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 imaging characteristics of monoclonal antibody SZ39 against glioma were evaluated in glioma-bearing nude mice. Monoclonal antibody SZ39 is a murine IgG2a that reacts with a glycoprotein epitope (molecular weight 180,000), a human glioma-associated membrane antigen. Monoclonal antibody SZ39 was labeled with 131I using a modified chloramine T method. Each glioma-bearing nude mouse was given 50 microCi/40 micrograms of the experimental agent, 131I-labeled monoclonal antibody, or 50 microCi/46 micrograms of a control agent, 131I-labeled monoclonal antibody C50, an antibody against colon cancer. Single-photon emission computed tomography (SPECT) was performed every 24 hours in the first week after administration. Glioma-bearing nude mice were killed in groups of 3 at 24 hours and daily up to 72 hours. The ratio of radioactivity uptake in glioma to normal organs was calculated. After administration of the labeled SZ39, glioma was visualized with SPECT on days 1 to 7, particularly at 72 hours. There was no accumulation of radioactivity in glioma with the labeled C50 antibody. All glioma-organ ratios increased with time. At 72 hours, the ratio of glioma to brain was 22.46 and of the other organs was 2.64 on average. SZ39 had a relatively low endocytosis rate and was favorable for 131I labeling. These characteristics were helpful to reduce free 131I in the blood and reduce the uptake by other organs. The results suggest that 131I-labeled SZ39 selectively accumulates in glioma, representing a potential strategy for SPECT imaging of these lesions.
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PMID:Preclinical evaluation of SPECT imaging with 131I-labeled monoclonal antibody SZ39 in nude mice bearing human glioma xenografts. 863 89

The expression of CMP-NeuAc: Gal beta 1,4GlcNAc alpha 2,6 sialyltransferase (alpha 2,6-ST) [EC 2.4.99.1] and glycoproteins bearing alpha 2,6-linked sialic acids were examined in primary human brain tumours and cell lines. 79% (19/24) of the meningiomas expressed alpha 2,6-ST mRNA, 42% (10/24) of which showed very high expression. alpha 2,6-ST mRNA expression was undetectable in normal brain tissue. In contrast, only 1/13 of the gliomas examined expressed detectable alpha 2,6-ST mRNA. Metastases to the brain did not express measurable amounts of alpha 2,6-ST mRNA. Less expression was found in malignant (i.e. anaplastic) compared to benign (i.e. meningothelial) meningiomas. Two-dimensional SDS-PAGE of glioma and meningioma proteins, followed by Sambucus nigra lectin staining, revealed the presence of a glycoprotein bearing alpha 2,6-linked sialic acids, M(r) = 53 kDa and a pI = 7.0 (MEN-1) that appeared in all seven of the meningiomas examined, but was expressed at barely detectable levels, if at all, in seven out of the seven glioblastomas examined. Thus, decreased alpha 2,6-ST expression may play a role in the aggressive nature of anaplastic meningiomas, but appears to be virtually absent in all tumours of glial origin.
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PMID:The expression of CMP-NeuAc: Gal beta 1,4GlcNAc alpha 2,6 sialyltransferase [EC 2.4.99.1] and glycoproteins bearing alpha 2,6-linked sialic acids in human brain tumours. 874 63

When treated with retinoic acid in vivo, C6 glioma cells show an enhancement of CMP-Neu5Ac:Gal beta 1-3 GalNAc-R alpha-2,3 sialyltransferase activity. A 300 kDa glycoprotein was detected by lectin affinoblotting in retinoic acid-treated C6 cells which stained weakly or not at all in control cells. Comparative studies with different lectins demonstrated that this glycoprotein contains alpha 2,3 Neu5Ac Gal-GalNAc O-glycan moieties. Cultures in the presence of an inhibitor of O-glycan synthesis (N-acetylgalactosaminide alpha-O-benzyl) demonstrated that enhancement of staining of the 300 kDa glycoprotein was not due to the increase of the alpha 2,3 sialytransferase but to the de novo synthesis of the polypeptide chain of this glycoprotein.
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PMID:Study of O-sialylation of glycoproteins in C6 glioma cells treated with retinoic acid. 878 91

In the immune system, mCD24, the mouse homolog of the human glycosyl phosphatidylinositol-anchored glycoprotein CD24, may play a role in cell adhesion. In the nervous system, the function of mCD24 has not been determined, but its transient expression by neurons suggests that it may be involved in axon growth in development. Here we show that retinal ganglion cells (RGCs) and dorsal root ganglion (DRG) neurons express mCD24 in the developing but not adult mouse in vivo and in DRG neurons of the injured adult peripheral nervous system (PNS). In vitro, mCD24 was expressed by immature neurons and by a subpopulation of adult DRG neurons. To analyze the possible function of mCD24 in the nervous system, we prepared rat C6 glioma cells stably transfected or retrovirally infected with mCD24 cDNA. The cells did not exhibit changes in their adhesive properties or cell division rate after transfection or infection. When mCD24-expressing cells were used as monolayer substrates for culturing RGCs and DRG neurons, neurite outgrowth was inhibited, depending on neuronal age and on the relative levels of mCD24 in the monolayer. This inhibition, however, was not dependent on the expression of mCD24 by the neurons themselves, because DRG neurons of a mouse deleted of the mCD24 gene showed the same response. These results show that mCD24 interacts in a heterophilic manner with a developmentally regulated molecule expressed by neurons, and they suggest that in vivo, mCD24 may inhibit the further extension or collateral branching of axons in late embryonic development.
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PMID:mCD24, a glycoprotein transiently expressed by neurons, is an inhibitor of neurite outgrowth. 878 38

104 N2-frozen samples from 33 astrocytic tumors previously untreated with cytotoxic drugs have been analyzed for the expression of p-glycoprotein transcripts (mdrl) by RT-PCR using beta2-microglobulin as an internal control. A remarkable variation was observed even within a single tumor in 50% of the cases. Nevertheless, a difference became visible between the groups of anaplastic astrocytomas and glioblastomas. While 78% of the grade 3 astrocytomas contained at least a minimum of 1 sample with a very low mdr1 expression, this was the case only in 23% of the glioblastomas. This supports an earlier observation revealing a positive correlation between tumor grading and the tumor cell fraction stained with the monoclonal antibody JSB1. On the other hand, no major differences were found between the histological groups when the samples with the highest mdr1 expression were selected to represent the individual tumors. Those samples are less informative. They might be derived from tumor regions in which capillaries deliver a larger fraction of the total mRNA pool. No induction of mdr1 was observed in some early astrocytoma or glioblastoma cell cultures even after administration of high concentrations of the drugs ACNU and VM26, often used in glioma therapy.
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PMID:Mdr1 mRNA expression differs between grade III astrocytomas and glioblastomas. 902 Mar 93

Tenascin (TN) is an extracellular matrix glycoprotein that is expressed in a characteristic spatiotemporal pattern during development and is up-regulated in the adult during tumorigenesis, wound healing, and nerve regeneration. In previous studies, we identified a promoter within the proximal 250 bp upstream of the mouse TN gene that contains several putative regulatory elements that are conserved among vertebrate TN genes. We have identified four different DNA elements within this promoter and show that they contribute in different ways to TN gene expression in NIH 3T3 fibroblasts, C6 glioma cells, and N2A neuroblastoma cells. These elements comprise a binding site for Krox proteins, one for nuclear factor 1, an octamer motif that binds POU-homeodomain proteins, and a novel TN control element. The nuclear factor 1 and TN control element had positive effects on TN promoter activity and formed similar DNA-protein complexes with nuclear extracts from all three cell lines. The Krox element had a negative effect on TN promoter activity in N2A cells, a positive effect in C6 cells, and no effect in NIH 3T3 cells. Two DNA binding complexes, one correlated with the negative and the other with the positive activities of the Krox element, were found to contain the protein Krox24. In cotransfection experiments, the octamer motif was required for induction of TN promoter activity by the POU-homeodomain protein Brn2 in N2A cells but was inactive in C6 cells. Consistent with these findings, N2A cells transfected with Brn2 formed octamer-binding complexes containing N-Oct3, the transcriptionally active form of Brn2, whereas complexes formed in C6 cells contained only N-Oct5A and N-Oct5B. Our results provide a striking example of the diversity of regulatory mechanisms that can be called forth by combining different promoter motifs with transcriptional activators or repressors.
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PMID:Multiple promoter elements differentially regulate the expression of the mouse tenascin gene. 905 Aug 67

Laminin is a major glycoprotein specific to basement membranes. Hepatocellular carcinoma tissue synthesize and secrete abundant laminin. By DNA-protein interaction assays, we have identified nuclear factors specific to hepatocellular carcinoma cells. The comparison of nuclear factor binding by Southwestern analysis with B1 and B2 laminin promoters revealed different patterns of nuclear factor binding in different cells types. In hepatocellular carcinoma, HepG2 cells, a specific pair of proteins (P105 and P98) consisting of 105 and 98 kDa were identified as common nuclear factors for both B1 and B2 laminin promoters, while in completely diverse human glioma cells (U251), various different and greater number of nuclear proteins ranging from 212 to 68 kDa were detected to interact separately with laminin B1 and B2 genes.
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PMID:Hepatocellular carcinoma cell type specific interaction of P105 and P98 nuclear factors with laminin B1 and B2 genes. 905 41

CMP-NeuAc: Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase (alpha2,3-ST) mRNA was expressed in human glioma specimens, human fetal astrocytes, and a panel of brain tumor cell lines. Maackia amurensis agglutinin staining revealed the presence of alpha2,3-linked sialic acids on glioma cell surfaces and extracellular matrices whereas normal human adult astrocytes were negative. Increased expression of alpha2,3-linked glycoprotein sialylation may play a role in glial tumorigenesis.
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PMID:alpha2,3-sialyltransferase mRNA and alpha2,3-linked glycoprotein sialylation are increased in malignant gliomas. 916 57

Expression of tenascin, an extracellular matrix glycoprotein, was measured in glioma cell lines using a newly established enzyme immunoassay. Secreted tenascin was found at concentrations greater than 800 ng/ml in eight of 14 glioma, three small cell lung carcinoma, two melanoma, and one sarcoma cell lines. The remaining six glioma and other carcinoma cell lines, and cell lines originating from normal tissues demonstrated low levels or no secretion into the supernatant. The glioma cell line, U-251-MG nu/nu, which has almost 100% transplantability in nude mice, had the highest expression level of tenascin among the glioma cell lines examined. Even low secretor glioma cell lines released high concentrations of tenascin, detectable by assaying the NP-40 solubilized cell lysates. Flow cytometric analysis revealed that tenascin was located on both the cell surface and primarily in the cytoplasm of glioma cells. When the glioma cell lines were exposed to tumor necrosis factor-alpha (TNF-alpha), levels of secreted tenascin increased between 36% and 380%, whereas transforming growth factor-beta induced only minimal changes. These results suggest that glioma cell lines may be classified according to the degree of tenascin secretion/expression: high secretor type, low secretor type, and non-expressing type. The increase in tenascin secretion by TNF-alpha suggests that the expression of tenascin in glioma growth and development may be mediated through a cytokine network.
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PMID:Enzyme immunoassay of glioma cell tenascin secretion and augmentation by tumor necrosis factor-alpha. 918 37

The Na,K-ATPase belongs to a family of P-type ion-translocating ATPases sharing homologous catalytic subunits (alpha) that traverse the membrane several times and contain the binding sites for ATP and cations. In this family, only Na,K- and H,K-ATPases have been shown to have a second subunit, a single-span glycoprotein called beta. Recently a new isoform (beta3) has been identified in mammals. Here we describe structural features and tissue distribution of the beta3 protein, utilizing an antiserum specific for its N terminus. beta3 was the only beta detected in Na,K-ATPase purified from C6 glioma. Treatment with N-glycosidase F confirmed that beta3 is a glycoprotein containing N-linked carbohydrate chains. Molecular masses of the glycosylated protein and core protein were estimated to be 42 and 35 kDa, respectively, which are different from those of the beta1 and beta2 subunits. Detection of beta subunits has historically been difficult in certain tissues. Sensitivity was improved by deglycosylating, and expression was evaluated by obtaining estimates of beta3/alpha ratio. The proportion of beta3 protein in the rat was highest in lung and testis. It was also present in liver and skeletal muscle, whereas kidney, heart, and brain contained it only as a minor component of the Na,K-ATPase. In P7 rat, we found skeletal muscle and lung Na,K-ATPase to be the most enriched in beta3 subunit, whereas expression in liver was very low, illustrating developmentally regulated changes in expression. The substantial expression in lung and adult liver very likely explains long-standing puzzles about an apparent paucity of beta subunit in membranes or in discrete cellular or subcellular structures.
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PMID:Tissue-specific expression of the Na,K-ATPase beta3 subunit. The presence of beta3 in lung and liver addresses the problem of the missing subunit. 927 90


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