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)

Three morphologically distinct types of neuron that contain acetylcholinesterase have been distinguished by Golgi-impregnation of sections of the rat neostriatum that had been incubated to reveal acetylcholinesterase activity. The neuron that stained most intensely for acetylcholinesterase was a large cell, with smooth or sparsely spiny dendrites; the axon of one these neurons was partially impregnated by the Golgi stain and had local axon collaterals (type 1). Another acetylcholinesterase-containing neuron had a small to medium-size cell body with long sparsely spiny dendrites emerging from opposite poles (type 2). The third type of neuron that contained acetylcholinesterase was medium to large size and had many primary, sparsely spiny dendrites that branched frequently (type 3). Examination of the same Golgi-impregnated, acetylcholinesterase-stained neurons that had been studied in the light microscope by electron microscopy allowed us to distinguish several other differences between the three types of neuron. Whereas all three types had acetylcholinesterase reaction product in the endoplasmic reticulum and along the nuclear envelope, only neurons of type 1 displayed reaction product in the Golgi apparatus. All three types of neuron received synaptic input, mainly along their dendrites. It is concluded that the combination of Golgi-impregnation with histochemical procedures that demonstrate endogenous enzyme activity can be applied to reveal the morphological characteristics, synaptic input and local synaptic output of neurons with specific biochemical properties.
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PMID:The section-Golgi-impregnation procedure--3. Combination of Golgi-impregnation with enzyme histochemistry and electron microscopy to characterize acetylcholinesterase-containing neurons in the rat neostriatum. 620 39

The cytochemical localisation of five hydrolytic enzymes has been studied in the brain capillaries of laboratory animals. Acid phosphatase is present in primary lysosomes of endothelial cells; alkaline phosphatase activity is seen mainly on the plasma membrane of the luminal side but also in the basal lamina. The latter is also active concerning 5'nucleotidase. Butyrylcholinesterase is an enzyme synthesized by most brain capillary endothelial cells, as can be seen by intensive staining of endoplasmic reticulum cisternae. In contrast acetylcholinesterase activity at the capillaries presumably is of neuronal origin. Local neurons appear to secrete this enzyme, which then reaches the endothelial basal lamina via the extracellular spaces. From these cytochemical observations it is concluded that pinocytotic traffic in brain endothelial cells is predominantly from the brain tissue side to the luminal side.
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PMID:Enzyme cytochemistry of the cerebral microvessel wall. 630 81

Exocrine acinar cells possess a unique system of basally located lysosomes. Cytochemically, these lysosomes do not contain acid phosphatase, but react positively for trimetaphosphatase (C Oliver: J Histochem Cytochem 28:78, 1980). The present study extends the morphological and cytochemical characterization of these lysosomes in pancreatic, parotid, and exorbital lacrimal acinar cells from Sprague-Dawley rats and National Institutes of Health Swiss mice. The basal lysosomes are highly pleomoric in nature, and frequently appear as a system of anastomosing tubules of varying width. The lysosomes have a close morphological relationship with both the rough endoplasmic reticulum and mitochondria. In addition to trimetaphosphatase activity, the lysosomes are reactive for aryl sulfatase B, thiolacetic acid esterase, and cholinesterase. Since the cholinesterase activity could not be inhibited by specific inhibitors, this activity is most likely due to the presence of nonspecific esterases. The results of this study confirm the lysosomal nature of the basal lysosomes and underscore the necessity of using multiple enzyme activities to identify and characterize lysosomes.
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PMID:Characterization of basal lysosomes in exocrine acinar cells. 630 50

In order to examine the ultrastructural features of the cholinergic neuron in the striatum (caudatoputamen) of the rat, cytochemistry for acetylcholinesterase was conducted 2-12 h after intramuscular injection of the irreversible acetylcholinesterase inhibitor diisopropylphosphorofluoridate. Light microscopic examination of Epon sections reacted from acetylcholinesterase showed that only large-sized cells in the striatum (25-35 microns in the long axis) were stained intensely. In the case of longer survival periods (10-12 h), some lightly stained cells (medium-sized) were seen dispersed amongst the large acetylcholinesterase-rich cells. Electron microscopic observations were made on ultrathin sections of selected large acetylcholinesterase-rich neurons that were first studied by light microscopy. The nucleus of these cells has an eccentric position and possesses several indentations of the nuclear envelope. The cytoplasm contains abundant organelles, many exhibiting features unique to this cell type. Many stacks of granular endoplasmic reticulum, arranged in a parallel manner and forming typical Nissl bodies, were observed in the periphery of the perikarya, and many distinct golgi complexes were seen in the perinuclear zone. At all post-diisopropylphosphorofluoridate survival times, heavy deposits of acetylcholinesterase reaction product were found within the perikarya of this cell type, for the most part within the cisternae of the granular endoplasmic reticulum. At the longer post-diisopropylphosphorofluoridate survival times, reaction product within the cytoplasm was very dense and appeared to have reached a maximum level. At these times reaction product also appeared in the secondary and tertiary dendritic branches of the large-sized neurons. Of the other cell types in the striatum, two types of medium-sized cells displayed a light deposit of reaction product in their perikarya, but this was observed only at longer recovery times (8-12 h). The majority of cells in the striatum lacked reaction particles. Throughout the early post-diisopropylphosphorofluoridate period, the recovery of enzyme activity in the neuropil was moderate compared to that seen within cell bodies. These findings indicate that the large-sized neuron is the only striatal structure that shows rapid regeneration of acetylcholinesterase activity during the early recovery phase after diisopropylphosphorofluoridate administration. Previous studies have indicated that this type of neuron represents the cholinergic interneuron of the striatum. (ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Ultrastructural observations of the cholinergic neuron in the rat striatum as identified by acetylcholinesterase pharmacohistochemistry. 632 44

The subcellular locations of several enzymes involved in dolichyl monophosphate (Dol-P) metabolism in brain have been investigated. Dolichol kinase is highly enriched in a heavy microsomal fraction from calf brain, while 71% of the Dol-P phosphatase activity was recovered with the light microsomes. Lower amounts of the phosphatase activity were also found in the heavy microsomal, mitochondrial-lysosomal, and synaptic plasma membrane fractions. Since the light microsomal fraction also contained substantial acetylcholinesterase activity, an axon plasma membrane marker, an axolemma-enriched fraction, was prepared from rat brain by a second procedure. A comparison with microsomal and mitochondrial-lysosomal fractions revealed that the axolemma-enriched fraction contained the highest specific activity of Dol-P phosphatase, indicating that the enzyme was present in the axon plasma membrane. The tunicamycin-sensitive UDP-N-acetylglucosamine:Dol-P N- acetylglucosaminylphosphotransferase , glucosyl- phosphoryldolichol (Glc-P-Dol) synthase, Glc-P-Dol:oligosaccharide glucosyltransferase, and the oligosaccharyltransferase were all found predominantly in the heavy microsomes. These results indicate that the enzymes responsible for the initiation and termination of biosynthesis, as well as the transfer of dolichol-linked oligosaccharides, reside in the rough endoplasmic reticulum (ER) of central nervous tissue. Evidence that at least some Dol-P molecules formed by dolichol kinase are accessible to multiple glycosyltransferases in the rough ER of brain is also presented.
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PMID:Subcellular sites of enzymes catalyzing the phosphorylation-dephosphorylation of dolichol in the central nervous system. 632 98

The distal portions of rat colon from 14-, 16-, 18-, and 21-day fetuses, newborns, and adults were histochemically examined for acetylcholinesterase (AChE) activity by light and electron microscopy. The specificity of AChE activity in Auerbach's plexus was confirmed by specific and/or nonspecific cholinesterase inhibition tests. Enzyme activity was first detectable after 18 days of gestation and became stronger with age. The reaction product was demonstrated by electron microscopy in and between the plasma membranes of the nerve fibers and their terminals. Ganglion cells also showed positive activity in the plasma membrane, nuclear envelope, and rough endoplasmic reticulum. The distribution pattern of the reaction product in fetal and newborn rat colons was basically the same as in adult rat colon. Therefore, the localization of AChE activity is considered to be a good marker for identifying premature ganglion cells in Auerbach's plexus, and the degree of AChE staining is a good indication of the degree of maturation of the plexus.
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PMID:Light- and electron-microscopic studies on acetylcholinesterase activity in Auerbach's plexus of the developing rat colon. 650 Sep 93

The effects of prostaglandin (PG) F2 alpha and E2 on the denervated smooth muscle of the urinary bladder in female rats were studied in vivo by histochemistry and electron microscopy. The urinary bladder denervated by bilateral removal of the pelvic ganglion was markedly distended, being filled with urine. Daily intravenous administration of PGF2 alpha or PGE2 for 6 days following the operation showed that rats receiving PGE2 urinated remarkably more than those receiving PGF2 alpha. But the ultrastructural changes on the smooth muscle cells, such as dilated tubules of rough endoplasmic reticulum and large Golgi vacuoles, were more prominent in the PGF2 alpha administrated urinary bladders than in PGE2 administrated ones. On occasion, cholinergic ganglion cells happened to be encountered in the muscular layer of a rat urinary bladder. These intramural ganglion cells and the cholinergic nerve fibers surrounding the cells displayed strong acetylcholinesterase activity, unaffected by bilateral pelvic ganglionectomy.
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PMID:[Innervation of the rat urinary bladder. II. Effects of prostaglandins on the denervated detrusor muscle after bilateral pelvic ganglionectomy]. 653 70

The source of butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) in the ganglion cells of the cat superior cervical and ciliary ganglia has been elusive, inasmuch as the enzyme is present in high concentrations in the neuropil, where it is confined largely to the dendritic and perikaryonal plasma membranes, but appears to be absent from the perikarya. In the present study, ganglionic butyrylcholinesterase was near-totally inactivated by the injection of tetramonoisopropyl pyyrophosphoramide (6.0 mumol/kg of body weight) intravenously. During the ensuing 72 hr, the regenerating enzyme became detectable by the copper thiocholine histochemical method in the somata of essentially all ganglion cells and in the neuropil. Results were similar in preganglionically denervated superior cervical ganglia and in normal ciliary ganglia. These findings suggest (i) that butyrylcholinesterase indeed is synthesized in the ganglion cell perikarya (presumably, the rough endoplasmic reticulum) and transported extremely rapidly to more peripheral cellular sites and (ii) that the synthesis is largely independent of control by any neurotrophic factor provided by the preganglionic axonal terminals. Similar studies were conducted in the rat. In this species, in contrast to the cat, the somata of essentially all ganglion cells of the superior cervical ganglion contain various but at least moderate concentrations of acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) and propionylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8). After injection of tetramonoisopropyl pyrophosphoramide, propionylcholinesterase reappeared in the ganglion cell somata before its accumulation in the neuropil, as would be expected.
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PMID:Identification of the probable site of synthesis of butyrylcholinesterase in the superior cervical and ciliary ganglia of the cat. 657 57

The synthesis, assembly, and processing of the multiple molecular forms of acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) in quail muscle cultures was studied by using lectins to distinguish enzyme molecules residing in different subcellular compartments. Special emphasis was given to the assembly of asymmetric AcChoEase molecules because these appear to be the predominant, if not unique, forms of AcChoEase at the vertebrate neuromuscular junction. All cell surface and secreted AcChoEase forms bind to immobilized wheat germ agglutinin, ricin, and concanavalin A, indicating that they have complex oligosaccharides. After treatment of muscle cells with a membrane-permeable irreversible AcChoEase inhibitor, there is a rapid reappearance of the globular monomeric, dimeric, and tetrameric AcChoEase forms. However, the collagen-tailed asymmetric form does not appear until about 90 min after treatment. Analysis of the AcChoEase oligosaccharides with lectins indicates maturation to complex forms over a 90-min period. A large fraction of the intracellular globular AcChoEase molecules bind only to concanavalin A, indicating that they are assembled in the rough endoplasmic reticulum. In contrast, all intracellular asymmetric AcChoEase binds to wheat germ agglutinin, and a significant fraction binds to ricin, indicating that this unique AcChoEase form is assembled from subunits that have previously acquired complex sugars. I conclude that assembly of asymmetric AcChoEase, hence acquisition of information specifying basal lamina localization, occurs in the Golgi apparatus.
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PMID:Asymmetric acetylcholinesterase is assembled in the Golgi apparatus. 658 3

In the present note we have investigated the cytochemical localization of acetylcholinesterase (AChE) in the chick ciliary ganglion (CG) after post-ganglionic axotomy obtained by ablation of the eyeball. Preliminary results show at quite early stages after axotomy a remarkable reduction of cytoplasmic AChE, the residual one being localized in the rough endoplasmic reticulum. On the contrary synaptic areas, in particular those concerning the calyciform synapses, still show a marked AchE activity, similarly to what observed in physiological conditions. The decrease of cytoplasmic AChe in axotomized CG does suggest the possibility that such AChE undergoes to a topographical rearrangement moving towards the synaptic areas of ganglionic neurons.
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PMID:[Location of acetylcholinesterase in axotomized ciliary ganglia]. 662 26


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