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)

Fibroblast surface antigen (SFA) is a high molecular weight protein antigen, first shown on the surface of cultured fibroblasts in fibrillar structures. It is shed to the extracellular medium and also present in the circulation (serum and plasma). Fibroblasts transformed by tumor viruses produce SFA but do not retain it on cell surface. In this report we show that SFA is also present in cultured nonestablished astroglial cells. The glial and fibroblast SFAs are immunologically indistinguishable. Glial cells (three different nonestablished lines) contain more SFA per milligram cellular protein than fibroblasts. SFA was located on cell surface in fibrillar striae that frequently extended out from the cell body. Fluorescence was also found intracellularly in the cytoplasm. Malignant gliomas (astrocytomas) established to grow in culture from human tumor material produced SFA into the growth medium but had very little (lines U-105 MG and U-343 MG) or no detectable (lines U-118 MG, U-251 MG, and U-343 MG-a) cell surface SFA. In cultures of the glioma cells many cells, in particular those that appeared to be in the telophase stage, stained strongly positive for intracellular cytoplasmic SFA. These data demonstrate that similar to fibroblasts transformed experimentally by oncogenic viruses, cells grown from naturally occurring human tumors (glioblastomas) produce SFA but lose ability to retain it on cell surface.
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PMID:A common cell-type specific surface antigen in cultured human glial cells and fibroblasts: loss in malignant cells. 124 21

Monoclonal antibodies (mAbs) recognizing the disialoganglioside II3(NeuAc)2GgOse3Cer (GD2) were produced by immunizing mice with the GD2-expressing neuroblastoma cell line LAN-1 and a prefusion boost with purified GD2 coupled to Salmonella minnesota. Two IgM mAbs were isolated which demonstrated high levels of reactivity (binding ratios in excess of 100) with GD2 by solid-phase radioimmunoassay and positivity in high-performance thin-layer chromatography (HPTLC) immunostain; only one (DMAb-20) was subsequently shown by analysis with a panel of defined ganglioside species to be specific for the minimum epitope of GD2 GalNAc beta 1-4(NeuAc alpha 2-8-NeuAc alpha 2-3)Gal-, DMAb-20 was used to evaluate the expression of GD2 by malignant glioma and medulloblastoma cell lines using cell surface radioimmunoassay. indirect membrane immunofluorescence. HPTLC immunostain, and densitometric analysis of extracted gangliosides from selected cell lines. Sixteen of 20 (80%) malignant glioma and 5 of 5 medulloblastoma cell lines reacted with DMAb-20; in agreement with previous studies, 5 of 5 neuroblastoma and 2 of 3 melanoma cell lines also reacted with DMAb-20, GD2 was proportionally increased in the glioma and medulloblastoma cell lines relative to levels in normal brain, as determined by densitometric analysis. In a phenotypic survey of malignant glioma biopsies, tumor cells in 24 of 30 (80%) cases stained positively with DMAb-20. Reactive astrocytes, both within the adjacent to tumors, were frequently intensely stained. Among the morphological variants of glioblastoma examined, the most intense staining with DMAb-20 was observed in neoplastic gemistocytes, with the weakest or absent staining in small cell glioblastomas. As GD2 is a commonly expressed surface antigen of gliomas and medulloblastomas, expression of which is retained in tissue culture. DMAb-20 will be useful in determining the functional role of GD2 in cell-cell interaction, adhesion, and invasion, and in defining altered growth control mechanisms of central nervous system neoplasms in in vitro models.
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PMID:Disialoganglioside GD2 in human neuroectodermal tumor cell lines and gliomas. 165 6

Two monoclonal antibodies (mAb), termed ED6 and LD6, were obtained by immunizing mice with cytotoxic T cell lines expressing the T cell receptor (TcR) gamma/delta. These mAb were selected according to their ability to trigger the cytolytic program of the immunizing cell lines in a redirected killing assay. Both mAb recognized molecule(s) expressed on the surface of most long-term cultured TcR gamma/delta +, TcR alpha/beta + and CD3-CD16+ lymphocytes, while it was absent on resting peripheral blood lymphocytes. In addition both mAb reacted with neoplastic B cell lines, Epstein-Barr virus-transformed B cell lines, small cell lung cancer and glioma cell lines, while no surface reactivity was detected on ovarian, breast, colon and non-small cell lung cancer lines. The functional activity of these mAb was studied by two cytolytic assays. Both mAb were able to trigger the cytolytic program of CD3+TcR gamma/delta + polyclonal cell lines and of a CD3-CD16+ NK cell clone against the murine mastocytoma target cell line P815 (Fc receptor+) in a 4-h 51Cr-release assay. In addition, ED6 and LD6 hybridomas were lysed by TcR gamma/delta + effector cells while other hybridomas (obtained from the same fusion) were not lysed. ED6 and LD6 mAb (in the presence of submitogenic doses of the phorbol 12-myristate 13-acetate) also induced the secretion of interleukin 2 by ED6/LD6+ T cell clones expressing TcR gamma/delta or alpha/beta. mAb-induced surface antigen modulation experiments showed that the antigenic determinant recognized by ED6 and LD6 co-modulated, thus indicating that the two mAb probably recognize the same or closely associated molecules. The molecular characteristics of the antigen recognized by the mAb were investigated by Western blot analysis. The LD6 mAb recognized a major band of approximately 65 kDa, both under nonreducing and reducing conditions. These data indicate that ED6 and LD6 mAb recognize a novel non-lineage-specific activation antigen which is involved in the induction of the functional program of long-term cultured T or natural killer cells.
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PMID:A novel surface molecule expressed by long-term cultured T and natural killer cells is involved in cell activation. 183 83

A murine monoclonal antibody designated as MAb 3H9 (IgG1 subclass immunoglobulin, kappa light chain) expressed specific antibody binding activity to a human brain malignant glioma cell line (GBM8401/TSGH,NDMC) and many formalin-fixed and paraffin-embedded malignant gliomas that have been produced in our laboratory by hybridoma technology. The immunohistochemical indirect immunofluorescence, peroxidase-antiperoxidase assays, and specific electron microscopic immunogold staining revealed that 3H9 probably recognized a distinct glioma-associated surface antigen on the GBM8401 cultured cells. In vivo radioimmunolocalization of GBM8401 xenografts in nude mice by external scintigraphy with radiolabeled 3H9 has been performed to evaluate potential clinical application as diagnostic or therapeutic reagents. On the 3rd day after an intravenous injection of 15 microCi, the 125I- or 131I-radiolabeled 3H9 was successful in immunolocalization of a human brain GBM8401 xenograft in the nude mouse. In large xenografts, the radioactivity ratios of tumor to brain and tumor to blood were 11.0 and 2.4, respectively. In small xenografts, the tumor to brain and tumor to blood ratios were 14.0 and 2.9, respectively. The clearance of radiolabeled 3H9 in the bloodstream of the nude mouse was not affected by the presence of a GBM8401 xenograft. This preliminary experiment reveals that human brain GBM8401 xenografts in nude mice can be detected in vivo by radiolabeled 3H9.
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PMID:Tumor localization of human brain malignant glioma xenograft in nude mice with a radiolabeled monoclonal antibody. 232 Feb 6

Monoclonal antibody (MCA) G-22 is directed against a human glioma-associated surface antigen. Its availability for the radioimmunodetection of human glioma was analyzed by utilizing the xenografts in athymic mice. Nude mice with subcutaneous grafts of U251-MG or U251-SP glioma received intravenous administration of 123I or 131I labeled F(ab')2 fragment or whole immunoglobulin. Results of radioimaging revealed that 123I-labeled antibody was better than the 131I-labeled. It was also noted that administration of 123I-labeled F(ab')2 fragment of G-22 MCA enabled the imaging of human glioma xenografts weighing 80-650 mg after 48 hours. When biodistribution of 123I MCA was compared between G-22 and control antibodies, the percentages of dose/g in tumors were 5.228-1.799 at 30 hours and 4.112-1.132 at 48 hours with G-22 and they were 4.164-1.248 and 0.314-0.142 with control. The tumor/blood ratio until 72 hours after injection was constantly above 1 with G-22 and less than 1 with control antibody. These results indicate the potential usefulness of G-22 MCA for the radioimmunodetection of human gliomas.
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PMID:Radioimaging of human glioma xenografts with 123I labeled monoclonal antibody G-22 against glioma-associated antigen. 235 55

A limiting dilution analysis (LDA) was used to assess the functional profiles of tumor-infiltrating lymphocytes (TIL) recovered from 15 human solid tumors. The microculture system applied in this study has been shown to allow virtually all normal peripheral blood T lymphocytes (PBL-T) to undergo clonal proliferation and was applied to obtain estimates of the frequency of both proliferating and cytolytic cells among the TIL population. A total of 624 microcultures proliferating in the presence of irradiated allogeneic spleen cells and interleukin 2 (IL 2) were expanded for clonal analysis. These TIL microcultures were assessed for surface antigen phenotype, IL 2 production (helper function) and for their cytolytic capabilities against the human erythroleukemic line K562 (natural killer (NK)-like activity) and P815, a mouse mastocytoma line, in the presence of phytohemagglutinin (PHA), i.e., lectin-dependent cell cytotoxicity (LDCC) which allows the detection of cytolytic activity irrespective of the antigenic specificity of the effector cells. Whenever feasible, cytolytic activity against autologous and allogeneic tumor cells was tested. LDA first demonstrated that the proliferative potential was decreased in T lymphocytes infiltrating human solid tumors (approximately 1 in 50 to 1 in 2 proliferating T lymphocyte precursors (PTL-P) in this series) as compared to normal PBL-T (1 in 2 to 1 in 1 PTL-P). The growth pattern in the titration cultures showed a remarkable agreement with the single-hit Poisson model implying that third party cells are unlikely to be involved in the reduced proliferative potential. Quantitative estimates of functional precursors showed that, in spite of reduced proliferative potential, cytolytic T lymphocyte precursors (CTL-P) against unknown antigens (LDCC-reactive) accounted for a considerable part of the microcultures in many cases. The precursor frequency of T lymphocytes with NK-like activity was usually low in situ (with the exception of glioma), whereas it was in the normal range in the patient's autologous PBL-T. In four evaluable cases, quantitative assessment showed that 1 in 200 to 1 in 1000 T lymphocytes from TIL was cytolytic against allogeneic tumor cells, which is in the range of alloreactive cytolytic T lymphocytes (CTL) generated in the mixed lymphocyte culture from normal PBL. Cytolytic activity against autologous target cells could not be quantitatively estimated but out of 88 clones from 4 patients, 3 clones originating from 2 glioma patients showed high lytic values against autologous tumor.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Clonal and frequency analyses of tumor-infiltrating T lymphocytes from human solid tumors. 310 80

Transforming growth factor-beta (TGF-beta) is known to have a potent inhibitory influence on several immune functions. It has recently been demonstrated that TGF-beta 2 is identical to the glioblastoma-derived T cell suppressor factor (G-TsF). In the present study, human malignant glioma cell lines were incubated with various concentrations of TGF-beta 2. An optimal concentration of 1 ng/ml TGF-beta 2 produced a partial but significant decrease of HLA-DR (class II) surface antigen expression on glioma cells expressing this antigen, as well as decreased levels of HLA-DR-specific mRNA. The surface expression of other HLA-related molecules, such as HLA-ABC (class I) and beta 2-microglobulin, was not influenced by TGF-beta 2. The suppressive effect of TGF-beta 2 on HLA-DR expression, both at the surface antigenic and cytoplasmic mRNA levels, could be completely overcome by adding relatively high concentrations (500 U/ml) of interferon (IFN)-gamma to the culture system. However, TGF-beta 2 inhibited the enhancement of HLA-DR surface expression produced by low concentrations of IFN-gamma on some cells which initially did not express these antigens. These results show that TGF-beta 2 can act as a regulator of HLA-DR antigen expression on human glioma cells.
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PMID:Transforming growth factor-beta 2 down-regulates HLA-DR antigen expression on human malignant glioma cells. 314 81

We prepared mouse monoclonal antibody (Mab S-11E10) for the surface antigen specifically distributed in ruffling membranes and filopodia of cultured human glioma cells. The antibody reacted to the specified structures of other glioma cells (U251MG, KNS 60) as well as those of KNS 42 cells, which were the immunizing source. The antigens, identified by Mab S-11E10, had molecular weights of 65 and 66 kDa. Immunohistochemically, the antibody reacted only to astrocytes in the human brain, but the cross-reactivity was noted in extraneural tissues such as lymphocytes and epithelium of the bowel ducts. In 5 out of 6 low grade astrocytomas, most of the tumor cells were strongly stained, while tumor cells of highly cellular areas of anaplastic astrocytomas and glioblastomas were either not stained or only weakly stained. The specific localization of 65-66 kDa doublet proteins may suggest relation to spreading and locomotion of cells, and may correlate to astrocytic differentiation and/or function.
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PMID:Surface proteins localized in ruffling membranes and filopodia of human glioma cells detected using Mab S-11E10. 330 22

It has been reported that human neuroblastoma lines are almost devoid of class I transplantation antigens, while human glioma lines express these antigens. Other studies have also shown a paucity of class I antigens on the murine neuroblastoma line N2A, and the expression of these antigens by the murine ependymoblastoma G26 lines. Such differences might represent heterogeneity in class I antigen expression by different brain cell types, and the importance of this to the immunology of the brain prompted us to re-examine class I expression by these cell lines in more detail. Using an exhaustive number of approaches, we were not able to detect significant differences in class I surface antigen expression between N2A and the G26 lines. We compared the murine neuroblastoma line Cl300 and its cloned derivative, N2A, to the lines G26-20 and G26-24. Antibody-dependent, complement-mediated cytotoxicity revealed detectable levels of both K and D region antigens on these lines. Immunocytofluorometric analysis further confirmed that these lines express high levels of class I antigens, although due to their large sizes, the surface densities of class I antigens on these cells are lower than splenocytes. This lower density of class I molecules did not impede the capacity of either the neuroblastoma or the G26 lines to serve as targets of H-2K- or D-specific T effectors. Finally, comparison of these two cell types for class I RNA transcripts also revealed no difference. Thus, our findings which are the most detailed study of these lines are drastically different from findings in humans as well as earlier findings in the murine system. Likely explanations are discussed and precautions are given for the study of class I antigen expression by these lines.
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PMID:The expression and detection of MHC class I antigens on murine neuroblastoma and ependymoblastoma lines. 349 12

Monoclonal antibody 217c binds to a tumor-associated surface antigen of transformed rat glial cells. Treatment of C6 glioma cells with 2.5% 1-butanol yielded an extract which was active in competitive inhibition of antibody 217c to cell monolayers in an 125l-protein A assay as well as in binding antibody 217c in an enzyme-linked immunodot assay. The antigen, however, was not released in soluble form, but in a particulate fraction which could be pelleted by ultracentrifugation for 2 h at 120,000 X g. Antibody binding activity in the immunodot assay could be destroyed by heating the extract to 100 degrees C for 10 min. To determine the molecular weight of the antigenic polypeptide, cell monolayer cultures were surface radioiodinated and extracted with Nonidet P-40. Immobilized antibody 217c bound only a single labeled polypeptide with a molecular weight of 64,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This surface peptide was present in the C6 glioma line as well as in oligodendrocyte and astrocyte cultures transformed either spontaneously or using ethylnitrosourea. It was absent from normal astrocyte and oligodendrocyte cultures of neonatal rat brain. In the glial lines studied the P-64 peptide appears as a surface marker indicating malignant transformation.
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PMID:Immunoprecipitation of a Mr 64,000 glial tumor-associated antigen by monoclonal antibody 217c. 394 Jun 49


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