Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017636 (glioblastoma)
 18,345 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cholera toxin was coupled to peroxidase to yield a highly specific marker for GM1 gangliosides. Study of embryonic brain cells in culture revealed intense binding of cholera-peroxidase by plasma membranes of both neurons and glial cells. In contrast, long-term monolayer glioblastoma cultures, including one producing C-type virus, revealed virtually no labelling of their plasma membranes. Such cells were shown to be capable of incorporating exogenously applied GM1 into their plasma membranes. Studies with fixed brain and synaptosomal fractions were in accord with results on embryonic brain cells in culture, and autoradiographic findings with 125I cholera supported observations made utilizing cholera-peroxidase. From our studies there is some indication that long-term propagation in vitro alters the plasma membrane GM1.
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PMID:Ultrastructural study of plasma membrane GM1 in neuroectodermal cells using cholera-peroxidase. 97 33

Using the monoclonal antibody Ki-67, proliferating cells were demonstrated immunohistochemically in 16 tumors of the nervous system in children, and these findings compared with those in 44 adult tumors. The antibody, which reacts with a nuclear protein expressed during the G1, S, G2, and M phases of the cell cycle, was demonstrated in frozen (13 cases) or smear (3 cases) sections using the peroxidase-antiperoxidase method. The percentage of stained tumor cells in children was in general agreement with the histological grade, ranging from 0.2% in a schwannoma to 12.4% in a juvenile type of glioblastoma. In a medulloblastoma, the fraction of labeled nuclei was 10.2%. In malignant gliomas of children, the percentage of stained cells did not differ from that in adult tumors. However, some cases demonstrated an unusually higher number of positive cells associated with higher cellularity than did adult tumors; this is in agreement with the content of small immature tumor cells in many pediatric tumors. The use of Ki-67 staining could become an important additional criterion for predicting the biologic behavior of nervous system neoplasms in children.
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PMID:The use of the monoclonal antibody Ki-67 in determination of the growth fraction in pediatric brain tumors. 245 70

Morphological changes of the basement membrane associated with endothelial proliferation in astrocytic tumors are studied in this report. Laminin is known to be a specific glycoprotein of basement membranes. We applied this characteristic of laminin to enable us to observe various characteristics of the basement membrane. The presence of laminin in 13 glioblastomas, 15 anaplastic astrocytomas, 7 astrocytomas, and 6 pilocytic astrocytomas was examined by peroxidase-antiperoxidase (PAP) staining of formalin-fixed and paraffin-embedded surgical specimens. White matter from five normal cerebral hemispheres obtained during autopsy and subsequently embedded using the same method, were used as a control. Laminin was observed at the glioma-mesenchymal junction in astrocytic tumors, and the deposits of laminin made the tumor vasculature come into intense relief. The destructive changes of the basement membrane, including disruption, thickening, disconnection, dissociation, winding, and conjunction, became greater with progressive endothelial proliferation in astrocytic tumors. Those changes were seen to be most remarkable in glioblastoma. In addition, there was a marked variety of morphological change in the basement membrane in different areas of glioblastomas, although the changes were almost constant in other astrocytic tumors. We present a schematic hypothesis of the stages of angiogenesis in glioblastoma based on the above morphological changes of the basement membrane and discuss it in this report.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Morphological changes in basement membrane associated with endothelial proliferation in astrocytic tumors--an immunohistochemical study of laminin]. 247 10

We examined the cellular distribution of lipocortin-1 (L-1), a major physiologic substrate for the epidermal growth factor receptor/kinase, in 122 central nervous system (CNS) and peripheral nervous system (PNS) neoplasms using the peroxidase-antiperoxidase technique with a polyclonal antibody specific for L-1. Extensive L-1 immunoreactivity was demonstrated in many CNS tumors; in 11 of 21 glioblastoma multiformes, in five of 12 anaplastic astrocytomas, and in five of 14 astrocytomas. Significant numbers of immunoreactive ependymocytes or astrocytes were also seen in six of 13 ependymomas. In contrast, no immunostaining was detected in the oligodendrocytes in any of ten oligodendrogliomas. PNS tumors, found in two of five malignant nerve sheath tumors, 13 of 15 schwannomas, 13 of 17 neurofibromas, and 14 of 15 traumatic neuromas, also contained considerable L-1 immunoreactivity in Schwann cells or mast cells. These findings raise the possibility that L-1 may participate in the proliferation or subsequent differentiation of neoplastic astrocytes, ependymocytes, and Schwann cells.
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PMID:Lipocortin-1 immunoreactivity in central and peripheral nervous system glial tumors. 252 74

Binding of type C neurotoxin (C1 toxin) from Clostridium botulinum (strain Stockholm) to neuroblastoma cell lines was studied by using biotinylated anti-toxin antibody and avidin-biotinylated peroxidase complex. The neurotoxin bound with high efficiency to mouse neuroblastoma (NS-20Y and NIE-115) cells and to hybridomas of rat glioblastoma and mouse neuroblastoma (NG108-C15) cells. The toxin bound little to human neuroblastoma, rat astrocytoma, and nonneural cell lines. Binding of the neurotoxin to NG108-C15 cells was inhibited by gangliosides (GT1b and GM1) and by monoclonal antibodies (CA-12 and C-9), although inhibition was not complete. Sequential preincubation of C1 toxin with GT1b and CA-12 caused complete inhibition. A Scatchard plot of binding of 125I-labeled C1 toxin to NG108-C15 cells showed a hyperbolic curve. Monoclonal antibody CA-12 but not C-9 neutralized the lethal activity of the toxin toward mice. Only C-9 clearly inhibited toxin binding to GT1b. These results suggest that NG108-C15 cells have at least two kinds of receptors for C1 toxin. From the results of binding tests with neuraminidase-, pronase-, and trypsin-treated NG108-C15 cells, the chemical nature of the high-affinity site was presumed to be a glycoprotein containing sialic acid. GT1b may have an important role in low-affinity sites.
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PMID:Binding of Clostridium botulinum type C neurotoxin to different neuroblastoma cell lines. 253 34

A mouse monoclonal antibody, FKH1, was produced to detect cytoplasmic melanoma-associated antigen. FKH1 was raised using cultured human melanoma cell line KHm-6 as an immunogen. Reactivity of this antibody was assessed by immunohistochemical techniques against cell lines and normal and neoplastic tissues. Positive reactions were seen against 5 human melanoma cell lines. It stained cytoplasm of melanoma cells in a diffuse and granular pattern in indirect immunofluorescence. Immunoelectron microscopy showed diffuse distribution of immunoreactant in the cytoplasm of KHm-1 cells excluding melanosomes and other organelles. Reactivity against frozen and alcohol-fixed, paraffin-embedded melanocytic tumors was also tested with IIF or indirect or avidin biotinylated horseradish peroxidase complex immunoperoxidase techniques. All cases of frozen sections from benign and malignant melanocytic tumors showed positive staining with FKH1. In fixed tissues, however, reactivity was 11 of 14 (79%) in malignant melanoma and 28 of 42 (67%) in other melanocytic tumors. FKH1 did not react against normal melanocytes and nonmelanocytic tumors except APUDoma and 2 glioblastoma cell lines. It failed to stain the B-16 mouse melanoma cell line, neuroblastoma cell line, breast carcinoma cell line, and T-cell lymphoma cell line. Normal human peripheral nerves were nonreactive with FKH1. In immunoelectroblot study, FKH1 bound with proteins having molecular weight of 71,000 and 55,000 extracted from KHm-6 cells. It was suggested that FKH1 is a useful monoclonal antibody in diagnostic study of human malignant melanoma specimens.
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PMID:Mouse monoclonal antibody (FKH1) detecting human melanoma-associated antigens. 375 74

Methods are described to study cell surface and cytoplasmic antigens of cultured human glioma, fetal brain cells and fibroblasts using flow cytometry. This required harvesting the cultured cells with Versene or mild trypsin treatment and fixation in 4% paraformaldehyde prior to staining for glial fibrillary acidic protein (GFAP) and fibronectin using indirect immunofluorescence. At passage 10, 38% of fetal brain cells [CHII] were GFAP-positive but at passage 14 only 3.5% expressed GFAP. Two glioblastomas and an anaplastic astrocytoma had 38.8%, 6.7% and 81.3% GFAP-positive cells, respectively. Of the 10(4) cells studied, 91.6%, 79.1% and 40.8% were fibronectin-positive for glioblastoma multiforme [12-18], oligodendroglioma [12-10] and fetal brain [CHII] cells, respectively. Two fibroblast lines had 33.5% and 43.1% of the cells expressing fibronectin. The validity of these results was confirmed by staining for GFAP and fibronectin using peroxidase-antiperoxidase and immunofluorescence microscopy. Using low angle forward light scatter to estimate cell size and gating techniques it was found that GFAP-positive CHII and anaplastic astrocytoma cells were generally larger than GFAP-negative cells of the same type. No correlation between cell size and fibronectin expression was found for glioblastoma [12-18] cells. These results demonstrate the validity of the described methods and illustrate some specific applications and the potential value of flow cytometry to neurooncology.
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PMID:Application of flow cytometry to analyses of cultured human glioma and fetal brain cells. 388 48

The authors investigated the immunohistochemical localization of S-100 protein in normal human brain and glioblastoma tissues by the peroxidase anti-peroxidase method of Sternberger. In normal human brain the positive immunoperoxidase reaction for S-100 protein was observed in astrocytes, oligodendrocytes, ependymal cells, Bergmann's glial cells and epithelial cells of choroid plexus. No positive staining was revealed in any cortical neurons. Immunoelectron-microscopically, the electron dense positive reaction for S-100 protein was seen throughout the cytoplasm, nucleoplasm and cell processes of astrocyte as well as oligodendrocyte. The positive reaction for S-100 protein was demonstrated occasionally in association with cytoplasmic membrane or the membrane constituting cell organelles. We suspect that this observation indicates the existence of membrane-bound form of S-100 protein. In glioblastoma cells, the positive reaction for S-100 protein was relatively weak in intensity as compared with astrocytes, and the degree of positive staining varied from cell to cell. Subcellular localization of S-100 protein in glioblastoma seemed to be essentially similar to that of normal astrocyte. There are some recent reports concerning immunohistochemical localization of alpha and beta subunits of S-100 protein. As compared with these reports, the present immunohistochemical results indicate that the rabbit anti-S-100 antibody embloyed in the present study is mainly against beta subunit of S-100 protein. Although there have been many reports concerning immunohistochemical localization of S-100 protein, the biological role of S-100 protein is still speculative. Some hypotheses are advocated in connection with the possible biological role of S-100 protein. For example, the modulation of synaptic transmission by S-100 protein, the participation of S-100 protein in hormonal secretion and in transport of cations through lipid membrane, the activation of protein kinase and the promotion of disassembly of microtubules by S-100 protein are postulated. It is hard to assume the biological role of S-100 protein based on the immunohistochemical results alone. The present study clearly indicates that S-100 protein exists widely in the cytoplasm, nucleoplasm, cytoplasmic membrane, outer membranes of cell organelles and cell processes of glial cells as well as glioblastoma cells. From these results we assume that S-100 protein plays an important role of intracellular transport of cations as one of the calcium binding proteins.
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PMID:[Immunohistochemical study of S-100 protein in the normal human brain and glioblastoma]. 391 99

Seven different experimental glioma models were studied to determine their capillary permeability to horseradish peroxidase. The models were the autochthonous ASV-viral model, intracerebral (ic) and (sc) injections of rat 9L and RG-2 tumor cell lines, the sc rat S-69C15 tumor cell line, and human glioblastoma cell lines in nude mice. The ASV-viral model showed an average HRP permeability of 63% of tumor volume, the ic RG-2 tumors were 100% permeable, and the ic 9L tumors were 41% permeable. The permeability of the marginal zone (brain-tumor interface) showed similar variation from group to group. In contrast, all of the sc tumors were 100% permeable regardless of the cell line used to create the tumors. Our results show the variability between these glioma models, and suggest that RG-2 ic gliomas and all sc gliomas should be optimal to assess the tumoricidal effect of drugs, because access to the tumor compartment from the vascular compartment is complete.
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PMID:Comparative permeability of different glioma models to horseradish peroxidase. 617 14

The antigenic relationships between human tumors of neuroectodermal origin and fetal brain were investigated by the production of hybridoma antibodies derived from a fusion of P3-NS1/1-Ag 4-1 (NS1) myeloma cells with splenocytes from a mouse multiply immunized with an homogenate of second-trimester human fetal brain tissue. Two monoclonal antibodies (MAs), 4D2cl 6 and 7H10cl 4, were studied in detail by cell surface radioimmunoassay (CS-RIA), quantitative absorption, indirect immunofluorescence, and peroxidase-anti-peroxidase (PAP) immunohistology. MA 4D2cl 6 binds to 5 of 14 glioblastoma (GBM) cell lines, 1 of 2 melanoma cell lines, 1 of 3 neuroblastoma cell lines, and 1 of 5 fetal fibroblast lines by CS-RIA and to 13 of 13 GBM, 1 neuroblastoma, and fetal brain, liver, spleen, and adult spleen unfixed frozen tissue by PAP analysis. MA 7H10cl 4 binds to 13 of 14 GBM, 1 of 3 neuroblastoma, and 1 medulloblastoma cell line(s) by CS-RIA analysis and to 13 of 13 GBM, 1 neuroblastoma, fetal brain, liver, spleen, thymus, and adult spleen by PAP analysis. Control non-central nervous system tumors and normal adult tissue, including brain, were unreactive with both MAs by CS-RIA, PAP, and absorption analysis. Tissue distribution and localization analyses established that MAs 4D2cl 6 and 7H10cl 4 recognize specificities of shared fetal-neuroectodermal-lymphoid distribution which are operationally specific within the adult central nervous system and which are not related to previously described oncofetal or onconeural antigens.
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PMID:Expression of human fetal brain antigens by human tumors of neuroectodermal origin as defined by monoclonal antibodies. 627 12


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