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 target size of neurotoxic esterase (NTE), the putative target site for the initiation of organophosphorus-compound-induced delayed neurotoxicity, and acetylcholinesterase (AChE) from hen brain were examined by determining the rate at which the activities of the esterases were destroyed by ionizing irradiation. Samples of hen brain were prepared by slowly drying a microsomal preparation under vacuum. The dried samples were then irradiated with electrons from a 1 MeV Van de Graaff generator. The doses ranged from 0 to 28 Mrad. The radiation doses were calibrated by the rate of inactivation of T1-bacteriophage plaque induction. Following the irradiation procedure, the samples were resuspended in buffer and enzymic activity was measured. The target size of NTE from hen brain was determined to be about 105 kDa, whereas hen brain AChE was found to have a target size of about 53 kDa. The target size of NTE was found to be similar in experiments with rat brain and cat brain. In addition, commercial preparations of electric-eel electric-organ AChE and horse serum butyrylcholinesterase were found to have target sizes that were identical with each other, and also were very similar to that of AChE from hen brain.
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PMID:Target size of neurotoxic esterase and acetylcholinesterase as determined by radiation inactivation. 407 37

1. The patterns of innervation and electrical properties of muscle fibres in a skeletal muscle of the blue tongue lizard Tiliqua nigrolutea have been investigated.2. Gold impregnation of nerve terminals and staining of muscle fibre junctional areas for cholinesterase showed that there are two histological types of muscle fibre in scalenus muscles of the lizard: (a) those usually receiving single en plaque innervation, and (b) those that receive multiple en grappe terminations.3. In normal solution and in solutions to which small doses of curare were added, two types of subthreshold post-junctional response were recorded following nerve stimulation, (a) potentials with rapid rates of rise and a half-decay time of less than 10 msec and (b) responses with fast rise times and long half-decay times (50 msec or more).4. Fast time course subthreshold responses often gave rise to propagated action potentials. In curarized preparations ((+)-tubocurarine 0.4-1.0 mug/ml.) action potentials failed, giving way to junction potentials of decreasing amplitude, when stimulation was maintained at rates of 5/sec or more. The decay phases of fast time course potentials were closely approximated by error functions.5. Slow time course responses summated during repetitive stimulation, but action potentials were never produced. The decays of slow junction potentials were well fitted by exponentials. It is suggested that fibres in which they were recorded received distributed, en grappe innervation.6. Fibres in which fast time course junction potentials were recorded were excited by direct stimulation via an intracellular micro-electrode. They had apparent membrane resistance and capacity of about 4000 Omega. cm(2) and 7 muF/cm(2).7. Fibres exhibiting slow junction potentials could not be excited directly, even when depolarizing pulses were preceded by hyperpolarizations of 50 mV or more for more than 20 msec. Such fibres had an apparent membrane resistance of 31 x 10(3) Omega.cm(2) (mean) and a capacity of less than 3 muF/cm(2) (eight fibres).8. Curarized muscles developed tension in response to nerve stimulation at frequencies of 5/sec or more. The tension profile was smooth at even the lowest frequencies at which a response was elicited. Normal fusion frequency was around 50/sec.9. It is suggested that fibres exhibiting slow junction potentials were functionally similar to amphibian tonic fibres.10. Some fibres were found in which action potentials could be elicited by stimulation of one or more axons. Their subthreshold responses and passive properties were not determined and it remains uncertain to which of the two structural types they belong.
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PMID:Histological and electrophysiological investigation of lizard skeletal muscle. 571 Apr 20

The electroplaques composing the electric organ of the eel, Electrophorus electricus, have been utilized for the dual purpose of demonstrating the subcellular sites of acetylcholinesterase activity and as a model for comparison of the several cytochemical methods available. Fresh tissue and tissue fixed by immersion in formalin, hydroxyadipaldehyde, or glutaraldehyde was reacted with the Cu-thiocholine method, the Cu-ferrocyanide thiocholine method, or the thiolacetic acid (TAA) method using Pb, Ag, or Au as capture reagents. Controls were obtained by omission of substrate, or by addition to complete media of varying concentrations of different cholinesterase inhibitors. Reactions were run at 0-5 degrees C at a pH range of 5.0-7.1 for 0.25 to 120 min. Regardless of the capture metal, the localization obtained with TAA as substrate was identical with that observed with acetylthiocholine, the majority of precipitate being deposited on or near the external innervated surface of the plaque and within the tubulovesicular organelles opening onto the innervated surface. Both of the thiocholine methods and the Pb-TAA method showed reaction product in synaptic vesicles of the nerve endings innervating the plaque which was uninhibitable by 10(-4)M physostigmine. All methods also showed some inhibitor-sensitive deposition of reaction product in the mucoid material forming the immediate extracellular environment of the innervated surface.
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PMID:Fine structural localization of acetylcholinesterase in electroplaque of the electric eel. 596 39

Numbers of IgM plaque-forming cells (PFC) were reduced by 65% in C57Bl/6 mice given parathion 2 days after immunization with sheep red blood cells (SRBC). The immunosuppressive dose (16 mg/kg, p.o.) caused signs of cholinergic poisoning and 20% mortality. Survivors appeared to have recovered fully from the cholinergic crisis at the time of immunologic assay. However, these animals had reduced tissue cholinesterase (ChE) activities and decreased numbers of nucleated spleen cells. Immunosuppression was apparent on day 4 but not on day 3 or days 5-8 of the primary IgM response. Reduction of serum hemagglutinin titers coincided with reduction of the number of splenic PFC. A lower dose of insecticide (4 mg/kg, p.o.) did not produce signs of poisoning and was not immunosuppressive. The number of 8-day IgG PFC was reduced by 45% when parathion (16 mg/kg, p.o.) was given 6 days after immunization, but not when parathion was given 2 days after immunization. The data suggest that cholinergic stimulation and/or the associated toxic chemical stress may be involved in parathion-induced immunosuppression.
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PMID:Parathion-induced suppression of humoral immunity in inbred mice. 650 99

Activities relating to the cholinergic system in post-mortem brain tissue have been examined in relation to ageing and Alzheimer-type pathology. As senile plaque numbers increased in non-demented and demented old people, activities of choline acetyltransferase and acetylcholinesterase decreased, butyrylcholinesterase increased and muscarinic receptor binding remained unchanged. The behaviour of these biochemical activities was further examined in relation to the ageing process in mentally normal people. Loss of choline acetyltransferase also occurred, to a lesser extent, with increasing age and muscarinic binding decreased but there was no age-related loss in acetylcholinesterase. These biochemical findings are discussed in relation to the possible involvement of the cholinergic system in 'normal' ageing and in Alzheimer's disease and are compatible with an extension of age-related nerve terminal changes to abnormalities of cholinergic processes in the disease itself.
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PMID:The cholinergic system in old age and Alzheimer's disease. 736 31

Propanidid is a competitive inhibitor not only of serum cholinesterase, but of neuromuscular plaque and brain acetylcholinesterase also. The I50 of plaque acetylcholinesterase occurs at much higher concentrations of anaesthetic than for serum enzyme, this may depend on the environmental conditions under which propanidide has to act, or on acetylcholinesterase's high degree of specificity by comparison with pseudocholinesterase. Succinylcholine also inhibits serum cholinesterase but not plaque enzyme. With respect to the serum enzyme, the inhibition curve of the two drugs combined is similar to that of propanidide alone. The prolongation of apnoea observed during propanidide-induced anaesthesia, when succinylcholine is administered, does not appear to be due to diminution of serum cholinesterase activity but rather to interference of the two other drugs with neuromuscular transmission.
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PMID:[Propanidid as an antagonist: competitive inhibitor of neuromuscular plaque acetylcholinesterase]. 746 80

In a sample of consecutively received, 4 demented and 4 age-matched nondemented brains, the total cortical area covered by plaque-like A beta amyloid and butyrylcholinesterase deposits was measured at two regions of the temporal cortex with the help of computed densitometry. Demented as well as age-matched nondemented brains contained A beta and butyrylcholinesterase-positive plaques. The total cortical area covered by the A beta precipitates was higher in demented individuals but there was overlap with the values seen in the specimens from nondemented individuals. The proportional plaque area displaying butyrylcholinesterase reactivity was very significantly and five fold to sixfold higher in the demented than in the nondemented group and there was no overlap between the two populations. Diffuse A beta deposits in nondemented elderly brains may represent a benign or preclinical stage of plaque deposition with relatively little pathological effect on brain tissue and mental function. Our results suggest that the progressively more extensive butyrylcholinesterase reactivity of plaques may participate in their transformation from a relatively benign form to pathogenic structures associated with neuritic degeneration and dementia.
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PMID:Butyrylcholinesterase reactivity differentiates the amyloid plaques of aging from those of dementia. 797 18

Butyrylcholinesterase histochemical techniques were applied to vibratome sections of several cortical areas from the brains of non-demented aged and of Alzheimer's disease patients. At the light microscope level, all the senile plaque types and all the structures with neurofibrillary degeneration showed butyrylcholinesterase reaction product, whereas nearby neuronal perikarya and axons on the same slides remained unstained. Areas containing stained elements were selected, re-sectioned, and finally observed under the electron microscope. Focusing on the sites of neurofibrillary degeneration, butyrylcholinesterase reaction product was found in both intra- and extracellular neurofibrillary tangles, in neurites associated with plaques, and in neuropil threads that were either axons or dendrites. This reaction product was exclusively located over filament bundles, and sometimes covered them so completely that they could not be identified. When the filaments were only partially covered, it was possible to identify them as either paired helical filaments or straight filaments. Occasionally, neurofibrillary tangles, neuropil threads and plaque-associated neurites, all of them containing either paired helical filaments or straight filaments, were found to be completely free of butyrylcholinesterase reaction product. The origin and possible role of butyrylcholinesterase, which is ultrastructurally localized over elements presenting neurofibrillary degeneration, is discussed.
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PMID:Ultrastructural localization of butyrylcholinesterase on neurofibrillary degeneration sites in the brains of aged and Alzheimer's disease patients. 800 45

Neurofibrillary tangles and amyloid plaques express acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activity in Alzheimer's disease. We had found that traditional AChE inhibitors such as BW284C51, tacrine and physostigmine were more potent inhibitors of the AChE in normal axons and cell bodies than of the AChE in plaques and tangles. We now report that the reverse pattern is seen with indolamines, carboxypeptidase inhibitor, and the nonspecific protease inhibitor bacitracin. These substances are more potent inhibitors of the cholinesterases in plaques and tangles than of those in normal axons and cell bodies. These results show that the enzymatic properties of plaque and tangle-associated cholinesterases diverge from those of normal axons and cell bodies. The selective susceptibility to bacitracin and carboxypeptidase inhibitor indicates that the catalytic sites of plaque and tangle-bound cholinesterases are more closely associated with peptidase or protease-like properties than the catalytic sites of cholinesterases in normal neurons and axons. This shift in enzymatic affinity may lead to the abnormal protein processing which is thought to play a major role in the pathogenesis of AD. The availability of pharmacological and dietary means for altering brain indolamines raises novel therapeutic possibilities for inhibiting the abnormal cholinesterase activity associated with Alzheimer's disease.
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PMID:Protease inhibitors and indolamines selectively inhibit cholinesterases in the histopathologic structures of Alzheimer's disease. 823 15

Butyrylcholinesterase (BChE) and an altered form of acetylcholinesterase (AChE) accumulate in the plaques and tangles of Alzheimer's disease (AD). The sources for these plaque- and tangle-bound cholinesterases have not been identified. We now report that AChE and BChE activities with pH preferences and inhibitor selectivities identical to those of plaque- and tangle-bound cholinesterases are found in the astrocytes and oligodendrocytes of control and AD brains. These glial-type cholinesterases are selectively inhibited by indolamines and protease inhibitors. In control brains glial-type cholinesterases appear confined to the intracellular space, whereas in patients with AD they decorate plaques and tangles as well. In control and AD brains AChE-positive glia are distributed throughout the cortical layers and subcortical white matter, whereas BChE-positive glia reach high densities only in the deep cortical layers and white matter. In non-AD control brains, the ratio of BChE to AChE glia was higher in entorhinal and inferotemporal cortex, two regions with a high susceptibility to the pathology of AD, than in primary somatosensory and visual cortex, two areas with a relatively lower susceptibility to the disease process. There was no age-related differences in the density or distribution of cholinesterase-positive glia. In comparison with age-matched control specimens, AD brains had a significantly higher density of BChE glia and a lower density of AChE glia in entorhinal and inferotemporal regions but not in the primary somatosensory or visual areas. These results suggest that glia constitute a likely source for the cholinesterase activity of plaques and tangles and that a high ratio of BChE- to AChE-positive glia may play a permissive or causative role in the neuropathology of AD.
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PMID:Neurological cholinesterases in the normal brain and in Alzheimer's disease: relationship to plaques, tangles, and patterns of selective vulnerability. 836 55


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