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Query: UMLS:C0017638 (glioma)
 30,880 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of three widely used glutaraldehyde-based fixatives on cellular volume and structure have been studied utilizing TEM, SEM, time-lapse micrography during the fixation procedure, volumetry and demonstration of the lysosomal enzyme acid phosphatase. The cells used were in vitro cultivated human glia and glioma cells and suspensions of isolated rat liver parenchymal cells. The fixatives compared were the following: 2 per cent glutaraldehyde (GA) in 0.1 M Na-cacodylate-HCL buffer (cac) with 0.1 M sucrose (pH 7.2); total osmolality (T) 510 mOsmol; vehicle osmolality (V) 300 mOsm, 2 per cent GA in 0.1 M cac (pH 7.2; T = 410 mOsmol; V = 200 mOsmol) and 1.5 per cent GA in 0.067 M cac with 0.033 M sucrose (pH 7.2; T = 320 mOsmol; V = 170 mOsmol). It was found that the fixative with a vehicle osmolality of 300 mOsmol gave results which were interpreted as ideal while the two fixatives were hypotonic vehicles resulted in changes which were easily demonstrated during volumetry, time-lapse micrography, SEM and cytochemistry. However, the differences observed in the TEM were less obvious and difficult to interpret, the major alternations being changes in the configuration of the ER in the liver cells. In conclusion, our findings show that even small variations in the composition of a glutaraldehyde fixative can result in structural changes which do not correspond to the functional morphology of a living cell. Such changes make correct interpretation of micrographs difficult.
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PMID:A comparison of the effects of three widely used glutaraldehyde fixatives on cellular volume and structure. A TEM, SEM, Volumetric and Cytochemical Study. 40 40

Using human and rat Glioma cell lines and mouse astrocytes prepared from newborn mice, lysosomal enzymatic activity, which is closely related with phagocytic activity, was assayed by spectrophotometric measurement of p-nitrophenol liberated from the relevant substrate. Lysosomal N-acetyl-beta-D-glucosaminidase and acid phosphatase activity was detected in neoplastic astrocytes at a level of enzymatic activity equal to that of monocyte/macrophage cell lines in certain glioma cells. From the implication of this data, it is suspected that astrocytes may function as phagocytic cells at inflammatory brain lesions.
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PMID:Lysosomal enzymic activity of astroglial cells. 154 50

Opioid receptor activity in neuroblastoma x glioma NG108-15 hybrid cell membranes was attenuated by acid phosphatase purified by high performance liquid chromatography and devoid of protease activity. Treatment of membranes with this phosphatase decreased opioid inhibition of adenylate cyclase and this effect was potentiated by the presence of the opioid agonist during the phosphatase treatment. Phosphatase treatment did not affect the number of opioid receptors but it did alter the distribution of receptors among affinity states, by increasing the percentage of receptors in the low affinity state. The similarities between these effects and desensitization of the opioid receptor, during chronic opioid treatment, are discussed.
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PMID:Modification of opioid receptor activity by acid phosphatase in neuroblastoma x glioma NG108-15 hybrid cells. 283 85

Gliomas were induced transplancentally by the administration of ethylnitrosourea to pregnant rats on the 15th day of gestation. The fine structure of neurones involved in these tumours was studied in order to assess the changes caused by neoplasia. The severity of the neuronal damage depended on their location, Those within the tumours being more affected than those in the neighbouring brain. The histological type and grade of malignancy also influenced the changes: periventricular pleomorphic gliomas and ependymomas of high-grade malignancy caused the most severe alterations. Neurones displayed a spectrum of appearances from apparent normality to complete necrosis. Both nucleus and cytoplasm were affected: of the cytoplasmic organelles the rough-surfaced endoplasmic reticulum and mitochondria showed the most striking changes. There were many lipofuscin granules and autophagic vacuoles. Axons underwent advanced degeneration: swollen mitochondria, disrupted vesicles and vacuoles, disintegrated microtubules, irregular filaments and unidentified debris were sometimes seen. Disintegration of myelin sheaths frequently occurred with consequent engulfing of their debris by macrophages and reacting astrocytes. The neuronal satellites--mainly oligodendrocytes--were often replaced by neoplastic glial cells. Hydrolytic 'marker' enzymes were demonstrated in neurones at various stages of degeneration. In all cases neurones displayed low acid phosphatase activity, while thiamine pyrophosphatase activity decreased with increasing neuronal degeneration.
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PMID:Neuronal changes in experimental gliomas. 610 64

A method for isolating plasma membranes based on the ability of cultured C6-glioma cells to phagocytize inert material such as polystyrene (latex) beads is described. The beads (phi 1.1 micron) were incubated for 16 h or 5 h. After several washings and homogenization of the cells, the beads with the surrounding membranes were isolated by use of a sucrose density gradient. The membranes were analyzed morphologically and biochemically. Morphological studies by means of light- and electron microscopy confirmed the intracellular localization of the beads. Enzymatic studies revealed that the specific activity of acid phosphatase decreased with shorter incubation periods (from 268.00 +/- 38.56 U X mg protein-1 X min-1 after 16 h to 125.12 +/- 9.10 after 5 h), whereas that of Na, K-ATPase showed the opposite trend (3.63 +/- 0.41 and 4.73 +/- 0.78 mumoles phosphate X mg protein-1 X h-1, respectively), indicating a lesser contamination with lysosomes. The main advantages of this procedure for membrane studies lie in purity and definite orientation ("inside-out") of the membranes.
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PMID:Isolation and characterization of internalized glioma cell membranes. 671 2

In the past, we transfected C6 glioma cells with connexin43 cDNA, resulting in a significant increase in connexin43 mRNA and protein, as well as reduced proliferation and tumorigenesis. To investigate the morphological aspects of increased connexin43 expression in these cells, we have used a combination of immunocytochemistry, cytochemistry, and electron microscopy. By confocal immunofluorescence microscopy, connexin43 protein was localized to the plasma membrane of transfected cells and extensive intracellular accumulations of connexin43 were also demonstrated. Freeze fracture preparations showed large aggregates of particles typical of mature gap junction plaques in the plasma membrane of these cells. Ultrastructural immunogold labeling with anti-connexin43 serum revealed that connexin43 protein was present in gap junctions in the plasma membrane, some of which were found in proximity to clathrin-coated pits. In addition, various intracellular membranous profiles were immunoreactive for connexin43, including annular profiles, some with fuzzy coats and some associated with lysosome-like structures. Enzyme cytochemistry revealed that these annular gap junction profiles were often associated with acid phosphatase-positive lysosomes. These studies on the intracellular localization of gap junction protein in connexin43-transfected cells are consistent with the functional expression of the transfected connexin43 cDNA and provide a useful model to study the pathways of gap junction assembly and degradation.
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PMID:Ultrastructural analysis of gap junctions in C6 glioma cells transfected with connexin43 cDNA. 838 23

Increased metabolic activity represented by an increase in both anabolism and catabolism in tumours, including gliomas, is a well known phenomenon and utilised in positron emission tomography imaging of tumours. In this study lysosomal enzyme activities of some glycohydrolases were investigated in glioma tissue from human brain. Tumour tissue (ten cases) and brain tissue surrounding the tumour tissue (seven cases) from patients with a histopathological diagnosis of glioblastoma multiforme or anaplastic astrocytoma were analysed for activity of the lysosomal enzymes galactosylceramidase, glucosylceramidase, beta-galactosidase, beta-N-acetyl-glucosaminidase, beta-glucuronidase and acid phosphatase. All of the investigated lysosomal enzymes except galactosylceramidase showed increased activity compared with that in normal brain tissue. Moreover, despite sparsity of tumour cells the specimens taken from surrounding areas showed elevated activities of the same enzymes. The findings indicate an upregulation of the activity not only in tumour but also in normal cells of the surrounding area.
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PMID:Increased activity of lysosomal glycohydrolases in glioma tissue and surrounding areas from human brain. 908 73

The box 1 and 2 motif of the myelin basic protein (MBP) promoter is a potential regulatory sequence of the MBP transcription unit. A DNA fragment that contained the sequence of the box 1 and 2 motif from mouse was synthesized, and its protein binding properties were examined by gel-shift assays. The box 1 and 2 probe and nuclear extracts from mouse brain generated a pattern of six major DNA-protein complexes (a, b, c, d, e, and f). The box 1 and 2 probe and nuclear extracts from oligodendrocyte-like glioma cells 1C10 generated a pattern of DNA-protein complexes that exhibited only complexes a, b, e, and f. Complex b generated by extracts from 1C10 cells, however, was very intense compared to any of the other complexes. It was determined that dephosphorylation of the proteins in nuclear extracts from 1C10 cells with acid phosphatase significantly altered their DNA binding properties. Two proteins of minimum M, approximately 32 and approximately 38 kDa (MBP32 and MBP38) that bind to the box 1 and 2 motif were identified in these nuclear extracts by using a UV crosslinking method. MBP32 and MBP38 are found in cell types and tissues known to express the golli transcription unit of the golli-MBP gene complex and may be involved in the modulation of the MBP unit in those cells.
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PMID:Two proteins bind to a novel motif in the promoter of the myelin basic protein gene from mouse. 929 31

We found that neuroblastoma x glioma hybrid NG108-15 cells accumulated lipofuscin-like autofluorescent materials during neuronal differentiation in culture in a medium containing 1% fetal calf serum, 1 mM dibutyryl cyclic AMP and 1 mM theophylline. The emission maximum of the lipofuscin-like autofluorescent materials was between 500 and 550 nm. Granules positive to acid phosphatase and periodic-acid Schiff were increased, as were the autofluorescent granules in NG108-15 cells. Thiolprotease inhibitors, N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucine-4-aminobutyla mide (E-64) and acetyl-Leu-Leu-Arg (leupeptin), markedly accelerated the accumulation of the lipofuscin-like autofluorescent materials in NG108-15 cells. On the other hand, activities of lysosomal thiolproteases, cathepsin B, C and L, were increased during neuronal differentiation. Protein content in the cells was gradually increased with the neuronal differentiation, and the rise was significantly accelerated when proteolysis was inhibited by E-64. These results suggest that the lipofuscin-like autofluorescent materials contain peptidic substances as a component, and indicate that the increase in hydrolytic activities of thiolproteases during neuronal differentiation is not enough for the hydrolysis of peptidic substrates, resulting in the accumulation of autofluorescent materials in NG108-15 cells.
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PMID:Formation of lipofuscin-like autofluorescent materials in NG108-15 cells: involvement of lysosomal protein degradation. 943 8

Brain fatty acid-binding protein (B-FABP) is expressed in the radial glial cells of the developing central nervous system as well as in a subset of human malignant glioma cell lines. Most of the malignant glioma lines that express B-FABP also express GFAP, an intermediate filament protein found in mature astrocytes. We are studying the regulation of the B-FABP gene to determine the basis for its differential expression in malignant glioma lines. By DNase I footprinting, we have identified five DNA-binding sites located within 400 base pairs (bp) of the B-FABP transcription start site, including two nuclear factor I (NFI)-binding sites at -35 to -58 bp (footprint 1, fp1) and -237 to -260 bp (fp3), respectively. Competition experiments, supershift experiments with anti-NFI antibody, and methylation interference experiments all indicate that the factor binding to fp1 and fp3 is NFI. By site-directed mutagenesis of both NFI-binding sites, we show that the most proximal NFI site is essential for B-FABP promoter activity in transiently transfected malignant glioma cells. Different band shift patterns are observed with nuclear extracts from B-FABP(+) and B-FABP(-) malignant glioma lines, with the latter generating complexes that migrate more slowly than those obtained with B-FABP(+) extracts. All bands are converted to a faster migrating form with potato acid phosphatase treatment, indicating that NFI is differentially phosphorylated in B-FABP(+) and B-FABP(-) lines. Our results suggest that B-FABP expression in malignant glioma lines is determined by the extent of NFI phosphorylation which, in turn, is controlled by a phosphatase activity specific to B-FABP(+) lines.
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PMID:Regulation of brain fatty acid-binding protein expression by differential phosphorylation of nuclear factor I in malignant glioma cell lines. 1089 61


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