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)

Monoclonal antibodies were used to investigate the immunochemistry of human erythrocyte acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7). A series of experiments on the sedimentation velocity and Stokes radius of acetylcholinesterase and its immune complexes indicated that each antibody recognized a single high-affinity binding site (epitope) on the monomeric enzyme. Further analysis suggested that the antibody-binding sites were replicated on multimeric enzyme forms but were subject to steric hindrance between nearby IgG molecules or adjacent enzyme subunits. The cellular localization of the epitopes was studied by measuring the binding of monoclonal antibodies to the cholinesterase of intact erythrocytes. The results implied that most of the epitopes are exposed to the external media. However, one antibody failed to bind to intact cells, despite a relatively high affinity for detergent-solubilized antigen, possibly because its epitope is buried in the lipid bilayer.
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PMID:Human acetylcholinesterase. Immunochemical studies with monoclonal antibodies. 258 May 61

The effect of selection pressure on the cholinesterase (AChE) activity of two strains of Boophilus microplus (Canestrini) resistant to coumaphos was monitored. Total AChE and protein was determined from three generations of resistant ticks and a susceptible strain. The effect of an AChE inhibitor, coroxon (the oxygen analog of coumaphos), was also determined. The resistance of the susceptible strain (Escondido) to coumaphos remained relatively unchanged throughout the study. The Tuxpan strain lost some of its resistance to coumaphos as the generations proceeded (AChE increased instead of decreased). The Tuxtla strain became more resistant to coumaphos as the generations proceeded (AChE increased).
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PMID:Effect of selection pressure on the cholinesterase of Boophilus microplus (Acari: Ixodidae) resistant to coumaphos. 270 29

To study the yet unknown role of the ubiquitous family of cholinesterases (ChoEases) in developing blood cells, the recently isolated cDNAs encoding human acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) and butyrylcholinesterase (BtChoEase; cholinesterase; acylcholine acylhydrolase, EC 3.1.1.8) were used in blot hybridization with peripheral blood DNA from various leukemic patients. Hybridization signals (10- to 200-fold intensified) and modified restriction patterns were observed with both cDNA probes in 4 of the 16 leukemia DNA preparations examined. These reflected the amplification of the corresponding AcChoEase and BtChoEase genes (ACHE and CHE) and alteration in their structure. Parallel analysis of 30 control samples revealed nonpolymorphic, much weaker hybridization signals for each of the probes. In view of previous reports on the effect of acetylcholine analogs and ChoEase inhibitors in the induction of megakaryocytopoiesis and production of platelets in the mouse, we further searched for such phenomena in nonleukemic patients with platelet production disorders. Amplifications of both ACHE and CHE genes were found in 2 of the 4 patients so far examined. Pronounced coamplification of these two related but distinct genes in correlation with pathological production of blood cells suggests a functional role for members of the ChoEase family in megakaryocytopoiesis and raises the question whether the coamplification of these genes could be causally involved in the etiology of hemocytopoietic disorders.
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PMID:Coamplification of human acetylcholinesterase and butyrylcholinesterase genes in blood cells: correlation with various leukemias and abnormal megakaryocytopoiesis. 273 15

In the blood of rabbits and rats poisoned with Intration, after 1, 3, 6 and 10 days of the experiment activities of AChE and ChE as well as those of beta-GR, AcP, AP and KT were checked. In addition, in the cardiac muscle, kidneys and liver, marker lysosomal hydrolases, i.e. beta-GR and AcP were determined. A long-standing reduction in the activities of AChE and ChE and increase in the activities in the concentrations of nonphysiologically great lysosomal hydrolases and AP were noted. A correlation between the inhibition of cholinesterase and organic lesions was found. Lysosomal enzymes share the responsibility for the necrotic process or rabbits' and rats' cardiac muscles. The use of oximes (PAM and Toxobidine) considerably contributed to reactivation of AChE and ChE and to normalization of the test marker enzymes.
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PMID:[Organ changes in rabbits and rats in phosphothioaliphatic acid poisoning. I. Effect of inhibition of cholinesterase and various marker lysosomal hydrolases on organ changes in rabbits and rats in phosphothioaliphatic acid poisoning]. 279 31

Stabilization of fetal bovine serum (FBS) acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) (AChE) and human butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) (BuChE) by ligands and inhibitors was studied as a function of physical and chemical perturbation. Denaturation of AChE occurred as a binary exponential function in the temperature range studied (50-56 degrees C); the slower fraction progressively diminished as the temperature was increased. Inclusion of ligands or inhibitors stabilized AChE as a function of temperature, ligand concentration and time. The rank order in which ligands stabilized AChE was: edrophonium greater than decamethonium greater than pralidoxime chloride much greater than procainamide. BuChE denaturation was retarded by ligands in the order: decamethonium greater than procainamide greater than edrophonium greater than pralidoxime. A plot of the quotient of the fast/slow ratio against the log of the 50% inhibitory concentration (I50) for ligands providing substantial protection yielded a linear relation, suggesting that these compounds stabilized AChE by a common mechanism involving the anionic site of the active center. Urea-induced cholinesterase denaturation was also retarded by these ligands.
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PMID:Ligand stabilization of cholinesterases. 280 38

The sequence of events leading to the formation of the NMJ based on the data presented in this chapter from rat, chick, and Xenopus muscle can be divided into three developmental stages, as shown in Table I. The essential components of the NMJ are acquired early. Acetylcholine is present and can be released from the growing nerve. Acetylcholine receptors are present in the muscle membrane and are functional even at the earliest times. These components of the junction--ACh release and functional ACh receptors--can develop independently of each other; i.e., cell culture studies have shown that nerve cells are capable of releasing ACh before their growing tips have come into contact with the postsynaptic muscle membrane. Conversely, muscle cells grown without nerve synthesize and incorporate in their membranes functional ACh receptors. This situation ensures that functional (table; see text) contacts can occur even at the earliest times. Local accumulation of ACh receptors is also detected at the earliest times of junction formation. Although cell culture studies have demonstrated that receptors can aggregate in the absence of nerve, it would appear that the nerve plays an important role in directing where the highest density of receptors will be localized. Acetylcholinesterase, identified both histochemically and electrophysiologically, occurs at the presumptive NMJ shortly after synaptic transmission and receptor clustering have begun, suggesting that these events may play a role in localizing cholinesterase. Although the studies on rat and chick muscle support this view, development of AChE on Xenopus muscle does not require prior exposure to nerve or muscle activity. The ultrastructural features characteristic of the adult NMJ also do not become apparent until after synaptic transmission and receptor clustering have been seen. However, detection of small regions of specialization could be easily overlooked at the ultrastructural level, particularly if the tissue has not been serially sectioned. The young tissue is more fragile (Gordon et al., 1974) and may be more susceptible to mechanical damage or alterations from the fixation procedures (Kullberg et al., 1977). For these reasons, results pertaining to when the ultrastructural specializations occur are difficult to interpret and must await identification of these structures by other means. A number of other changes occur at the NMJ late in development: (1) ACh receptors become metabolically more stable, (2) there is a conversion in the kinetics of the ACh receptor channel, and (3) junctional folds become apparent. The extent to which these changes occur varies among the different organisms discussed.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Formation of the vertebrate neuromuscular junction. 290 8

In patients with probable Alzheimer's disease and in controls, acetyl- and butyrylcholinesterase activities were studied in cerebrospinal fluid (CSF) and plasma, and acetylcholinesterase activity of erythrocytes was determined. In addition, the molecular forms of acetylcholinesterase were measured in CSF. Severely demented patients had significantly lower acetylcholinesterase (p less than 0.01) and butyrylcholinesterase (p less than 0.05) activities in CSF than the controls had, but the activities of these enzymes in plasma and erythrocytes were within the same range in both groups. Acetylcholinesterase and butyrylcholinesterase activities in the CSF of mildly demented patients did not differ from control values. The ratio of the intermediate molecular form of acetylcholinesterase to the light molecular form of the enzyme did not differ significantly between patients with Alzheimer's disease and controls. According to our results, AChE levels were lower in the CSF of severely demented patients, but both light and intermediate molecular forms were affected.
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PMID:Cholinesterases in the cerebrospinal fluid, plasma, and erythrocytes of patients with Alzheimer's disease. 291 4

The cholinesterase (AChE) activity and total protein in homogenates of unfed larvae of Amblyomma americanum (L.), A. cajennense (Fabricius), A. maculatum Koch, Anocentor nitens Neumann, and Boophilus microplus (Canestrini) were determined weekly in ticks 1-6 wk of age. There was a considerable variation in total protein, AChE, and the ratio of AChE to protein as the ticks aged. However, AChE activities were constant or increased with age and total protein levels were constant or decreased. No direct relationship was detected between AChE activity and total protein levels. The ratio of AChE to protein increased as the unfed larval ticks aged.
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PMID:Effect of age on cholinesterase activity and protein of unfed larval ticks. 291 44

We have investigated the structure and the cholinesterase features of the brain capillaries in two adult Amphibians (Rana esculenta and Bufo bufo). We found that brain capillaries are un-fenestrated and the endothelial cell edges are joined by tight junctions. The brain capillaries in both species are characterized by high levels of AChE. This enzyme is only localized in the basal membrane, whereas we have found the reaction product neither in the endoplasmatic reticulum nor in the Golgi apparatus. On the contrary the brain capillaries are deprived of BuChE. Only in one experiment traces of reaction product were found. The significance of this datum and the non-nervous role of cholinesterase is discussed.
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PMID:Ultrastructural analysis and cholinesterase activity in the brain capillaries of Bufo bufo and Rana esculenta. 312 23

Polyclonal antisera were raised in rabbits against the purified sialated, presumed-globular tetrameric pseudocholinesterase (pseudo-ChE) from surgeonfish (Leibel: Journal of Experimental Zoology 1988b) and against commercially obtained Electrophorus electroplax AChE. The resulting antisera probes were absolutely specific for their respective antigens and failed to titrate ChE activities heterologously. However, each antisera probe did crossreact with its other respective globular and asymmetric aggregational isozymes. The resultant specific probes were then used to examine interspecific evolutionary conservation of the two ChE activities and, in conjunction with velocity sedimentation analysis and differential paraoxon inhibition, the tissue distribution and molecular polymorphism of these same two enzyme systems in surgeonfish. These experiments suggest the tight evolutionary conservation of AChE in contrast to the apparent high variability of pseudo-ChE amongst the wide range of teleost fishes tested. The native atypical pseudo-ChE was shown to exist, like AChE, as a series of sialated and asialated globular and asymmetric aggregational isozymes whose relative distribution exhibits marked tissue specificity. The extremely high levels of pseudo-ChE characteristic of white skeletal (epaxial) muscle, in particular, was conspicuous, and its occurrence in the sarcolemma is discussed in the context of its possible function and in relation to the apparent lack of evolutionary conservation amongst marine teleosts.
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PMID:Antisera probes to an atypical pseudocholinesterase from surgeonfish reveal immunochemical variability and tissue-specific molecular polymorphism. 318 92


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