Ingestion of the carbofuran produced acute visceral congestion and pulmonary edema. Death was caused by anoxia due to respiratory paralysis produced by cholinesterase inhibition from Furadan (carbofuran) ingestion.

Adult↗
PubMedDate not supplied

Detection of cholinesterase inhibition. The significance of cholinesterase measurements.

Human cholinesterase exists in two forms--acetylcholinesterase located in tissue microsomes and red blood cells and serum cholinesterase found in serum or plasma. The two enzymes display marked differences in structure, substrate specificity, biological function, and origin. Contemporary methods employ acylthiocholine as substrate for serum cholinesterase and a second coupled reaction of thiocholine and chromogenic disulfide agents. Clinical applications are primarily centered on subnormal levels of enzyme activity. The decreased activity levels can be caused by inhibitors, reduced biosynthesis, or dysfunctional genetic variants. Changes in enzyme activity should be related to baseline levels because there is wide individual variation as well as methodological variation. Once baseline levels have been established, cholinesterase activity becomes a sensitive indicator of pesticide intoxication and hepatic biosynthetic capacity. A more sophisticated assay, performed in the presence of an inhibitor, is required to detect the atypical genetic variants of serum or plasma cholinesterase.

Acetylcholinesterase↗
PubMed1989

Serum cholinesterase isoenzymes and the WHHL rabbit: the relationship between the activity of cholinesterase not bound to low-density-lipoprotein and lipoprotein titer.

Serum cholinesterase has been previously shown to complex with beta-lipoprotein in the plasma. Since serum cholinesterase exists as isoenzymes in plasma, the relationship between the activity of these isoenzymes (unbound to beta-lipoprotein) and lipoprotein titer was investigated. The results indicated that the total of C2, C3, and C4 isoenzyme activities were expressed within a narrow range and independent of low density lipoprotein titer. These findings may indicate that unbound plasma cholinesterase may undergo autoregulation independent of cholinesterase bound to beta-lipoprotein.

Animals↗
PubMed1989

Additional electrophoretic components of cholinesterase in plasma: a phenomenon of no importance to the total plasma cholinesterase activity.

Total plasma cholinesterase and cholinesterase isozyme components were studied in 193 healthy subjects without occupational exposure to known cholinesterase inhibitors. The study showed that the four additional isozyme components, C5, C1', C6, and C7 occurred in plasma independently of each other, and that the total plasma cholinesterase activity was completely uninfluenced by the presence of any of the four components.

Adult↗
PubMedDate not supplied

[Cholinesterase profile of geriatric patients with reference to pathologically lowered serum cholinesterase].

1. Analysing systematically 416 geriatric patients with a predominance of heart's and circulations's disease and disturbance of mobility we find a pathological lowered cholinesterase in 36% of the cases. This percentage is higher than expected in regard to the hepatological diagnosis. 2. Analysing the histological data of 26 patients with pathological lowered cholinesterase we find with all of them a granular edema of the hepatocyt cytoplasme and intracellular lipofiscin deposit near the central veins. We find also often a diabetic and fat liver. The pathological lowered cholinesterase goes hand in hand with a pathological histology. 3. There is no correlation between the cholinesterase and the other liver enzymes. 4. These results may be interpretated as a sign for a lowered synthesis efficiency of pathological hepatocyts and there are discussed the consequences for the adaptation of the metabolism. A correlation of the years of age corresponding to the theory of deficit in age is not proved.

Adult↗