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)

In peripheral nerves of mouse embryos Schwann cells exhibit a high activity of unspecific cholinesterase. At first (day 12 of embryonic development) this enzyme occurs in the nuclear envelope and in the granular endoplasmic reticulum. Thus, it is possible to differentiate between Schwann cells and fibroblasts which lack cholinesterase. Later on (day 16) the cholinesterase has shifted to the cell membrane of the Schwann cells. However, only that part of the plasmalemma which encircles single axons and the mesaxons exhibits an irregular deposition of the reaction end product. In newborns the first loops of the just formed myelin sheath are still stained. With maturation of the myelin sheath the enzyme activity disappears. The functional role of cholinesterase is unclear. Possible roles are discussed. The expression of cholinesterase in Schwann cells depends on the integrity of the axons. After a few hours, the cultivation of amputated limbs results in a reduction of the enzyme activity. After 1 day in culture cholinesterase disappears totally.
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PMID:Expression of cholinesterase in the Schwann cells of peripheral nerves during development. 186 52

The ultracytochemical localization of the enzyme acetylcholinesterase (AChE) was studied in the germinal epithelium and cortex during chick ovarian morphogenesis at the 7, 12.5, 14 and 19 day of incubation. The results evidenced at day 7 the presence of the enzyme in some somatic cells, both "dark" and "light" and in some gonocytes. The reaction appears also in some tracts between these types of cells. At day 12.5 the reaction is present in some somatic cells only towards the deepest zone of the cortex, in many oogonia and oocytes and in some tracts between germ and somatic cells. At day 14 and day 19 the various cell categories of the cortex are negative for the reaction. The significance of the presence of the enzyme is discussed in relation to an embryonic cholinergic system active during morphogenesis. Regarding the presence of the enzyme in germ cells, the positivity in endoplasmic reticulum cisternae associated to mitochondria may suggest an implication of the enzymatic activity in the proliferation and transformation of these organelles.
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PMID:Fine localization of the acetylcholinesterase activity in somatic and germ cells during the morphogenesis of chick ovarian cortex. 207 76

Rat liver cholinesterases were found to share properties and characteristics with those expressed in cholinergic tissues. The distribution and presence of different molecular forms of cholinesterases in different subcellular organelles of rat liver were studied. The rough and smooth endoplasmic reticulum and Golgi apparatus were enriched in the G4 molecular form of acetylcholinesterase (AChE) (relative to the G2 molecular form), while the inverse was found in the plasma membrane. The interaction of these molecular forms of AChE with the Golgi membrane was studied in detail. Approximately one-half of the G4 form was free within the lumen while the remainder was an intrinsic membrane protein; all the G2 molecular form was anchored to the membrane via phosphatidylinositol. Only the G1 and G2 molecular forms of butyrylcholinesterase (BuChE) were found in the above subcellular organelles; both molecular forms were soluble within the lumen of Golgi vesicles. These results indicate that rat liver expresses several molecular forms of AChE which have multiple interactions with membranes and that liver is unlikely to be the source of the G4 form of BuChE present in high concentration in the plasma.
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PMID:Differential association and distribution of acetyl- and butyrylcholinesterases within rat liver subcellular organelles. 215 20

The ultrastructural localization of acetylcholinesterase (AChE) activity in guinea pig pineal gland was studied using the copper-glycine procedure. A small number of pinealocytes and bundles of unmyelinated nerve fibers were labeled by the AChE reaction. The AChE-positive pinealocytes were located near blood vessels and distributed in small groups. The AChE reaction product was localized in the perinuclear cistern, in the cisternae of the endoplasmic reticulum (ER), and in the saccules of the Golgi apparatus. These findings suggest that the AChE-positive pinealocytes synthesize AChE. The AChE reaction product was also seen in the intercellular space between pinealocyte processes. Besides pinealocytes, AChE activity was localized on the axolemma of myelinated and unmyelinated nerve fibers and in the basement membrane surrounding unmyelinated nerve fibers. Pseudocholinesterase activity was confined to Schwann cells, which showed the reaction product in their perinuclear cistern, in the cisternae of the ER, and on the plasmalemma.
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PMID:Ultrastructural localization of acetylcholinesterase in the guinea pig pineal gland. 233 Oct 60

The subnuclear and synaptic staining patterns for acetylcholinesterase (AChE) activity and choline acetyltransferase (ChAT) activity were studied in the rat interpeduncular nucleus (IPN) using histochemical and immunohistochemical methods. AChE reactivity was prominent in the neuropil of the rostral, lateral and dorsomedial subnuclei, whereas ChAT immunoreactivity was confined to axons and terminals in the rostral, intermediate and central subnuclei. AChE-positive somata were evident in all the subnuclear divisions of the IPN, and possessed reaction product in the rough endoplasmic reticulum and nuclear envelope. ChAT-positive somata were not present in the IPN. Characteristic axodendritic synapses in the rostral, intermediate and central subnuclei possessed ChAT immunoreactivity presynaptically, and AChE reactivity both pre- and postsynaptically. Other synaptic arrangements in the lateral subnucleus lacked ChAT-immunoreactive terminals, yet possessed prominent AChE reactivity. The results of the present study reveal that AChE reactivity and ChAT immunoreactivity are heterogeneously distributed among the subnuclear divisions of the rat IPN, and that AChE reactivity is present in both the cholinoceptive and noncholinoceptive subnuclei. Although neuronal colocalization of ChAT and AChE activity is not evident in the IPN, AChE-positive neurons are in receipt of putative cholinergic, as well as peptidergic, afferent inputs.
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PMID:A comparison of the subnuclear and ultrastructural distribution of acetylcholinesterase and choline acetyltransferase in the rat interpeduncular nucleus. 233 26

Acetylcholinesterase is a key enzyme in cholinergic neurotransmission for hydrolyzing acetylcholine and has been shown to possess arylacylamidase activity in addition to esterase activity. The enzyme is found at various loci, where its functional significance remains to be clarified, and it exists in multiple molecular forms. Sheep platelets have been shown to exhibit acetylcholinesterase activity associated with plasma membrane (Bp), endoplasmic reticulum (Cp), mitochondria granules (Dp), and soluble (As) fractions. These activities show differences in some physicochemical and kinetic properties. The soluble acetylcholinesterase is the most thermostable, and the enzyme from the Cp fractions shows the lowest affinity for the acetylthiocholine substrate and the strongest inhibition by fluoride. In all cases a noncompetitive inhibition of the enzyme by this ion is found. When membrane-bound acetylcholinesterases were assayed at temperatures between 12 degrees C and 33 degrees C, the Arrhenius plots of all activities exhibited a break point at about 17 degrees C. This discontinuity was abolished by addition of detergent to the assay medium (0.02% Triton X-100, final concentration). Their Hill coefficients were calculated in the presence of fluoride, showing unitary values in all cases, which points to a noncooperative effect and nonallosteric behavior in the particulate enzyme. These results suggest that the sheep platelet acetylcholinesterase associated with membrane-bound systems is modulated by the physical state of its environment, despite the fact that the enzyme might be lipid- or nonlipid-dependent.
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PMID:Subcellular distribution and characterization of acetylcholinesterase activities from sheep platelets: relationships between temperature-dependence and environment. 238 54

A combination of choline acetyltransferase immunohistochemistry and acetylcholinesterase histochemistry was used to characterize the ultrastructural distribution of acetylcholinesterase in identified cholinergic and non-cholinergic neurons in the ferret brain. Previous studies have shown that most of the cholinergic input to the brain arises from choline acetyltransferase-positive neurons found in the neostriatum, basal forebrain and dorsolateral pontine tegmentum. In all these cells intense staining for acetylcholinesterase was localized within the cisternae of the rough endoplasmic reticulum, in the nuclear envelope and Golgi apparatus, and along the plasma membranes of the soma and dendrites. In contrast, the distribution of acetylcholinesterase in non-cholinergic neurons was restricted mainly to the cisternae of the endoplasmic reticulum and the nuclear envelope. Since previous studies have associated high levels of acetylcholinesterase staining with non-cholinergic neurons in the locus coeruleus and substantia nigra zona compacta, these areas were examined as well. The ultrastructural localization of acetylcholinesterase in the principal locus coeruleus neurons was as observed in typical non-cholinergic neurons. On the other hand, the distribution of acetylcholinesterase in the principal cells of the zona compacta of the substantia nigra was more like that found in cholinergic neurons. In conclusion, the subcellular distribution of acetylcholinesterase in the principal cholinergic neurons of the brain follows a characteristic pattern which, with one exception, is different from that of acetylcholinesterase-positive non-cholinergic neurons.
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PMID:Acetylcholinesterase on the dendrites of central cholinergic neurons: an electron microscopical study in the ferret. 247 71

Using an antiserum (AS) raised against rat cerebral acetylcholinesterase (AChE), we revealed a neuron population in lateral and dorsal areas of the posterior rat hypothalamus. These neurons were previously described using antibodies to human growth hormone-releasing factor(1-37) (GRF-37), alpha-melanotropin (alpha-MSH) and melanin-concentrating hormone (MCH). Different intracytoplasmic distributions of the immunodeposits were observed depending on the used serum. Ultrastructural investigations demonstrated that AChE-AS labeled rough endoplasmic reticulum and nuclear envelope in control rats. MCH-AS stained Golgi apparatus in control animals and secretory granules in colchicine-injected rats. GRF-37-AS always revealed secretory granules, and alpha-MSH-AS gave the same staining only after colchicine injection.
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PMID:Coexistence of acetylcholinesterase-, human growth hormone-releasing factor(1-37)-, alpha-melanotropin- and melanin-concentrating hormone-like immunoreactivities in neurons of the rat hypothalamus: a light and electron microscope study. 254 28

Tissue-cultured muscle cells synthesize several oligomeric forms of acetylcholinesterase (AChE) destined for the cell surface or secretion. Previous studies on the biogenesis of AChE polypeptide chains have shown that only a small fraction become assembled into catalytically active oligomers which transit the Golgi apparatus and acquire endoglycosidase H (endo H) resistance. Most of the AChE polypeptides remain endo H-sensitive and are rapidly degraded intracellularly. We now show that all newly synthesized AChE polypeptides are transported from the rough endoplasmic reticulum to the Golgi apparatus where they acquire N-acetylglucosamine. However, approximately 80% of these AChE polypeptides remain endo H-sensitive and are degraded intracellularly with a half-life of about 1.5 h by a mechanism which is insensitive to lysosomotropic agents. These endo H-sensitive AChE molecules can be chased into clathrin-coated vesicles and/or the sarcoplasmic reticulum prior to degradation. Pulse-chase studies of isotopically labeled or catalytically active AChE molecules suggest that there are at least two discreet populations of clathrin-coated vesicles which leave the Golgi, one whose origin is cis/medial and one whose origin is trans. These studies indicate the existence of a post-rough endoplasmic reticulum, non-lysosomal degradative pathway for intra-luminal proteins and suggest that post-translational events at the levels of protein sorting and degradation may play a role in regulating the abundance of exportable proteins.
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PMID:Intracellular transport, sorting, and turnover of acetylcholinesterase. Evidence for an endoglycosidase H-sensitive form in Golgi apparatus, sarcoplasmic reticulum, and clathrin-coated vesicles and its rapid degradation by a non-lysosomal mechanism. 256 79

A subacute toxicity study of propiverine hydrochloride (P-4), a new anti-pollakiuria agent, was carried out using male and female Wistar rats. P-4 was orally administered to rats at dose levels of 2, 10, 50 and 150 mg/kg/day for 13 weeks, followed by 5 weeks recovery period. The results obtained are as follows: 1. In the general conditions, transient salivation was observed immediately after administration and blotted fur at lower abdomen was noted in rats given 50 mg/kg/day or more. There were no deaths related to P-4. 2. Body weight gain was depressed in males given 50 mg/kg/day or more and females given 150 mg/kg/day. No significant changes in food consumption were observed. Water consumption increased in the groups of 50 mg/kg/day or more. 3. Urinalysis revealed an increase of urine volume, decreases of osmotic pressure, protein and urobilinogen, and a slight increase in excretion of electrolyte in rats given 50 mg/kg/day or more. 4. Hematological examinations revealed slight changes such as an increase in erythrocyte count and a shortening of APTT in rats given 150 mg/kg/day. 5. Serum biochemical examinations showed a decrease in triglyceride and increases in gamma-GTP and AlP activities, and urea nitrogen in males given 50 mg/kg/day or more and females given 150 mg/kg/day. Additionally, decreases in total and free cholesterol, and phospholipid for males and an increase of total cholesterol and a decrease of cholinesterase activity for females were detected. 6. At autopsy, atrophy of thymus and spleen was observed in rats given 50 mg/kg/day or more, but without histopathological correlation. Histopathological examinations revealed hypertrophy and fatty degeneration of hepatocytes, which were accompanied with increases of absolute and/or relative liver weight, in males given 50 mg/kg/day or more and females given 150 mg/kg/day. Electron-microscopy showed proliferation of smooth endoplasmic reticulum in the same groups. In the kidney, eosinophilic and intranuclear inclusions in the tubular epithelium were detected, in which cytoplasm there were no toxic injuries, in males given 10 mg/kg/day or more and females given 50 mg/kg/day or more. 7. After 5 weeks recovery period, above-mentioned changes were generally disappeared, suggesting that these were reversible. 8. The non-effective dose levels and the toxic dose levels of P-4 were estimated to be 2 mg/kg/day for males and 10 mg/kg/day for females, and 50 mg/kg/day for males and 150 mg/kg/day for females, respectively.
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PMID:[Thirteen-week oral toxicity study of propiverine hydrochloride in rats]. 260 52


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