Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017638 (glioma)
 30,880 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The establishment of a new glioma cell line, DBTRG-05MG, in a modified RPMI 1640 medium is described. The cells were derived from an adult female with glioblastoma multiforme who had been treated with local brain irradiation and multidrug chemotherapy; the tumor showed substantial change in histologic appearance compared to the original biopsy 13 mo. previously. The line has been successfully cryopreserved and passaged up to 20 times. The karyotype of the cells demonstrated it as a hypotetraploid line; the DNA index of 1.9 confirmed the karyotype analyses. By immunocytochemical analysis, the cell line reacted with polyclonal antibodies to vimentin, S100, and neuron specific enolase, reflecting its primitive neuroectodermal character. Positive immunostaining for epidermal growth factor receptor correlated with the excess of chromosome 7 seen in the karyotype. The cell line reacted negatively to antibodies against platelet-derived growth factor and its receptor, neuronal cell adhesion molecule, and glial fibrillary acidic protein. By flow cytometry, the cells were major histocompatibility class I antigen positive and class I antigen negative. Growth kinetic studies demonstrated an approximate population doubling time of 34 to 41 h and a colony forming efficiency of 71.4%. Western blot analysis showed the presence of low levels of normal-sized retinoblastoma protein. When compared to the patient's lymphocyte DNA, no loss of heterozygosity of the p53 tumor suppressor gene was observed in the DBTRG-05MG cell line DNA.
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PMID:Characterization of a continuous human glioma cell line DBTRG-05MG: growth kinetics, karyotype, receptor expression, and tumor suppressor gene analyses. 133 Oct 21

The protein statin is found in nuclei of nonproliferating cells. Here we report that statin is a phosphoprotein, phosphorylated at serine residues in cultured cells. During immunoprecipitation with anti-statin (S44) antibody, a 45-kDa protein co-precipitates with the 57-kDa statin. In vitro kinase assays demonstrate that the S44 immunoprecipitates can phosphorylate, besides statin, immunoglobulins, enolase, and casein, at either serine or serine/threonine residues. Kinase assays with immunoprecipitated proteins performed on casein- or enolase-impregnated gels show that these substrates are phosphorylated by the 45-kDa (p45) protein. When the S44 immunoprecipitates from human cultured fibroblasts with different in vitro life-spans were compared, the p45 kinase activity was present only in young nongrowing and senescent cells, but not in young growing ones. In other cell cultures, the kinase is detected only in protein complexes precipitated from quiescent 3T3 cells, but not from cycling 3T3 cells or from transformed human glioma (U251-4) cells. Cell fractionation studies, indicating that the phosphorylating activity of S44 immunoprecipitates correlates both qualitatively and quantitatively with the amount of statin present, provide strong evidence that in vivo statin is specifically associated with the p45 kinase. These results suggest that the nonproliferation-specific nature of statin is indeed related to the phosphorylated property of this protein and maybe contributed by the associated kinase.
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PMID:Statin, a protein specifically present in nonproliferating cells, is a phosphoprotein and forms a complex with a 45-kilodalton serine/threonine kinase. 140 Apr 86

Three cell lines established from human gliomas were found to differ in the capacity to phosphorylate the glycolytic enzyme pyruvate kinase in vitro. Phosphorylation in the glioblastoma cell line U-138 was more pronounced than in the glioma cell line Hs 683 and in the glioblastoma cell line A-172. All 3 cell lines showed similar pyruvate kinase isozyme patterns and expressed about 90% K-type and 10% M-type subunits. So, differences in pyruvate kinase phosphorylation could not be explained by differences in the availability of the appropriate substrate, being pyruvate kinase type K. As in gliomas, phosphorylation could specifically and almost completely be inhibited by fructose-1,6-bisphosphate. In order to investigate a potential physiological significance of the phosphorylation of pyruvate kinase, we have characterized these cell lines for several glycolytic parameters. In U-138 cells, the production of lactate appeared to be 2 times higher as compared with A-172 and Hs 683 cells under normal growth conditions and even 4 times higher under low glucose culture regime. The efflux of lactate correlated with the pyruvate kinase phosphorylation pattern in the cell lines. In none of the cell lines could the lactate production be stimulated by glutamine as additional energy source under low glucose culture conditions. The higher glycolytic flux in U-138 cells was not accompanied by higher glycolytic enzyme activities. The isozyme patterns of hexokinase, pyruvate kinase, aldolase, enolase and lactate dehydrogenase in the cell lines were nearly identical and resembled the patterns previously described for solid gliomas. However, the isozyme composition of phosphofructokinase in the cell lines differed from the situation in gliomas. While in gliomas the expression of L-type phosphofructokinase is favored, in the glioma cell lines, we found an increase in the expression of C-type subunits.
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PMID:Phosphorylation of pyruvate kinase and glycolytic metabolism in three human glioma cell lines. 179 9

S-100 protein in clonal GA-1 and C6 rat glioma cell lines was released in serum-free medium supplemented with adrenocorticotropic hormone (ACTH). The induction of S-100 protein release by ACTH was dose-dependent, showing a half-maximal release at about 5 microM, and the S-100 protein concentration in the medium increased sharply within 3 min, but slightly during further incubation. The S-100 protein release was apparently accompanied by a decrease in the membrane-bound form of S-100 protein in the cell. The S-100 protein release was induced not by the ACTH1-24 fragment, which exhibits the known effects of ACTH, but by the ACTH18-39 fragment, which is designated as corticotropin-like intermediate-lobe peptide (CLIP). These results indicate that the C-terminal half of ACTH is responsible for the S-100 protein release. The enhancement of S-100 protein release by ACTH was also observed in normal rat glioblasts. The release induced by ACTH was apparently specific to S-100 protein, because little release of the cytoplasmic enzymes, creatine kinase, and enolase was observed under the same conditions. High concentrations (5 mM) of dibutyryl cyclic AMP or dibutyryl cyclic GMP were also found to induce S-100 protein release; however, catecholamines (epinephrine, norepinephrine, isoproterenol, and dopamine), acetylcholine, and glutamic acid did not enhance the release.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:S-100 protein in clonal astroglioma cells is released by adrenocorticotropic hormone and corticotropin-like intermediate-lobe peptide. 282 56

Human cell lines with neuronal and neuroendocrine features were examined for their expression of pp60c-src, the cellular homolog of the transforming gene product pp60v-src of Rous sarcoma virus. Four neuroblastoma (LA-N-5, SH-SY5Y, Paju, and SK-N-MC) and three small-cell lung carcinoma (U-2020, U-1690, and U-1285) cell lines were selected on the basis of their stage of neurocrine differentiation, as determined by the expression of neuron-specific enolase. In an immune complex protein kinase assay, all seven cell lines displayed c-src kinase activity which was considerably higher than that found in nonneurocrine cells (human diploid fibroblasts, glioma, and non-small cell lung carcinoma cell lines). Furthermore, the c-src kinase activity, as determined by autophosphorylation or phosphorylation of an exogenous substrate, enolase, correlated with the stage of neurocrine differentiation. There was an approximately 30-fold difference in c-src kinase autophosphorylation activity between the cell lines representing the highest and lowest stages of neurocrine differentiation. A similar variation was found in the steady-state levels of the c-src protein of these cell lines. Highly differentiated neuroblastoma cells expressed two forms of the src protein. Digestion by Staphylococcus aureus V8 protease did reveal structural diversity in the amino-terminal ends of these c-src molecules. In summary, we found a clear correlation between c-src kinase activity and the stage of neuronal and neuroendocrine differentiation. Thus, the phenotypic similarity between neurons and neuroendocrine cells includes high c-src expression.
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PMID:Expression of c-src in cultured human neuroblastoma and small-cell lung carcinoma cell lines correlates with neurocrine differentiation. 283 Apr 84

Two continuous human glioma-derived cell lines, UC-11MG and UC-302MG were established in our laboratory. Both cell lines persistently showed cytologic features similar to those of their respective original tumors. UC-11MG expressed glial fibrillary acidic protein (GFAP) and S-100 protein. The cell lines were negative for factor VIII related antigen (FVIII/RAg) and positive for fibronectin and neuronal specific enolase (NSE). Electron microscopic studies of UC-11MG revealed intermediate filament; filopodia and pinocytic vesicles were present in both lines. Dibutyryl cAMP (dB-cAMP) caused inhibition of growth and marked shift in the morphology of UC-302MG toward spindle cells. The cytologic appearance of UC-11MG treated with dB-cAMP was altered less, but cells showed a stronger GFAP expression, with 'cable' formation. Doubling time was 41.0 +/- 6.4 hours for UC-11MG and 43.7 +/- 6.6 hours for UC-302MG. The karyotypes of both cell lines were aneuploid with chromosomal derangement and markers characteristic for each line.
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PMID:Continuous human glioma-derived cell lines UC-11MG and UC-302MG. Morphologic, immunocytochemical and chromosomal characterization. 300 88

Neuron-specific gamma-enolase in human neurogenic tumors, including gliomas, transplanted gliomas, and permanent human glioma cell lines, was studied quantitatively, using newly established enzyme immunoassay methods, together with immunostaining of the tissue and cell preparations. A significantly high level of gamma-enolase was found in some glioblastomas, astrocytomas and oligodendrogliomas as well as medulloblastomas. Glioblastomas transplanted into mice and cultured cell lines derived from the same origins, as well as the permanent human glioma cell lines, also contained gamma-enolase, although the contents were low compared with findings in the original tumor tissues. Immunohistochemically, gamma-enolase stained intensely in the glioblastomatous cells. Serum gamma-enolase concentrations in some patients with gliomas and those of all the transplanted mice were enhanced. The serum gamma-enolase levels in the mice correlated well with size of the transplanted tumor tissues. These results indicate that neuron-specific gamma-enolase is produced in some neurogenic tumors of nonneuronal origin, therefore, serum gamma-enolase may be a useful biomarker for monitoring the extent of disease in patients with gliomas.
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PMID:Neuron-specific gamma-enolase derived from human glioma. 301 1

Calmodulin is present in higher concentrations in brain tissues. The content rapidly increased during the 2nd postnatal week in rat brain. Although the protein is ubiquitous in all eukaryotic cells, immunohistochemical studies have revealed that calmodulin is mainly localized in the neurons, exhibiting a similar distribution to that of gamma-type neuron-specific enolase. In the mouse retina, both calmodulin and gamma-enolase were found to be localized in optic nerves, ganglion cells, and inner and outer plexiform layers. The development study showed that gamma-enolase increased in the 2nd postnatal week and that the levels of calmodulin did not significantly change in that stage. In the mouse retina with an inherited retinal dysplasia (C3H), in which all the photoreceptor cells degenerate during the 2nd and 3rd postnatal weeks, calmodulin-specific staining decreased in the residual layers. Calmodulin is also enriched in mammalian testes. In the mouse testis, levels of calmodulin were high in the spermatocytes and in the spermatids, as compared to the level in spermatozoa. This suggests that the large amount of calmodulin in the testis may be associated with miotic divisions and/or spermatogenesis. Immunocytochemical staining of calmodulin in C6 glioma cells and PC12 pheochromocytoma cells showed a high level of calmodulin to be localized on the half spindles between poles and chromosomes in mitotic cells. The protein was also shown to be localized on fibrous structures in the interphase of those cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Calmodulin and neuron: immunohistochemical studies]. 307 1

For the determination of their possible utility as tumors markers, 2 neural-associated isozymes, neuron-specific enolase [(NSE) EC 4.2.1.11] and creatine kinase BB [(CK-BB) EC 2.7.3.2], were quantitated by radioimmunoassay in human neuroectodermal-derived cell lines, primary brain tumors, and sera and cerebrospinal fluid (CSF) from brain tumor patients. The NSE content of neuroblastoma cell lines was more than sixfold that of the glioma and medulloblastoma lines; the CK-BB content of neuroblastoma and medulloblastoma lines was fourfold to nineteen-fold that of the glioma and other lines. Expression of NSE in neuroblastoma cell lines was not related to time in culture and was cell line specific. NSE in ex vivo medulloblastomas was raised six to ten times that in astrocytomas and gliomas, although no significant differences were noted for the CK-BB content. Serum and CSF NSE levels were markedly raised above control values in 10 of 29 and 6 of 10 cases of astrocytoma, respectively. Raised CK-BB levels in serum (greater than 10 ng/ml) and CSF (greater than 12 ng/ml) were found in 9 of 18 and 2 of 10 patients, respectively. These data suggest that NSE is preferentially expressed by neuroblastoma lines and medulloblastomas and that NSE and CK-BB may have clinical utility as markers for prognosis, diagnosis, and monitoring of response to therapy.
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PMID:Differential expression of neural isozymes by human medulloblastomas and gliomas and neuroectodermal cell lines. 346 6

Distribution of three isoenzymes of brain enolase (2-phospho-D-glycerate hydro-lyase, EC 4.2.1.11) (alpha alpha, alpha gamma and gamma gamma forms) in clonal cell lines of neuroblastoma (NS20Y and N18TG-2), glioma (C6BU-1), and hybrid cells NG108-15, NCB20, Nbr10A, Nbr20A, N4G-B-a and N4G-C-a) was examined with a sensitive enzyme immunoassay system, that uses a rabbit antibody to rat brain enolase alpha alpha or gamma gamma. All cell lines tested were found to possess the enolase which contains gamma subunit (a neuron-specific protein), although the alpha alpha enolase (non-neuronal enolase) was the dominant from in these cells. A clonal rat glioma (C6BU-1) cell contained about 40, 1 and 0.07 microgram/mg protein of alpha alpha, alpha gamma and gamma gamma enolases, respectively, at the confluent stage. Inclusion of 1 mM dibutyryl cyclic AMP or 10 micrometers prostaglandin E1 plus 1 mM theophylline in the culture medium of a hybrid cell (NG108-15, mouse neuroblastoma x rat glioma) resulted in a more than 2-fold increase in the concentrations of alpha gamma and gamma gamma in the cell within a few days, with little change in the alpha alpha enolase concentration. A similar increase in the concentration of gamma subunit by the nucleotide (but not by prostaglandin E1 plus theophylline) was also observed in the glioma cell (C6BU-1) line. The results suggest that the gamma subunit or the neuron-specific protein can be regulated in NG108-15 and C6BU-1 cells in a cyclic AMP-dependent fashion.
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PMID:Regulation of neuron-specific enolase in NG108-15 hybrid cells and C6BU-1 glioma cells. 626 72


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