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 study deals with the distribution of acid and alkaline phosphatases, ATPase, 5-nucleotidase, nonspecific esterase, specific cholinesterase, and beta-galactosidase in the diencephalon of the frog. The highlights of the present study are the following: i) Acid phosphatase is present in all the neurons, whereas the tracts and commissures are completely negative. ii) Most of the tracts and commissures are positive for 5-nucleotidase. This confirms the author's previous findings that the tracts and commissures of all the areas of frog brain are intensely positive for 5-nucleotidase. iii) beta-galactosidase activity in the nuclei of the diencephalon is either mild or completely absent, whereas the commissures and tracts show positive activity. iv) Habenulothalamic connections are intensely positive for specific cholinesterase and non-specific esterase, moderately positive for beta-galactosidase and completely negative for other enzymes. v) The epiphysis (pineal organ) shows intense reaction for adenosine triphosphatase, acid phosphatase, and 5-nucleotidase and moderate reaction for alkaline phosphatase and non-specific esterase. In contrast to the above enzymes, the specific cholinesterase and beta-galactosidase are completely missing. vi) Lateral forebrain bundles are completely negative for all the enzymes except alkaline phosphatase and beta-galactosidase. The distribution of these enzymes has been correlated with the functional aspects of various nuclei, tracts, and commissures of the diencephalon of the frog.
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PMID:The chemoarchitectonics of the diencephalon of frog (Rana tigrina). 15 81

The epithelial cells in the taste buds of C. jacchus and C. penicillata show a moderate amount of ribonucleic acid an a concentration of a PAS-positive diastase-resistant material at their apical part. These cells are devoid of UDPG-GT, phosphorylases, G-6-PA, alanyl aminopeptidase, leucine aminopeptidase, cholinesterase and MAO; they present a weak reaction of F-1, 6-P Ald, LDH, SDH, MDH, cytochrome oxidase, beta-OHBDH, nonspecific esterase and acid phosphatase and a stronger reaction to ADH, NADPH2-TR, ATPases, alpha-GPDH, alkaline phosphatase, 5-nucleotidase and GDH. Although some enzymes (alkaline phosphatase, 5-nucleotidase and ATPases) have an almost uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller taste buds of the fungiform papillae. As a rule the apical part of the cells shows a stronger enzymatic reactivity. The taste buds of the marmosets are penetrated by acetylcholinesterase positive nerve fibers whereas the autonomic ganglia in the connective tissue contain both-acetyl and butyrylcholinesterase.
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PMID:Histochemical observations on the taste buds of the marmosets (Callithrix jacchus and Callithrix penicillata). 15 39

A procedure is described for isolating two membrane fractions from rabbit spinal-cord white matter enriched with 5'-nucleotidase, a nonspecific plasma membrane marker, 2',3'-cyclic nucleotide phosphohydrolase, an oligodendroglial plasma membrane marker, and acetylcholinesterase, an axonal plasma membrane marker. While the two membrane fractions exhibited similar enrichments with respect to cyclic nucleotide phosphohydrolase, enrichments of 5'-nucleotidase and acetylcholinesterase were significantly greater in the heavier membrane fraction. Selected enzyme markers for cyto- and mitochondrial membranes were not detected. Moreover, gray matter did not yield homologous membrane fractions in the gradient when subjected to the identical procedure, indicating that the two membrane fractions were unique to white matter. While electronmicroscopic examination revealed that both membrane fractions were comtaminated with myelin, the heavier fraction was least contaminated and exhibited a fair degree of homogeneity with respect to single membrane vesicular profiles. It was concluded that both membrane fractions were enriched with oligodendroglial and axonal plasma membranes, with the heavier fraction containing significantly more axolemma.
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PMID:Isolation of non-myelin plasma membranes unique to white matter. 19 99

Axolemma-enriched fractions were prepared from rat brain by osmotic shock of a purified preparation of myelinated axons and subsequent separation of myelin, two axolemma-enriched fractions and myelin-free axons by density gradient centrifugation. Compared with the starting whole homogenate, the fractions were enriched in specific activity of Na+K+ ATPase, acetylcholinesterase, 5'nucleotidase as well as 2',3'-cyclic nucleotide 3'phosphohydrolase. Compared with myelin, the axolemmal fractions are greatly enriched in high molecular weight proteins. The 1.0/1.2 fraction has a predominant peak of fucose-labeled glycoprotein with a molecular weight between that of the myelin associated glycoprotein and the Wolfgram protein which is absent from the myelin glycoprotein profile. Polyacrylamide gel electrophoresis showed that the protein profile of myelin isolated by this procedure was similar to that of myelin isolated by other procedures and that the myelin specific basic and proteolipid proteins were virtually absent in the axolemma-enriched fractions. Both axolemma fractions were enriched in higher MW proteins, some of which resembled proteins in the myelin protein profile. Both axolemma-enriched fractions specifically bind between 2 and 3 pmoles of [3H]tetrodotoxin per mg protein. The axolemma-enriched fractions incorporated [3H]leucine and [14C]fucose exclusively into high molecular weight proteins and glycoproteins. In contrast myelin concomitantly isolated with the axolemma-enriched fractions had a significant amount of [3H]leucine labeled protein in myelin proteolipid and basic proteins. In addition to the myelin associated g-ycoprotein the [14C]fucose labeled a glycoprotein of slightly larger apparent molecular weight than proteolipid protein was found in the myelin fraction while the comparable labeled glycoprotein was absent in the axolemma-enriched fractions. The possible extent of contamination of these fractions by myelin or myelin subfractions and relationship of these axolemma-enriched fractions to other axolemma preparations are discussed.
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PMID:Isolation and partial characterization of rat CNS axolemma enriched fractions. 20 16

The distributions of acid and alkaline phosphatases, 5-nucleotidase, ATPase, non-specific esterase, specific cholinesterase, succinic dehydrogenase and beta-galactosidase are described in the mesencephalic auditory, tegmental and cranial nerve nuclei of the frog (Rana tigrina). The main results of the study are as follows: The laminar, principal, and magnocellular nuclei of the torus semicircularis, which are associated with auditory functions, show intense activity of specific cholinesterase. On the other hand, the commissural and subependymal mid-line nuclei, whose functions are doubtful, show a complete lack of this enzyme. The nucleus isthmi shows intense acid phosphatase, ATPase, non-specific esterase, specific cholinesterase and succinic dehydrogenase activities. Non-specific esterase is virtually absent from all the areas studied except the nucleus isthmi and the 3rd and 4th cranial nerve nuclei. Most of the commissures and fibre tracts show intense activity for beta-galactosidase and 5-nucleotidase. The possible roles of these enzymes in glycolipid and myelin metabolism are discussed.
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PMID:Histoenzymological analysis of mesencephalic auditory, tegmental and cranial nerve nuclei in the frog (Rana tigrina). 21 17

Subfractions of fraction A, which floats on top on 0.8 M sucrose in the classical density gradient used for the isolation of brain subcellular fractions (A1 corresponding in adult rats to myelin and A2 which corresponds to the myelin-like fraction), were studied in comparison to other brain subcellular fractions in 5 day old rats and at different stages of development, up to 60 days of age. Variations in the enzymatic activity of acetylcholinesterase, non-specific cholinesterase and 2',3'-Cyclic nucleotide phosphohydrolase, changes in lipid and protein composition and turnover of phosphatidyl choline were investigated. Results indicate that fractions A1 and A2 obtained prior to the beginning of myelination could be composed of fragments of the oligodendroglial cell plasma membranes, and that both fractions undergo substantial changes in chemical composition, enzymatic activity and in turnover of phosphatidyl choline during maturation. In vivo experiments at short times, using radioactive choline as a precursor of phosphatidylcholine suggest that membrane fragments isolated in fraction A2 are precursors of those isolated in fraction A1 at all ages.
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PMID:Turnover of phosphatidyl choline and changes in enzymatic activity in cell membranes of the CNS during early myelination. 22 34

Exposure to a 60 Hz, 4 uT electromagnetic field caused significant changes in levels of 5'nucleotidase (5'NT), acetylcholinesterase (AChE) and alkaline phosphatase (ALP) during early embryonic development in the chicken. Enzyme levels were significantly higher in embryos with various forms of anatomic malformations (abnormal) than in those with no visible abnormal characteristics (normal). The presence of the electromagnetic field was associated with a marked reduction in enzyme activities in abnormal embryos. Overall mean specific activities for 5'NT, AChE and ALP were 12, 57, 67 and 38, 196, 111 nmol/min/mg protein in abnormal-exposed versus abnormal-control embryos, respectively. In normal-exposed versus normal-control embryos, the values were 5, 28, 57 and 10, 29, 58, respectively.
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PMID:Effects of extremely low-frequency electromagnetic fields on three plasma membrane-associated enzymes in early chicken embryos. 148 2

In order to define metabolic profiles of smooth muscle cell (SMC) modulation, 16 enzyme activities linked to nucleotide hydrolysis, lipolysis, lysosomal reactivity and intermediate glucose catabolism were compared in four rat arterial models, exhibiting four metabolic phenotypes of modulated smooth muscle cells: (i) "primary synthetic" statein immature aorta; (ii) "contractile" state in adult aorta; (iii) "hypertensive" state in aorta of hypertensive rat, SHR; (iiii) "secondary synthetic" state in diffuse intimal thickening of ligated carotid artery. Contractile SMC presented strong activities of enzymes linked to nucleotide ester hydrolysis and contractility (ATP-A-Ca, ATP-A-Mg, ATP-A-Ca/Mg, 5'nucleotidase) and to lipolytic process (butyryl cholinesterase, acid esterase). These enzyme activities were more pronounced in "hypertensive SMC". Incontrast, the same enzymes were weakly active or not expressed in "synthetic SMC". Increased lysosomal enzyme reactivity was a particular expression of "secondary synthetic SMC". The observed enzyme abnormalities in reactively modulated SMC (proliferative-synthetic phenotype) might be related to the loss of contractility and to the enhanced cell proliferation and lipid accumulation, characteristic features of modulated SMC in atherogenesis.
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PMID:Enzyme histochemical expressions of smooth muscle cell modulation in arterial development, hypertension and remodeling. 193 22

Neurotransmitter-related (choline acetyltransferase, acetylcholinesterase, glutamate decarboxylase, L-glutamate and GABA high affinity uptake) and glial neurochemical markers (glutamine synthetase, beta-alanine uptake and 2',3' cyclic nucleotide phosphohydrolase) have been quantitatively assayed in various regions of the rat CNS during normal postnatal development: spinal cord, cerebellum, superior colliculus, hippocampus, striatum, visual cortex, frontal sensory-motor cortex and prefrontal cortex. In general, neurochemical markers show an obvious trend toward increasing levels in parallel with brain maturation. However, some relevant exceptions have been observed and discussed. Detailed knowledge of regional neurochemical brain maturation is important since it gives us information concerning some key events of brain development. In addition, this knowledge is the essential pre-requisite for studies aimed at the alteration of specific regional and temporal parameters through experimental manipulation.
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PMID:Regional maturation of neurotransmitter-related and glial markers during postnatal development in the rat. 197 Feb 17

The effects of ethanol on the activities of five membrane bound enzymes were determined using a crude membrane preparation obtained from cortex of long-sleep (LS) and short-sleep (SS) mice. These two mouse lines were selectively bred for differences in duration of ethanol-induced sleep time. The enzymes studied were two forms of NaK-ATPase, Mg-ATPase, 5'nucleotidase, and acetylcholinesterase. Arrhenius plots of the ethanol-temperature-enzyme activity studies indicate specificity in ethanol's actions. NaK-ATPase activity consists of two enzymes which were distinguished by sensitivity to ouabain. The Arrhenius plot of the high ouabain sensitivity enzyme (low Ki) exhibited a transition temperature which was reduced twice as much by ethanol in LS membranes as in SS membranes. Ethanol did not affect the transition temperature of the high Ki NaK-ATPase but the control (no ethanol) transition temperature was 2.7 degrees higher in SS membranes. Arrhenius plots of Mg-ATPase activity did not exhibit a transition temperature and ethanol did not alter enzyme activity. Ethanol did not alter the transition temperatures of 5'nucleotidase or acetylcholinesterase but the control transition temperature for acetylcholinesterase was 2.3 degrees higher in SS membranes. These results indicate specificity in ethanol's actions on membranes and that inhibition of the lipid-enzyme interactions for the low Ki NaK-ATPase is correlated with the difference in sensitivity to ethanol seen between the LS and SS mice.
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PMID:Ethanol and temperature effects on five membrane bound enzymes. 615 1


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