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:3.1.4.37 (CNPase)
539 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzymatic activities in post-mortem rat brain kept at 4 degrees C and at 25 degrees C were determined for a number of enzymes localized in specific cell types in the central nervous system. Choline acetyltransferase (CAT), glycerol-3-phosphate dehydrogenase (GPDH), glutamine synthetase (GS), lactate dehydrogenase (LDH) and 2',3'-cyclic nucleotide phosphohydrolase (CNPase) were found to be very stable at both 4 degrees C and 25 degrees C with only slight, if any, losses of activity being seen even at periods as long as 72 hr. Glutamic acid decarboxylase (GAD) activity was less stable than that of the other enzymes. In brains kept at 4 degrees C GAD activity was stable out to 24 hr after which it began to decline rapidly to 65% of control at 72 hr. In brains kept at 25 degrees C, GAD activity was stable for 6-8 hr and then began to steadily decline to 58% of control at 24 hr and 29% of control at 72 hr. Assuming that these enzymes have similar stabilities in post-mortem human brain, the effect of post-mortem delay in processing tissues may be of lesser significance than other factors with regard to the measured enzyme activities in human brain samples.
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PMID:Stability of neuronal and glial marker enzymes in post-mortem rat brain. 301 Jan 49

Developmental changes in protein N-glycosylation activity have been studied using cultures of dissociated fetal rat brain cells as an in vitro model system. These cultures undergo an initial phase of neurite outgrowth and cell proliferation (4-6 days in culture), followed by a period of cellular differentiation. N-Glycosylation activity has been measured by assaying the incorporation of [2-3H]mannose into dolichol-linked oligosaccharides and glycoprotein over a period of 1-25 days in culture. This study revealed a marked induction of N-glycosylation activity beginning at approximately 1 week of culture. [2-3H]Mannose incorporation into the oligosaccharide-lipid intermediate fraction and glycoprotein reached maximal values between 12 and 16 days of culture and declined thereafter. The major dolichol-linked oligosaccharide labeled by the brain cell cultures was shown to be Glc3Man9GlcNAc2 by HPLC analysis. Parallel incorporation studies with [3H]leucine showed that the increase in protein N-glycosylation was relatively higher than a concurrent increase in cellular protein synthesis observed during the induction period. Maximal labeling of glycoprotein corresponded to the period of glial differentiation, as indicated by a sharp rise in the marker enzymes, 2',3'-cyclic nucleotide 3'-phosphohydrolase (an oligodendroglial marker) and glutamine synthetase (an astroglial marker). The results describe a developmental activation of the N-glycosylation pathway and suggest a possible relationship between N-linked glycoprotein assembly and the growth and differentiation of glial cells.
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PMID:Induction of N-glycosylation activity in cultured embryonic rat brain cells. 333 55

The metabolism of thyroxine (T4) and triiodothyronine (T3) in cultured glial cells was studied in situ. Cultures were prepared from fetal rat brain and grown for the last 4 days in a chemically defined medium (CDM). They contained astrocytes and oligodendrocytes as shown by the enzyme markers, glutamine synthetase and 2',3'-cyclic nucleotide phosphohydrolase. These cells contained high affinity (22-33 pM), limited capacity (120-230 fmol/mg DNA) nuclear receptors for T3. Cells incubated in situ with 50 pM [125I]T4 actively metabolized the hormone. The major iodothyronine produced was T3 (220-570 fmol/4 h/mg DNA). About 70% accumulated in the cells, the remainder was released into the medium. Within the cells, T3 was partly bound to the nuclear receptors (16.5-20 fmol/mg DNA). Reverse T3 (rT3) was a minor metabolite (30-45 fmol/4 h/mg DNA); it was almost completely released into the medium. The half-life of [125I]T3 (50 pM) was found to be about 15 h. These results show that, in situ, glial cell cultures containing astrocytes and oligodendrocytes grown in CDM actively deiodinate T4 to T3 and degrade T3 rather slowly.
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PMID:Thyroid hormone metabolism by glial cells in primary culture. 380 6

Macromolecular markers for glial cells have been sought for a variety of reasons. One of the earliest was the need for a means of assessing the purity of cell and subcellular fractions prepared from nervous tissue. While there is still a requirement for this kind of tool, emphasis has shifted towards seeking information on biochemical differentiation among cells and their functional interactions. A brief general review will be made of glial markers and two of these, 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) and glutamine synthetase (GS), will be considered in detail. Until recently studies of markers have been concentrated on the higher vertebrates and those on lower vertebrates and invertebrates have hardly begun. However, such comparative studies may lead to fresh insight into old problems. For example, CNP has long been regarded as a marker for myelin and oligodendrocytes but it has not been possible to attribute a functional role to it and its relation to myelination has remained obscure. The finding that it is present in the glia of a moth Manduca sexta which lacks myelin provides a stimulus for a fresh approach to the problem. Another example is provided by studies on GS. This enzyme is found in astrocyte feet and preliminary results indicate that it is localized also in the perineurial glia of Aplysia ganglia. These results lead to a reconsideration of the perennial question of the possible role of astrocyte feet in barrier mechanisms. Extension of comparative studies may not only raise new questions but also provide some answers.
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PMID:Comparative studies on glial markers. 612 Sep 87

Serum-free aggregating cell cultures of fetal rat telencephalon grown in the presence of 3 ng/ml (5 X 10(-10) M) epidermal growth factor (EGF) until day 12 showed 2- to 3-fold increased activities in the two glial enzymes, glutamine synthetase (GLU-S) and 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNPase). This effect was concentration-dependent, with maximal stimulation in cultures treated daily with 3 ng/ml EGF. Addition of EGF during the first 10 culture days was sufficient to produce a maximal stimulation of both GLU-S and CNPase on day 19, whereas treatments starting on day 12 were ineffective. The stimulation of GLU-S preceded that of CNPase. The EGF-induced increase in GLU-S activity was not directly dependent on the presence of insulin, triiodothyronine, or hydrocortisone in the medium, whereas insulin was required for the stimulation of CNPase. A single dose of 5 ng/ml EGF on day 2 caused a slight but significant decrease in DNA synthesis after day 6. The present results indicate that in serum-free aggregating cell cultures of fetal rat telencephalon EGF partially inhibits DNA synthesis, and stimulates an early step in glial differentiation.
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PMID:Epidermal growth factor (EGF) stimulation of cultured brain cells. I. Enhancement of the developmental increase in glial enzymatic activity. 614 40

The production of extracellular soluble proteins was studied in serum-free aggregating cell cultures of fetal rat telencephalon labeled on culture day 7 with a mixture of radioactive amino acid precursors. Cultures treated continuously with epidermal growth factor (EGF; 20 ng/ml) showed a generally increased protein secretion and a particularly enhanced production of a few distinct extracellular proteins. The time lag of this response after an initial dose of EGF (25 ng/ml) on day 7 was 48 h. The total macromolecular radioactivity that accumulated within 96 h of labeling in the media of EGF-treated cultures was 175% of untreated controls, whereas no difference was found in the proportions of intracellular amino acid incorporation. Cultures which received a single dose of EGF (25 ng/ml) on day 1 showed still a greatly increased protein secretion on day 7. Prevention of extracellular protein accumulation by reducing the initial cell number and increasing the rate of media changes did not affect the EGF-induced stimulation of the two glial enzymes, glutamine synthetase and 2',3'-cyclic nucleotide 3'-phosphohydrolase. The results suggest that both the increased production of extracellular proteins and the enhanced development of glial enzymatic activities reflect the stimulated phenotypic expression of EGF-sensitive brain cells.
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PMID:Epidermal growth factor (EGF) stimulation of cultured brain cells. II. Increased production of extracellular soluble proteins. 614 41

The involvement of voltage-gated calcium channels in the survival of immature CNS neurons was studied in aggregating brain cell cultures by examining cell type-specific effects of various channel blockers. Nifedipine (10 microM), a specific blocker of L-type calcium channels, caused a pronounced and irreversible decrease of glutamic acid decarboxylase activity, whereas the activity of choline acetyltransferase was significantly less affected. Flunarizine (1-10 microM, a relatively unspecific ion channel blocker) elicited similar effects, that were attenuated by NMDA. The glia-specific marker enzymes, glutamine synthetase and 2',3'-cyclic nucleotide 3'-phosphohydrolase, were affected only after treatment with high concentrations of nifedipine (50 microM) or NiCl2 (100 microM, shown to block T-type calcium channels). Nifedipine (50 microM), NiCl2 (100 microM), and flunarizine (5 microM) also caused a significant increase in the soluble nucleosome concentration, indicating increased apoptotic cell death. This effect was prevented by cycloheximide (1 microM). Furthermore, the combined treatment with calcicludine (10 nM, blocking L-type calcium channels) and funnel-web spider toxin-3.3 (100 nM, blocking T-type channels) also caused a significant increase in free nucleosomes as well as a decrease in glutamic acid decarboxylase activity. In contrast, cell viability was not affected by peptide blockers specific for N-, P-, and/or Q-type calcium channels. Highly differentiated cultures showed diminished susceptibility to nifedipine and flunarizine. The present data suggest that the survival of immature neurons, and particularly that of immature GABAergic neurons, requires the sustained entry of Ca2+ through voltage-gated calcium channels.
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PMID:High sensitivity of immature GABAergic neurons to blockers of voltage-gated calcium channels. 1036 97

The present study investigated whether 3-nitrotyrosine is an early marker for neurodegenerative processes involving oxidative stress. We characterized the 3-nitrotyrosine formation after 3-nitropropionic acid (3-NP) exposure in the whole brain spheroid culture model and in a rat model, using Lewis and Wistar rats. Increased 3-nitrotyrosine concentration in spheroid cultures from Lewis rats was observed at lower dose of and shorter exposure time to 3-NP as compared to alterations in glial fibrillary acidic protein concentration, decrease in glutamine synthetase activity or cell loss. Five days of exposure to 3-NP (5 mM) resulted in decreased staining of GABAergic processes, while neuronal nitric oxide synthase staining was preserved. In addition, staining of EAAC1, anti-2',3'-cyclic nucleotide 3'-phosphohydrolase and ED1 was diminished after treatment of spheroid cultures with 3-nitropropionic acid (5 mM), while isolectin B4 staining was increased. Dithiothreitol and vitamin E inhibited the increased formation of 3-nitrotyrosine. Interestingly, N(G)-nitro-L-arginine methyl ester increased the 3-nitrotyrosine formation. No increased 3-nitrotyrosine concentration was shown after exposure to 3-nitropropionic acid during 5 days in spheroid cultures obtained from Wistar rats. In the striatum of 3-NP-exposed Lewis and Wistar rats, no change in 3-nitrotyrosine concentration was observed, whereas only in Wistar rats the glial fibrillary acidic protein concentration was increased in addition to activation of microglial cells. It is concluded that 3-nitrotyrosine was a more sensitive marker for oxidative stress-induced neurodegeneration than glial fibrillary acidic protein and glutamine synthase in spheroid cell cultures of Lewis rats. Finally, the similarities between the 3-NP spheroid model and the vivo model indicate that the spheroid cultures provide a good alternative for chronic exposure of animals to neurotoxins.
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PMID:Evaluation of 3-nitrotyrosine as a marker for 3-nitropropionic acid-induced oxidative stress in Lewis and Wistar rats and strain-specific whole brain spheroid cultures. 1189 84

The effects of saikosaponins (a, b(1), b(2), c, d), isolated from Bupleurum Radix, on the induction of differentiation in rat C6 glioma cells were studied. Saikosaponins a and d were shown to inhibit cell proliferation and alter cell morphology. In addition to cytostasis, the enzymatic activities of glutamine synthetase (GS) and 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) were also noticeably increased after treatment with saikosaponin a. Nevertheless, saikosaponin d only showed an increase of GS activity, no significant changes in CNP activity were found. These results suggest that saikosaponin a can induce the differentiation of C6 glioma cells into astrocytes and/or oligodendrocytes, but saikosaponin d can only induce the differentiation of C6 glioma cells into astrocytes.
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PMID:Induction of differentiation in rat C6 glioma cells with Saikosaponins. 1193 11

As an extension of a previous validation study, the concentration-dependent effects of a series of anticonvulsant drugs were examined in aggregating cell cultures of foetal rat telencephalon. Cultures were treated either at an early (day 5 to day 14) or at an advanced (day 20 to day 28) developmental stage, and assayed for changes in the activities of the cell type-specific enzymes choline acetyltransferase (ChAT), acetylcholinesterase (AChE), glutamic acid decarboxylase (GAD), glutamine synthetase (GS) and 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP). Five drugs (carbamazepine, diazepam, phenobarbital, phenytoin and valproate), currently used in the treatment of epileptic patients, were tested together with losigamone, a recently developed anticonvulsant. The results show distinct, concentration-dependent patterns of biochemical changes for the different drugs. Phenytoin, carbamazepine, losigamone and diazepam greatly reduced GAD, ChAT and AChE activities, indicating a relatively high neuron-specific toxic potential. Diazepam produced a more general pattern of toxicity and, in contrast to the anticonvulsants, showed higher toxicity in less-differentiated cultures. Phenobarbital and valproate slightly but significantly increased the activities of several enzymes. The patterns of concentration-dependent effects observed in this three-dimensional cell culture system are in good agreement with the presumed neurotoxic and/or teratogenic potential of these drugs.
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PMID:Anticonvulsant drug toxicity in rat brain cell aggregate cultures. 2065 Jan 3


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