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:3.1.1.7 (acetylcholinesterase)
28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ultrastructural features and the acetylcholinesterase (AChE) localization of the rat habenula have been studied. On the basis of different morphology and AChE content, it is suggested that at least two types of neurons are present in the medial habenula (MHb) and three types of neurons in the lateral habenula (LHb). In particular, actively AChE-synthesizing neurons have been noticed in both LHb and MHb. Some unusual ultrastructural arrangements of the endoplasmic reticulum have been described in habenular neurons. Finally, the most common types of synaptic contacts present in the habenular complex have been surveyed.
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PMID:Ultrastructural features and acetylcholinesterase histochemistry of the rat habenular complex. 663 74

In this study, maturational alterations in acetylcholinesterase-dependent staining of the thalamic ventrobasal complex of rat and mouse were examined. The study was undertaken to address the question of whether this nucleus exhibits transient acetylcholinesterase positivity during its development and whether the enzyme is likely to be synthesized by its immature intrinsic neurons. Also, the patterning due to acetylcholinesterase staining of cells and fibers, and the developmental changes in these patterns, have not been described in earlier work. In contrast to surrounding thalamic nuclei, the ventrobasal complex is acetylcholinesterase-positive at birth. In rat, acetylcholinesterase staining of the ventrobasal thalamus is still more intense than in adjacent nuclei at the end of the first week postnatally. Virtually all somata in the nucleus are filled with dense reaction product at this time. Ultrastructurally, reaction product is associated with the granular endoplasmic reticulum. At this stage, there is a marked difference in intensity of staining between the medial and lateral subdivisions of the nucleus, and patterned clustering of somata within each subdivision is readily appreciated in acetylcholinesterase-stained material. In the second postnatal week, intrinsic acetylcholinesterase activity is progressively lost. By the end of the third postnatal week, the nucleus is quite pale except for one area. In the posterior portion of the lateral subdivision, adjacent to the nucleus reticularis, interconnecting bundles of acetylcholinesterase-positive fibers enter the nucleus. They course medially in the lateral subdivision and break up into a plexus of fine fibers. The development of acetylcholinesterase-dependent staining patterns in the mouse is quite similar, except that histochemically detectable levels of enzyme are substantially lower in the neonatal period. It is concluded that the ventrobasal complex can be distinguished from other thalamic nuclei in regard to earlier onset and/or transience of acetylcholinesterase staining. Ultrastructural observations suggest that virtually all immature ventrobasal neurons are synthesizing acetylcholinesterase. It is suggested that the transient staining for enzyme is due primarily to alteration in synthesis and/or turnover in neurons of the ventrobasal complex. In addition, the acetylcholinesterase staining reveals a patterning of fibers and cells that also undergoes developmental alteration. Evidence is discussed suggesting that axons in the barrels of somatosensory cortex (SmI) are derived from these transiently acetylcholinesterase-positive somata. Consequently, the loss of acetylcholinesterase fiber staining in the barrels, during the third postnatal week (noted previously), may be related to a decrease in synthesis of enzyme in the neuronal somata of the ventrobasal complex.
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PMID:Acetylcholinesterase in the ventrobasal thalamus: transience and patterning during ontogenesis. 664 36

Previous work by our group has demonstrated that mesencephalic neural crest cells at an early stage of migration are able to synthesize acetylcholine (ACh). Acetylcholinesterase (AChE), the enzyme responsible for ACh degradation, was examined in neural crest cells of the chick embryo, using cytochemical and biochemical methods. Observations at the light microscope level showed that cholinesterase activity, identified as true AChE, was present at all axial levels in presumptive crest cells of the neural folds, soon after closure of the neural tube. Subsequently, AChE activity was found in cells of the individualized neural crest and in crest cells migrating at cephalic and trunk levels. Cell counts revealed that 88-94% of the total crest population was AChE-positive. Electron microscope observations indicated that the enzyme was confined to perinuclear and endoplasmic reticulum cisternae. The AChE of migrating mesencephalic neural crest cells was identified as the dimeric form (sedimentation coefficient 6.9 S) of the catalytic subunit. These results indicate that the specific AChE is present in the majority of neural crest cells all along the neural axis. Thus the ability to synthesize and degrade ACh is expressed at least in some neural crest cells at an early stage of development.
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PMID:Cholinergic traits in the neural crest: acetylcholinesterase in crest cells of the chick embryo. 686 7

A method is described allowing localization of acetylcholinesterase (AChE) by both light and electron microscopy. During the reaction lead thio-diacetyl is decomposed, and therefore precipitated as PbS in the presence of native -SH group produced by the hydrolysis of acetylthiocholine perchlorate. The reaction takes place at neutral pH, since improves the sensitivity of AChE localizations. Application of the method to parasympathetic neurons showed that AChE was mainly localized in the rough endoplasmic reticulum of the perikaryons. No reaction was visible in glial cells. AChE was also localized on the plasma membrane of parasympathetic neurons. In mouse embryo muscles AChE activity was seen to be high and was not yet restricted to the synaptic area. The well developed Schwann cells accompanying the neurites displayed constant AChE activity on their plasma membrane.
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PMID:Ultrastructural localization of acetylcholinesterase. A direct method for light and electron microscopy. 698 1

Cytochemical localization of acetylcholinesterase (AchE, E.C.3.1.1.7) was studied in cat bone marrow. The reaction product precipitate was present only in megakaryocytes, and all other marrow cells were AchE-negative. Moderate electron dense AchE reaction product was found in basophilic megakaryocytes in the nuclear membrane, endoplasmic reticulum, Golgi complex, and demarcation membrane system (DMS). In granular and thrombocytogenic stages the intense AchE reaction product was present in all cytoplasmic membranes. The Golgi-derived AchE-positive granules were found to fuse with DMS and their contents were discharged into the extracellular compartment.
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PMID:Acetylcholinesterase in cat megakaryocyte. Evidence for extracellular secretion. 702 57

In the PC12 clonal nerve cell line derived from a rat pheochromocytoma, the activity of acetylcholinesterase (AChE) is regulated by nerve growth factor (NGF). The specific activity of AChE was significantly increased 2 days after exposure of PC12 cells to NGF (8 X 10(-8) M), and reached its maximal increase of 94% after 3 days. Thereafter the specific activity of AChE did not significantly vary during the following 7 days. AChE cytochemistry showed the enzyme activity to be localized predominantly in cisternae of the rough endoplasmic reticulum, with a strongly enhanced activity after NGF treatment.
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PMID:Regulation of acetylcholinesterase by nerve growth factor in the pheochromocytoma PC12 cell line. 705 5

The development of the lamellar cells of mouse digital corpuscles (Meissner corpuscle) was studied by light and electron microscopic histochemistry for cholinesterase (ChE) The materials used were the hind limbs taken from fetuses at 14, 17 and 20 days of gestation, and from young mice at 1, 5, 7, 15 and 20 days after birth. Embryonal Schwann cells had non-specific ChE activity in the cisternae of the rough endoplasmic reticulum and the nuclear envelope, suggesting that they had the ability of synthesizing the enzyme. After birth, such ability gradually decreased and by five days of age non-specific ChE activity was no longer demonstrable in Schwann cells at the time when myelin sheath formation began. However, Schwann cells which were associated with the axonal tips penetrating into the epidermis still had an intense non-specific ChE activity. Such Schwann cells surrounded the axons in gradually increasing numbers of cytoplasmic processes, which later became the lamellae around the axon terminals; thus by 20 days after birth they had differentiated into mature lamellar cells of Meissner corpuscles. These lamellar cells had, as in the embryonal Schwann cells, an intense ChE activity in the cytoplasm. These findings indicate that the lamellar cell is a specialized form of Schwann cell which still retains the embryonal characteristics for synthesizing non-specific ChE.
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PMID:Histochemical study of lamellar cell development of Meissner corpuscles. 710 93

The myotome of early chick embryos was investigated histochemically by means of the acetylcholinesterase (AChE) reaction. Light-microscopically, at the cervical level, the myotome was first recognized and AChE activity demonstrated at stage 13 (2-day-old embryo). Subsequently, the myotome elongated ventro-laterally along the inner surface of the dermomyotome and reached the ventro-lateral end of the dermomyotome at stage 17 to 18 (3 day-old embryo). AChE activity in the myotome showed subsequent increase in intensity during the course of development. The myotome consisted mainly of AChE-positive cells displaying enzymatic activity along the nuclear membrane and within the cytoplasm. In contrast, almost all cells of the dermomyotome and the interstitial cells were AChE-negative. Electron-microscopically, the myotome cells of the 2 day-old embryo and the cells in the dorso-medial portion of the myotome of the 3 day-old embryo were morphologically undifferentiated; AChE activity was detected in the nuclear envelope and in single short profiles of the endoplasmic reticulum (ER). On the other hand, in the 3 day-old embryo the cells in the ventro-lateral portion of the myotome showed AChE activity in the nuclear envelope, numerous profiles of the ER and some Golgi complexes. These AChE-positive cells were regarded as developing myogenic cells based on their morphological characteristics. The present findings indicate (i) that the appearance of AChE activity in the cytoplasm is the first sign of the differentiation of myogenic cells, and (ii) that in these myogenic cells the increase in AChE activity is based on the development of the ER.
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PMID:Acetylcholinesterase activity in the myotome of the early chick embryo. 717 12

Cat superior cervical ganglia (SCG), denervated preganglionically 6-8 d previously, were stained for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) by the bis-(thioacetoxy)aurate (I), or Au(TA)2, method and compared by electron microscopy with normal SCG described previously (Davis, R., and G. B. Koelle. 1978. J. Cell Biol. 78:785-809). In confirmation of earlier light microscopic findings by the highly specific copper thiocholine method, there was nearly a total disappearance of AChE from the ganglion; no myelinated or unmyelinated axons with AChE-stained axolemmas were found, and only occasional traces of AChE staining were noted at dendritic and perikaryonal plasma membranes. Considerable staining for BuChE persisted at the latter sites, however. As in the normal SCG, physostigmine-resistant staining, caused by noncholinesterase enzymes plus the possible presence of very low concentrations of AChE or BuChE, was noted at external mitochondrial membranes, elements of the endoplasmic reticulum of neurites and Schwann cells, and also in lysosomes. These findings confirm the previous identification of AChE-stained myelinated fibers in the normal SCG as preganglionic and of the unstained myelinated fibers as postganglionic. It is proposed that the maintenance of AChE at postsynaptic sites in normal ganglia is caused by the release of a trophic factor(s) from presynaptic terminals. The source of the postsynaptic BuChE, which is apparently completely absent from the endoplasmic reticulum of the ganglion cells, remains unexplained.
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PMID:Electron microscope localization of acetylcholinesterase and butyrylcholinesterase in the superior cervical ganglion of the cat. II. Preganglionically denervated ganglion. 721 5

With the use of quantitative histochemistry and cytochemistry methods the localization of acetylcholinesterase in the brain of man and animals in cases of acute poisoning with organophosphorus compounds was studied. In the brain of animals poisoned with chlorophos the activity of the enzyme, according to cytophotometric findings, dropped 2 or 3 times, this drop being more pronounced in the neuropile. In the human brain, the drop of the acetylcholinesterase activity caused by organophosphorus compounds was the most pronounced in the neuropile and the neurons of the cortex, caudate nucleus and hypothalamus. The cytochemical examinations of the enzyme in the cases of poisoning showed absence of the sediment on the basal membrane of the capillaries and the membranes of the nervous fibres and synapses. However, acetylcholinesterase was found to remain active in some neurons at the nuclear membrane and in the endoplasmic reticulum (presence of the sediment in the form of individual granules or discrete zones). Probability of the acetylcholinesterase activity inhibition mainly in the outer (in relation to the neuron) barrier systems and possibility of reparative processes in the neurons are discussed.
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PMID:[Effect of anticholinesterases on acetylcholinesterase distribution in the human and animal brain (cytochemical study)]. 723 52


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