Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Some of the biochemical characteristics of acetylcholinesterase from rat and human erythrocytes were studied. 2. Both for rat and man two different acetylcholinesterase molecular forms were identified by gel electrophoresis. The faster moving form is less conspicuous and is not present in all individuals, therefore single-banded and double-banded preparations of red cell acetylcholinesterase can be obtained. The two components appear to be isomers of different molecular size (approximately Mr 150 000 and Mr 245 000) as estimated by gel electrophoresis at different polyacrylamide concentrations. 3. A single band, with a molecular weight of approximately 135 000, was obtained by sodium dodecyl sulphate gel electrophoresis. These results suggest that the faster moving form is a protomer and the slower a dimer. 4. The different sedimentation values obtained by density gradient centrifugation in the presence of Triton X-100 of double-banded (5.3S) and single-banded (6.3S) rat and human acetylcholinesterase preparations, are consistent with a protomer-dimer hypothesis. 5. The isoelectric pattern observed for both double- and single-banded preparations was similar for rat and man acetylcholinesterase and showed a considerable microheterogeneity (thirteen activity bands for rat and eleven for man with isoelectric values from 4.6 to 5.9).
Mol Cell Biochem 1982 Sep 17
PMID:Acetylcholinesterase molecular forms from rat and human erythrocyte membrane. 714 43

Acetylcholinesterase (acetylcholine acetylhydrolase; EC 3.1.1.7) levels of Nematospiroides dubius from laboratory mice and Trichostrongylus colubriformis from lambs have been measured. The anthelmintic levamisole (leavo isomer of 2,3,5,6-tetrahydro-6-phenylimidazo-(2,1b)-thiazole (Tetramizole)) did not affect the level of acetylcholinesterase in N. dubius in vivo but caused a reduction in the level of the enzyme in T. colubriformis following paralysis in vivo. The effect of levamisole on acetylcholinesterase in the nematodes is explained in terms of the differing roles of the enzyme in these two species.
Mol Biochem Parasitol 1981 May
PMID:Changes in the level of acetylcholinesterase of nematospiroides dubius and Trichostrongylus colubriformis following paralysis by levamisole in vivo. 725 46

Acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) activities of Nippostrongylus brasiliensis were measured following treatment of the hosts with oxfendazole and mebendazole. Drug treatment of N. Brasiliensis caused large, sustained increases in enzyme activity in male and female worms which coincided with the expulsion of the nematodes from the small intestine of the host. It is suggested that the increases in acetylcholinesterase activity may be due to an inhibition by the benzimidazole carbamates of the secretion of enzyme to the exterior of the worms which, in turn, leads to expulsion through failure of the so-called "chemical holdfast".
Mol Biochem Parasitol 1981 Nov
PMID:Changes in the acetylcholinesterase activity of the nematode Nippostrongylus brasiliensis following treatment with benzimidazoles in vivo. 732 89

To explore the molecular basis of the biochemical differences among acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) and their alternative splicing and allelic variants, we investigated the acylation phase of cholinesterase catalysis, using phosphorylation as an analogous reaction. Rate constants for organophosphate (DFP) inactivation, as well as for oxime (PAM)-promoted reactivation, were calculated for antibody-immobilized human cholinesterases produced in Xenopus oocytes from natural and site-directed variants of the corresponding DNA constructs. BuChE displayed inactivation and reactivation rates 200- and 25-fold higher than either product of 3'-variable AChE DNAs, consistent with a putative in vivo function for BuChE as a detoxifier that protects AChE from inactivation. Chimeric substitution of active site gorge-lining residues in BuChE with the more anionic and aromatic residues of AChE, reduced inactivation 60-fold but reactivation only 4-fold, and the rate-limiting step of its catalysis appeared to be deacylation. In contrast, a positive charge at the acyl-binding site of BuChE decreased inactivation 8-fold and reactivation 30-fold. Finally, substitution of Asp70 by glycine, as in the natural 'atypical' BuChE variant, did not change the inactivation rate yet reduced reactivation 4-fold. Thus, a combination of electrostatic active site charges with aromatic residue differences at the gorge lining can explain the biochemical distinction between AChE and BuChE. Also, gorge-lining residues, including Asp70, appear to affect the deacylation step of catalysis by BuChE. Individuals carrying the 'atypical' BuChE allele may hence be unresponsive to oxime reactivation therapy following organophosphate poisoning.
Brain Res Mol Brain Res 1995 Jul
PMID:Successive organophosphate inhibition and oxime reactivation reveals distinct responses of recombinant human cholinesterase variants. 747 18

The relationship of genes associated with contact inhibition of cell growth and the commitment for differentiation was studied in the human neuroblastoma cell line SH5Y. These cells could be induced to differentiate in vitro into neuronal-like cells upon incubation with retinoic acid, an event that was accompanied by an enhancement in levels of neuron-specific acetylcholinesterase. The kinetics of differentiation, based on morphology and acetylcholinesterase levels, showed that proliferation arrest always preceded differentiation and may be a prerequisite for differentiation. To determine if this growth arrest is mediated by the same pathway underlying contact inhibition of proliferation, the expression of a gene associated with the induction of contact inhibition, protein disulfide isomerase (PDI), was quantified by Northern blot analysis and enzymatic activity after retinoic acid treatment. Retinoic acid caused a significant elevation of PDI-mRNA within 24 hrs. after treatment with a corresponding increase in enzyme activity which immediately preceded proliferation arrest and differentiation. Bacitracin, a specific inhibitor of PDI, abrogated the ability of retinoic acid to induce differentiation. However, treatment with interferon also increased PDI activity and caused proliferation arrest and SH5Y differentiation but into a fibroblastoid cell without neurite outgrowth. These results suggest that the commitment for differentiation of SH5Y cells involves a form of proliferation arrest in which activation of PDI activity is a required and early event but one that does not determine the final differentiation pathway.
Cell Mol Biol (Noisy-le-grand) 1995 Jun
PMID:Induction of protein disulfide isomerase during proliferation arrest and differentiation of SH5Y neuroblastoma cells. 754 84

Erythrocyte aspartate aminotransferase (AST) and alanine aminotransferase (ALT) activities are often used as indices of vitamin B-6 nutritional status; however, results using a mixed population of erythrocytes can be quite variable. Erythrocytes from two strains of mice (Mus domesticus), A/Ibg and DBA/Ibg, were separated according to age by centrifugation through discontinuous Percoll density gradients into three fractions: top (least dense, youngest), middle and bottom (most dense, oldest). A sufficient yield of age-fractionated erythrocytes was obtained from a single mouse for all of the enzyme measurements. The activities of AST, ALT and three age-marker enzymes, pyruvate kinase, acetylcholinesterase and hexokinase, were found to be significantly higher in the youngest cell fractions, and declined in the older, more dense fractions. A mice had significantly lower AST and ALT activities in the age separated fractions than did DBA mice. The measurement of enzyme activities in low density, young cells may be especially useful in studies involving conditions in which the proportion of young erythrocytes may be elevated with respect to the entire erythrocyte mass.
Comp Biochem Physiol B Biochem Mol Biol
PMID:Aminotransferase activities in mouse, Mus domesticus, erythrocytes separated according to age. 755 57

The interaction of halo-quaternary pyridinium hydrochloride salts on acetylcholinesterase (AChE, E.C.3.1.1.7) has been investigated. Kinetic analysis has shown that they reflect a non-competitive inhibition with Ki values in the range 8-13 microM and 5-34 microM for chloro- and bromo-substituted salts respectively. Spectrophotometry was used to study the binding of the ligands with the enzyme and Scatchard analysis used to calculate the respective dissociation constants (Kd) and the number of binding sites. The substitution position of the halogen on the pyridine ring also influenced the binding capacity and the Ki values.
Biochem Mol Biol Int 1995 Aug
PMID:Protein ligand interactions 7 halogenated pyridinium salts as inhibitors of acetylcholinesterase from Electrophorus electricus. 758 Oct 6

Blood dwelling stages of schistosomes have acetylcholinesterase (AChE) on their teguments. As an initial step towards understanding the function of tegumental AChE, we have used specific ligand-binding assays to identify nicotinic acetylcholine receptors (nAChR) on the schistosome surface. AChR could not be detected on migratory stages using fluoroscein isothiocyanate-alpha-bungarotoxin binding but the amount of specific labelling increased on sexual pairing and as the parasites matured into egg-producing adults. Both AChE and nAChR were concentrated on the dorsal surface of the adult male. These results indicate a role for AChE and AChR associated with the transporting function of this membrane.
Mol Biochem Parasitol 1995 Apr
PMID:Nicotinic acetylcholine receptors on the surface of the blood fluke Schistosoma. 763 Mar 76

Pluripotent embryonic stem (ES) cell cultures provide an efficient method for genome manipulation with many applications in marine biotechnology. To develop this technology we have been working to derive fish ES cell lines for in vitro studies of embryo cell growth and differentiation and for the generation of transgenic fish. Zebrafish embryonal cell cultures were derived from blastula-stage embryos in LDF medium supplemented with fetal bovine serum, trout serum, trout embryo extract, selenium, insulin, and leukemia inhibitory factor. Cultures derived under these conditions on feeder layers of zebrafish embryonic fibroblasts possessed a diploid karyotype and exhibited an ES-like morphology with elevated levels of alkaline phosphatase enzyme activity. Injection of primary cell cultures derived from embryos of transgenic fish carrying neo produced chimeric fish detected by polymerase chain reaction analysis. Embryo cells cultured on poly-D-lysine substrate in the presence of retinoic acid or Buffalo rat liver cell-conditioned medium (BRL-CM) and a reduced serum concentration differentiated into neuronal cell types exhibiting elevated levels of acetylcholinesterase enzyme activity and expression of neurofilament and glial fibrillary acidic protein.
Mol Mar Biol Biotechnol 1995 Sep
PMID:ES-like cell cultures derived from early zebrafish embryos. 767 May 94

We have performed docking studies with the SYSDOC program on acetylcholinesterase (AChE) to predict the binding sites in AChE of huperzine A (HA), which is a potent and selective, reversible inhibitor of AChE. The unique aspects of our docking studies include the following: (i) Molecular flexibility of the guest and the host is taken into account, which permits both to change their conformations upon binding. (ii) The binding energy is evaluated by a sum of energies of steric, electrostatic and hydrogen bonding interactions. In the energy calculation no grid approximation is used, and all hydrogen atoms of the system are treated explicitly. (iii) The energy of cation-pi interactions between the guest and the host, which is important in the binding of AChE, is included in the calculated binding energy. (iv) Docking is performed in all regions of the host's binding cavity. Based on our docking studies and the pharmacological results reported for HA and its analogs, we predict that HA binds to the bottom of the binding cavity of AChE (the gorge) with its ammonium group interacting with Trp84, Phe330, Glu199 and Asp72 (catalytic site) and to the opening of the gorge with its ammonium group partially interacting with Trp279 (peripheral site). At the catalytic site, three partially overlapping subsites of HA were identified which might provide a dynamic view of binding of HA to the catalytic site.
J Comput Aided Mol Des 1994 Dec
PMID:Prediction of the binding sites of huperzine A in acetylcholinesterase by docking studies. 773 3


<< Previous 1 2 3 4 5 6 7 8 9 10