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)

Certain organophosphorous compounds caused the inhibition of 'neurotoxic esterase' present in central nervous system. The role of this enzyme is different from that of cholinesterase. The level of neurotoxic esterase in brain, corpus striatum and spinal cord of rats, mice, guineapigs and hens was measured. Maximum level of the enzyme was found in hens, followed by guineapigs, rats and mice in the order. The concentration of the enzyme was higher in corpus striatum greater than whole brain greater than spinal cord. The determination of the normal level of neurotoxic esterase may be useful in monitoring the exposure to organophosphorous compounds.
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PMID:Distribution of neurotoxic esterase in certain brain regions of laboratory animals. 277 58

Ten menopausal females were studied. Histopathologically, the nasal mucosa was normal, except for the tunical glands which were reduced in number, more localized and showed hyperfunction. Histochemically, there was an increased activity of succinic dehydrogenase, alpha esterase, acid and alkaline phosphatase and choline esterase, indicating an increase in carbohydrate metabolism, lipid breakdown, phagocytic activity, vascularity, secretory activity and parasympathetic hyperactivity which may be responsible for these changes, reflecting the emotional disturbances common in the menopause. These changes were not related to the ovarian steroid hormones. The change in the PAS stain was due to the low estrogen blood level.
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PMID:The human nasal mucosa in the menopause (a histochemical and electron microscopic study). 283 59

The blood esterase mediating the hydrolysis of esmolol was characterized in several different species including man. In contrast to most ester-containing drugs, hydrolysis of esmolol was mediated by an esterase in the cytosol of red blood cells (RBC) in man and dogs and not in plasma or RBC membrane. Species differences in the esterase activity existed. Guinea pig and rat blood esterase activities were much greater than those in the dog followed by those in man. In addition, the esterase activity in rat and guinea pig blood was localized in plasma and not in RBC. Purified human serum cholinesterase, human RBC membrane acetylcholinesterase, human hemoglobin, human carbonic anhydrases A and B, and human and dog serum albumin were all inactive against esmolol. Esmolol esterase activity in human and dog blood was inhibited by sodium fluoride, EDTA, and p-hydroxymercuribenzoate, but not by echothiophate, eserine, and acetazolamide. In contrast, echothiophate and sodium fluoride, but not eserine, inhibited the esterase activity in rat and guinea pig plasma. Metabolic interaction studies indicated that acetylcholine, succinylcholine, procaine, and chloroprocaine did not interfere with the metabolism of esmolol by human and dog blood. Based on the results, it appeared that an arylesterase in human and dog RBC cytosol mediated the hydrolysis of esmolol while an aliphatic esterase mediated the hydrolysis of esmolol in guinea pig and rat plasma.
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PMID:Biochemical properties of blood esmolol esterase. 286 4

1. We have studied the cholinesterase activity from the skeletal muscle of the ammocoete of the lamprey Petromyzon marinus. 2. On the basis of pharmacologic and kinetic criteria, we conclude that the enzyme is true acetylcholinesterase, not pseudocholinesterase. 3. The acetylcholinesterase was found to be present in both globular and asymmetric forms. 4. In contrast to muscle of adult spawning lamprey, where globular esterase is almost exclusively G4, we found that muscle from ammocoete also contains significant amounts of G1 and G2. 5. This difference may be related to the physiological states of the lamprey during the various stages of its life cycle.
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PMID:Molecular forms of acetylcholinesterase from the skeletal muscle of the ammocoete of the lamprey Petromyzon marinus. 292 45

The genetic structure of two Chukot Evens subpopulations (314 individuals) for electrophoretic protein systems and taste sensitivity to PTC was studied. 17 of the 39 loci were polymorphic (43.59%). The following systems were completely monomorphic: diaphorase NAD H (Dia); glucose-6-phosphate dehydrogenase (G-6-PD); glutamatoxalate transaminase (GOT); carbonic anhydrase (Ca-1); catalase (Ct), lactate dehydrogenase (loci LDH-A and LDH-B); leucine aminopeptidase (Lap); malate dehydrogenase (MDH); purine nucleoside phosphorylase (PNP); superoxide phosphorylase (PNP); superoxide dismutase (SOD); phosphoglucomutase-2 (PGM2); cholinesterase (locus E1); red cell esterase (4 loci); albumin (Alb); hemoglobin (Hb A and B); ceruloplasmin (Cp); and blood, gren, using the standard method. The following systems were polymorphic: red cell acid phosphatase (AcP); phosphoglucomutase-1 (PGM1); 6-phosphogluconate dehydrogenase (PGD); glutamatepyruvate transaminase (GPT); glyoxalase-1 (GLO-1); esterase (EsD); adenilatkinase (AK); alkaline phosphatase (Pp); cholinesterase (locus E2); haptoglobin (Hp); transferrin (Tf); group-specific component (Gc) and ABO, MN, Lewis, P blood groups and taste sensitivity to PTC. The following allele frequencies for polymorphic loci have been detected: AKI = 0.994; GLO = 1I = 0.082; GPT1 = 0.653; AcPA = 0.400; AcPB = 0.599; AcPC = 0.001; PGDA = 0.944; PGM1(1) = 0.906; EsD1 = 0.897; E2+ = 0.048; HpI = 0.394; GcI = 0,919; Tfc = 0.987; r(O) = 0.669; p(A) = 0.184; q(B) = 0.146; M = 0.711; Le = 0.411; P1+ = 0.521; t = 0.295. The genetic structure of Chukot Evens population is significantly nearer to that of the other ethnic groups of the North-East, in comparison with the genetic structure of Evenks of the Middle Siberia.
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PMID:[Genetic structure of the populations of native inhabitants in the northeastern USSR. V. The Chukot Evens]. 293 99

The tegument of Orthocoelium scoliocoelium and Paramphistomum cervi was examined using histochemical techniques and electron microscopy. On the basis of the distribution of acid and alkaline phosphatase (E.C. 3.1.3.2, E.C. 3.1.3.1), non-specific esterase (E.C. 3.1.1.1), cholinesterase (E.C. 3.1.1.7) and succinate dehydrogenase (E.C. 1.3.99.1) at light microscope level two distinct regions were recognized, an outer and an inner zone. Electron microscopy revealed that the tegument comprises an outer surface syncytium underlain by a thick subsyncytial zone and musculature. Deeper still occur the nucleated "tegumental cells". The latter are in cytoplasmic continuity with the surface syncytium via vacuolated cytoplasmic trabeculae which traverse the muscle layers and the subsyncytial zone. Three types of tegumental cells each lacking mitochondria were observed. The T1 cells synthesize discoid and electron dense T1 bodies while T2 cells produce oval and electron lucent T2 bodies. The third type of tegumental cells apparently produce no secretory bodies and may represent an embryonic cell type. The surface syncytium contains T1 and T2 secretory bodies and is bounded apically by a plasma membrane invested externally by a fuzzy and filamentous glycocalyx. The surface syncytium lacks mitochondria and is traversed by infoldings of the basal plasma membrane. Beneath the surface syncytium the subsyncytial zone is largely comprised of fibrous interstitial material. This zone, which is particularly thick in the amphistomes, is traversed by trabeculae and extensions of underlying parenchymal cells which usually contain mitochondria and lysosomes. The subsyncytial zone overlies numerous circular and longitudinal muscle fibres. The absence of mitochondria and enzymes associated with active transport suggests that the amphistome tegument may be mainly specialized for protection of the worm against mechanical and chemical conditions prevailing in the rumen. Active uptake of nutrients is probably not a primary function.
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PMID:Ultrastructure and cytochemistry of the tegument of Orthocoelium scoliocoelium and Paramphistomum cervi (Trematoda: Digenea). 297 78

Plasma pseudocholinesterase and porcine liver esterase were used to catalyse the incorporation of the stable isotope oxygen-18 into the carboxyl moiety of lipoxygenase metabolites of arachidonic acid. This simple method produces eicosanoid products containing two oxygen-18 atoms; but the enzymes studied were found to display large substrate specificity in the efficiencies at which oxygen-18 could be incorporated into the lipoxygenase metabolites. Furthermore, [18O2]LTB4 was found not to back exchange during in vitro incubation with human neutrophils. The methods involved for stable isotope incorporation are simple, efficient and produce highly enriched species in a short time. By varying the type of esterase, the amount of esterase or the length of incubation highly enriched species of all eicosanoids tested could be prepared.
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PMID:Preparation of oxygen-18-labeled lipoxygenase metabolites of arachidonic acid. 300 15

The inhibition of neurotoxic esterase activity in chicken brain has been studied in vitro and in vivo. Aphos exposure, causing chicken paralysis, has demonstrated that the initial stage of delayed neurotoxicity was significant esterase activity inhibition (by 60-80%) within 3-24 hours after the pesticide administration. The inhibition of cholinesterase activity occurred both in the blood and sciatic nerve. The delayed conduction through peripheral nerves caused by demyelination has been revealed in the latent period (before the clinical signs of intoxication).
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PMID:[Early manifestations and mechanism of the neurotoxic action of organophosphorus pesticides]. 301 51

We have measured aspirin esterase, cholinesterase, paraoxonase, and phenylacetate esterase activities in samples of plasma from British and Ghanaian subjects. Aspirin esterase, paraoxonase, and phenylacetate esterase activities were significantly lower in Ghanaians compared with British subjects. However, cholinesterase activities were similar in Ghanaian and British plasma samples. The lower esterase activities in Ghanaian plasma samples may result in higher circulating concentrations and greater pharmacological effects of drugs such as aspirin.
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PMID:Activity of esterases in plasma from Ghanaian and British subjects. 302 17

An acetylcholinesterase (AChE) activity and a cholinesterase (ChE) activity were localized in mammalian kidneys, using a modified histochemical method of Koelle. The animals studied were mouse, hamster, cat, rat, and guinea pig. The kidneys were excised after in situ perfusion and fixation to eliminate AChE and ChE activities of blood. We carried out a relatively long incubation (up to 4 h) to detect weak AChE and ChE activities in the tissue. The differences in enzymatic activities in the kidneys from these 5 animals were important. The AChE activity was localized in the glomerulus (mouse, hamster, cat, and rat) and in the tubule (mouse, hamster, and rat). The ChE activity was also localized in the glomerulus (mouse and rat) and in the tubule (mouse and cat). An important nonspecific esterase activity was observed in the tubules of rat, guinea pig, and cat. In the thin segment of the loop of Henle, except of cat kidney, no esterase activity at all was observed. Electron microscopy revealed that, in the mouse kidney, both AChE and ChE activities were localized in the endoplasmic reticulum of glomerular endothelial cells and mesangial cells. (An AChE activity was localized mainly in mesangial cells, while ChE activity was localized mainly in endothelial cells). AChE and ChE activities were also localized in the endoplasmic reticulum of tubule cells.
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PMID:A histochemical localization of acetylcholinesterase and cholinesterase activities in mammalian kidneys. 309 Aug 31


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