Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a previous paper (Burri et al., 1990), we have shown that experimental hyperphenylalaninemia (hyper-Phe) in 3-17 d-old rats leads to reduced myelinogenesis. Such treated rats recover during a 6 w low phenylalanine (Phe) period between days 17 and 59. In order to get more detailed information about the disturbed myelinogenesis and recovery, we measured in hyper-Phe rats the developmental pattern of two brain enzymes typical for myelination, cerebroside sulfotransferase (CST), and 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP), and other developmental parameters. Further, we correlated brain Phe levels with the brain damage in hyper-Phe rats, and we measured brain acetylcholinesterase (AChE) as a neuronal marker. Experimental hyper-Phe rats, injected between postnatal days 3 and 17 with alpha-methylphenylalanine and phenylalanine, showed a delayed age-dependent increase of CST activity, compared to that of controls. In hyper-Phe rats, CST peak activity was reached 2-4 d later, and was lower than in controls. The age-dependent decrease of the CST activity, however, started in test and control rats at the same time, at day 21. Between days 24 and 59, hyper-Phe rats had normal CST activity. CNP activity in hyper-Phe rats was lower than in controls from day 10 to 35, and recovered to normal values between days 35 and 59. Our results indicate that recovery from reduced myelinogenesis is possible after the period of fast myelination without compensatory increased CST activity. Further, the brain damage in test rats with Phe levels higher than average is more severe than in test rats with Phe levels lower than average; and there is no effect of hyperphenylalaninemia on brain neurons containing AChE.
Mol Chem Neuropathol
PMID:Reduced myelinogenesis and recovery in hyperphenylalaninemic rats. Correlation between brain phenylalanine levels, characteristic brain enzymes for myelination, and brain development. 209 83

Exogenously applied dopamine may interfere with cholinergic activity in the brain. The aim of the present work was to study the effect of L-dopa administration on acetylcholinesterase (EC 3.1.1.7) activity in rat (Wistar) brain striatum. Short-term administration of a mixture of L-dopa (10 mg/kg) and carbidopa (1 mg/kg) resulted in an increase in dopamine content and a decrease in acetylcholinesterase activity of the tissue. The greatest changes were found 30 min postinjection, and activity returned to near-control values after 2 h. When the drug mixture was injected for a period of 30 d and the animals were killed 24 h after the last injection, a lower dopamine content and higher enzyme activity were seen, compared to control values. It would appear that chronic administration of L-dopa gradually reduced the dopamine-storage capacity of the striatum and that the activity of acetylcholinesterase might be controlled by the levels of dopamine in the brain striatum.
Mol Chem Neuropathol 1990 Dec
PMID:Short- and long-term effects of L-dopa administration on striatal acetylcholinesterase activity. 209 84

Using chromatography on DE-52 and acetylcholine-Affi-Gel columns, nicotinic acetylcholine receptor was purified to approximately 10,000 fold from Lubrol extract of rat brain with a recovery of 15%. The purified preparation contained no cholinesterase activity. alpha-Bungarotoxin did not inhibit [3H]acetylcholine binding to the purified preparation. Sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed 4 major protein bands with apparent molecular weights of 53,000, 67,000, 80,000 and 108,000. When nicotinic acetylcholine receptor was eluted with either carbachol or nicotine from the affinity column, these major bands were found on SDS-PAGE gels. Immunoblot analysis showed that the Mr 80,000 protein was an acetylcholine-binding subunit and that the Mr 48,000 protein, a minor band on SDS-PAGE gel, was a structural subunit.
Brain Res Mol Brain Res 1990 Apr
PMID:Affinity purification of nicotinic acetylcholine receptor from rat brain. 215 81

1. The influences of enzyme treatments (trypsin and collagenase) on responses to perfused acetylcholine were examined on physically isolated single Aplysia neurons, using the voltage-clamp, internal perfusion, and rapid external perfusion technique. 2. During treatment with trypsin (0.025 to 0.1%) for 10 to 30 min at room temperature (22 to 25 degrees C), the peak amplitude of the Na current induced by acetylcholine increased in a time- and dose-dependent manner, and the decay in the continued presence of acetylcholine was slowed. This effect of trypsin treatment was irreversible after washing for 60 min without enzyme. 3. Edrophonium, a cholinesterase inhibitor, has previously been shown to augment the Na acetylcholine response in this preparation by inhibition of acetylcholinesterase. After treatment of the neuron with trypsin, the augmentation after edrophonium was abolished. Furthermore, in the presence of edrophonium, trypsin also failed to increase the response. The dose-response curve for acetylcholine after treatment of trypsin was similar to that in the presence of edrophonium. These results suggest that the modification of the current response by trypsin is a result of removal of cholinesterase activity from the membrane. 4. In contrast to the effects of trypsin, collagenase (0.03 to 0.1%) for 10 to 60 min did not change the current amplitude of the acetylcholine response. However, collagenase treatment did alter the kinetics of the acetylcholine response in a dose-dependent manner, in that the rate of decay was accelerated. A similar acceleration was seen in the acetylcholine responses on other neurons which were due to Cl or K currents, suggesting that the effect was independent on the type of channel. This effect of collagenase was reversible after 30 to 60 min of washing of the neuron. 5. In the presence of edrophonium or after the treatment with trypsin, collagenase still accelerated the current kinetics of the acetylcholine response, indicating that cholinesterase activity is not related to this effect. Furthermore, heated collagenase (presumably inactivated) had a similar action, suggesting that the enzymatic activity of collagenase is not related to the modification of the response. 6. These results suggest that Aplysia acetylcholinesterase is sensitive to trypsin but not to collagenase. However, the preparation of a collagenase used in these studies contains some factor which alters the response to acetylcholine, but this effect is reversible and unrelated to enzymatic activity.
Cell Mol Neurobiol 1990 Jun
PMID:Influences of trypsin and collagenase on acetylcholine responses of physically isolated single neurons of Aplysia californica. 216 51

Chlorpromazine, an antipsychotic drug, is found to inhibit Na+,K(+)-ATPase activity in rat brain microsomal membranes in vitro in concentration and time dependent manner but some inconsistency is observed when the effect was studied with respect to different temperatures. Various ligands and/or substrate affect the inhibition by chlorpromazine in different ways. The in vivo study with this drug shows that the activities of Na+,K(+)-ATPase, Ca2(+)-ATPase and acetylcholinesterase in the microsomal membranes of different organs are inhibit with increases in concentration or lengths of time of treatment and then levels off.
Mol Cell Biochem 1990 Jun 01
PMID:The chlorpromazine inhibition of transport ATPase and acetylcholinesterase activities in the microsomal membranes of rat in vitro and in vivo. 216 37

The reactive synaptogenesis that takes place in the rat hippocampal formation after certain experimental manipulations affords an opportunity to investigate the molecular events that underlie structural remodeling in the adult CNS. Between 2 and 4 days after lesioning the perforant pathway, levels of the synaptic phosphoprotein, GAP-43 (B50, F1, pp46, neuromodulin), were found to increase markedly in the inner molecular layer (iml) of the dentate gyrus, coincident with the time at which commissural-associational (CA) fibers begin to sprout axon collaterals into dendritic portions denervated by the lesion. GAP-43 immunostaining in the iml began to decline by 8 days but continued to define an expanded CA projection for at least one month. In the outer molecular layer (oml), GAP-43 levels decreased after the loss of perforant pathway terminals and did not return for 2-3 weeks, the time at which sprouting of septal inputs into this layer can be visualized by cholinesterase histochemistry. These results demonstrate that GAP-43 levels change during reactive synaptogenesis, and point to differences among neural systems in their expression of this protein.
Brain Res Mol Brain Res 1990 Jun
PMID:The pattern of GAP-43 immunostaining changes in the rat hippocampal formation during reactive synaptogenesis. 216 97

In Torpedo electric organ much of the acetylcholinesterase is a 'globular' dimer (G2), anchored to the plasma membrane via covalently attached phosphatidylinositol and solubilized by a bacterial phosphatidylinositol-specific phospholipase C. This suggested that selective solubilization with phosphatidylinositol-specific phospholipase C, coupled with immunocytochemistry, might be used to localize G2 acetylcholinesterase in excitable tissues of Torpedo. Cryostat sections of electric organ, electromotor nerve, electric lobe and back muscle from Torpedo ocellata were labelled, using three different antibody preparations to Torpedo acetylcholinesterase, followed by a fluorescent second antibody, before and after exposure to the phospholipase. Sites of innervation on electrocytes and myofibers were labelled selectively, as were motor and electromotor nerves. In all these cases labelling was substantially diminished by prior exposure to the phospholipase. The results support our previous assignment, based on biochemical evidence, for a neuronal and synaptic localization of the G2 acetylcholinesterase in Torpedo. Electric lobe acetylcholinesterase appears insensitive to the phospholipase treatment and lacks certain epitopes present in both electric organ and electromotor nerve enzyme. This suggests that substantial processing of the G2 form occurs concomitantly with its movement from the electric lobe into the electromotor nerve.
Brain Res Mol Brain Res 1990 Aug
PMID:Immunocytochemical localization of phosphatidylinositol-anchored acetylcholinesterase in excitable membranes of Torpedo ocellata. 217 Jul 99

1. Possible interactions of contrathion (pralidoxime sulfomethylate), a reactivator of phosphorylated acetylcholinesterase (AChE), with the regulation of cholinergic transmission were investigated on an identified synapse in the buccal ganglion of Aplysia californica. 2. Transmitter release was evoked either by a presynaptic action potential or, under voltage clamp, by a long depolarization of the presynaptic cell. At concentrations higher than 10(-5) M, bath-applied contrathion decreased the amplitude of miniature postsynaptic currents and increased their decay time. At the same time, the quantal release of ACh was transiently facilitated. The facilitatory effect of contrathion was prevented by tubocurarine but not by atropine. Because in this preparation, these drugs block, respectively, the presynaptic nicotinic-like and muscarinic-like receptors involved in positive and negative feedback of ACh release, we proposed that contrathion activates presynaptic nicotinic-like receptors. 3. Differential desensitization of the presynaptic receptors is proposed to explain the transience of the facilitatory action of contrathion on ACh release. 4. The complexity of the synaptic action of contrathion raises the possibility that its therapeutic effects in AChE poisonings are not limited to AChE reactivation.
Cell Mol Neurobiol 1990 Sep
PMID:Receptor-mediated presynaptic facilitation of quantal release of acetylcholine induced by pralidoxime in Aplysia. 225 62

The mucosal cells of the chicken intestine contain a cholinesterase activity essentially due to butyrylcholinesterase. The enzyme is present during embryonic and post-hatching development. The activity reaches a maximum value at day 19 in ovo and decreases prior to and after hatching up to day 4 ex ovo. Then the activity again rises reaching a second maximum at 2-3 weeks. Beyond this stage, the activity slowly decreases leveling off to the value determined in adult chicken. The enzyme exists as two globular forms (G1 and G4) soluble at low-ionic strengths. The G4 form is predominant in ovo up to day 19. From this stage and after hatching the G1 form is the main one. This change in the form proportion differentiates the mucosal cell butyrylcholinesterase from butyrylcholinesterase of other origins such as the chicken plasma enzyme which always shows a predominant G4 form.
Mol Cell Biochem 1990 Aug 10
PMID:Embryonic and post-natal changes in activity and molecular forms of mucosal cell butyrylcholinesterase in chicken intestine. 227 47

The enzymatic activities of aspartate aminotransferase, GABA-transaminase and acetylcholinesterase were studied by means of histochemical methods in the mesencephalic trigeminal nucleus (MTN) neural complex of the turtle Mauremys caspica. Light microscope observations have demonstrated that MTN neurons have a positive reaction for these enzymes.
Cell Mol Biol 1990
PMID:Light microscope study of the enzymatic activities of aspartate aminotransferase, GABA transaminase and acetylcholinesterase in the mesencephalic trigeminal nucleus neural complex of Mauremys caspica. 237 32


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