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)

Thirty-two cases of human central nervous tumor and one experimental glioma were studied in fixed paraffin or epon embedded tissues using the peroxidase-antiperoxidase method. The present study confirms the usefulness of immunohistochemical methods for the diagnostic evaluation of neuro-epithelial neoplasms. The authors also include some prognostic and histogenetic comments about glial tumors.
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PMID:[Detection of glial fibrillary acidic protein in central nervous tumors using an immunohistochemical method. Preliminary study of 33 cases (author's transl)]. 625 99

The sarcomatous components of most glioma-sarcomas are thought to arise from the neoplastic transformation of hyperplastic endothelial and adventitial vascular cells in a preexisting glioblastoma multiforme. The expression of factor VIII/von Willebrand factor (FVIII/vWF), a marker for endothelial cells, and of glial fibrillary acidic protein (GFAP), a marker for glial cells, was examined in 10 glioblastomas and seven mixed glioma-sarcomas using the peroxidase-antiperoxidase immunohistochemical technique. Hyperplasia of small blood vessels was observed in all 10 glioblastomas; in five, the vascular proliferation had resulted in the formation of prominent glomeruloid structures. FVIII/vWF was detected in the endothelial cells in these vascular structures, but not in the adventitial cells. In the mixed glioma-sarcomas. FVIII/vWF was detected only in endothelial cells; there was no staining for FVIII/vWF in the neoplastic mesenchymal cells. The gliomatous components of the mixed tumors stained intensely for GFAP. These observations indicate that both endothelial and nonendothelial cell types contribute to the small vessel hyperplasia in glioblastomas, and that the sarcomatous components of mixed glioma-sarcomas are derived from either non-endothelial cells or endothelial cells that have undergone antigenic loss following transformation.
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PMID:Immunohistochemical detection of factor VIII/von Willebrand factor in hyperplastic endothelial cells in glioblastoma multiforme and mixed glioma-sarcoma. 628 91

We have investigated the antigenic heterogeneity of human glioma cells and its correlation with other parameters of tumor cell heterogeneity (karyotype, 2':3' cyclic nucleotide 3'-phosphohydrolase expression, in vitro morphology) using the established human glioma cell line D-54 MG and eight single-cell-derived clones. The panel of antibodies used included 3 previously described heterologous sera raised against human gliomas and lamb oligodendroglia and 10 monoclonal antibodies with demonstrated reactivity for tumors of neuroectodermal origin, human fetal tissue, or human Thy-1. Antigen expression was determined by cell surface radioimmunoassay and peroxidase-antiperoxidase immunohistology. The use of a monoclonal antibody panel composed of ten reagents of varied specificity resulted in the demonstration of highly variable and complex antigenic patterns on the cell surfaces of cloned subpopulations of the human glioma cell line D-54 MG. Only one antigen, human Thy-1, was present on the parent line and all clones; the remaining nine antigens exhibited a distribution unrelated to other predictive parameters of genotypic or phenotypic heterogeneity such as karyotype, 2':3' cyclic nucleotide 3'-phosphohydrolase expression, or in vitro morphology. With the exception of clones 3 and 4, which shared a common antigen profile but exhibited distinctly different in vitro morphological patterns, the detected antigenic profile of each clone was distinct, with the proportion of expressed antigens ranging from 2 of 10 (clone 2) to 10 of 10 (clone 1). The demonstration of distinct, selectively maintained cell subpopulations within a human glioma cell line has direct implications for immunotherapeutic designs.
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PMID:Demonstration of complex antigenic heterogeneity in a human glioma cell line and eight derived clones by specific monoclonal antibodies. 630 81

Extraneural metastases from malignant glioma and glioblastoma are believed to be rare. The most common sites of metastases are lung, lymph nodes, bone, and liver. We recently encountered two patients with glioblastoma multiforme who presented with pain and thrombocytopenia caused by diffuse metastasis to bone marrow. A premortem diagnosis was established in the first patient with the aid of peroxidase-antiperoxidase staining of the bone marrow biopsy specimen for glial fibrillary acidic protein, a glial-specific marker. In the second patient glial fibrillary acidic protein staining confirmed the glial nature of the primary brain tumor as well as the metastatic tumor in bone marrow. The first patient also had metastatic nodules on the pleural surface and on the fifth rib. All three metastatic foci had similar cellular morphology, suggesting selection of a population of tumor cells with extraneural metastatic potential.
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PMID:Diffuse bone marrow metastasis by glioblastoma: premortem diagnosis by peroxidase-antiperoxidase staining for glial fibrillary acidic protein. 631 36

The distribution and localization of a glioma-associated antigen defined by monoclonal antibody 81C6 has been examined using human cultured cell lines and tissues. Monoclonal antibody 81C6 was selected from a hybridoma fusion of spleen cells of mice immunized with the glial fibrillary acidic protein-positive human glioma cell line U-251 MG. Results of cell surface radioimmunoassay and absorption analysis demonstrated that 81C6 defined a glioma-mesenchymal extracellular matrix (GMEM) antigen expressed by 14 of 16 gliomas, 1 of 3 neuroblastomas, 1 of 7 melanomas, 2 of 6 sarcoma cell lines, and 8 of 9 cultured fibroblast lines. GMEM was not expressed by carcinoma or by the myeloid-lymphoid cell lines examined. Within the central nervous system, GMEM was expressed in 10 of 11 glioblastomas but was undetected in 5 of 6 astrocytomas and in normal adult and fetal brain by peroxidase-antiperoxidase immunohistology. In glioblastomas, the GMEM antigen was localized to basement membranes of the distinctive glomeruloid endothelial proliferations and hyperplastic blood vessels. The GMEM antigen was also expressed in 3 of 3 glioblastoma cell lines and 6 of 8 glioblastoma biopsy xenografts in athymic nude mice. Among non-central nervous system tissues and tumors, GMEM was found by peroxidase-antiperoxidase immunohistology in normal liver sinusoids, spleen red pulp sinusoids, kidney medullary tubule interstitium, and glomerular mesangium and in association with vascular and stromal elements of several undifferentiated tumors. The GMEM antigen is distinct from previously described forms of fibronectin, laminin, collagen types I to V, hyaluronic acid, chondroitin sulfate, and heparin, as determined by absorption analysis and immunohistological localization in tissues. The expression of GMEM in glioblastoma but not normal brain, association with glioblastoma-proliferative endothelium basement membranes, and expression in glioblastoma cell lines and nude mouse xenografts suggest that GMEM may be a useful marker of gliomas in vivo and in vitro.
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PMID:Human glioma-mesenchymal extracellular matrix antigen defined by monoclonal antibody. 634 60

Various tissues from rat were examined for the occurrence and cellular localization of plectin, a 300,000-dalton polypeptide component present in intermediate filament-enriched cytoskeletons prepared from cultured cells by treatment with nonionic detergent and high salt solution. The extraction of liver, heart, skeletal muscle, tongue, and urinary bladder with 1% Triton/0.6 M KCl yielded insoluble cell residues that contained polypeptides of Mr 300,000 in variable amounts. These high Mr polypeptide species and a few bands of slightly lower Mr (most likely proteolytic breakdown products) were shown to react with antibodies to rat glioma C6 cell plectin using immunoautoradiography and/or immunoprecipitation. By indirect immunofluorescence microscopy using frozen sections (4 micron) of stomach, kidney, small intestine, liver, uterus, urinary bladder, and heart, antigens reacting with antibodies to plectin were found in fibroblast, endothelial, smooth, skeletal, and cardiac muscle, nerve, and epithelial cells of various types. Depending on the cell type, staining was observed either throughout the cytoplasm, or primarily at the periphery of cells, or in both locations. In hepatocytes, besides granular staining at the cell periphery, conspicuous staining of junctions sealing bile canaliculi was seen. In cardiac muscle strong staining was seen at intercalated disks and, as in skeletal muscle, at Z-lines. In cross sections through smooth muscle, most strikingly of urinary bladder, antibodies to plectin specifically decorated regularly spaced, spot-like structures at the cell periphery. By immunoelectron microscopy using the peroxidase technique, antiplectin-reactive material was found along cell junctions of hepatocytes and was particularly enriched at desmosomal plaques and structures associated with their cytoplasmic surfaces. A specific immunoreaction with desmosomes was also evident in sections through tongue. In cardiac muscle, besides Z-lines, intercalated disks were reactive along almost their entire surface, suggesting that plectin was associated with the fascia adherens, desmosomes, and probably gap junctions. In smooth muscle cells, regularly spaced lateral densities probably representing myofilament attachment sites were immunoreactive with plectin antibodies. The results show that plectin is of widespread occurrence with regard to tissues and cell types. Furthermore, immunolocalization by light and electron microscopy at junctional sites of various cell types and at attachment sites of cytoplasmic filaments in epithelial and muscle cells suggests that plectin possibly plays a universal role in the formation of cell junctions and the anchorage of cytoplasmic filaments.
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PMID:Occurrence and immunolocalization of plectin in tissues. 635 Mar 22

Twenty cases of ovarian or testicular teratomas were studied with a sensitive peroxidase-antiperoxidase (PAP) method utilizing an antibody to glial fibrillary acidic protein (GFAP). Positive staining was restricted to the perikaryon, to extensively distributed neuroglial fibrils, or to ependymal lining cells in 13 of 20 teratomas studied. Positively stained cells were also occasionally observed in the choroid plexus, thus indicating the possibility that such cells also retain the capability of producing GFAP. GFAP-positive material was also found in the tumour cells of an undifferentiated ovarian teratocarcinoma; this tumour was believed to represent an ovarian glioma. It is concluded that the PAP method represents a sensitive and valuable histochemical tool which should be further explored to characterize a functional basis of normal and neoplastic cells. Findings are of particular interest in the "germ cell tumours" in which multiple differentiation patterns may be expressed.
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PMID:Immunohistochemical studies of ovarian and testicular teratomas with antiserum to glial fibrillary acidic protein. 636 59

Monoclonal antibodies ( MCAs ) have been derived from a fusion of P3-NS1/1-Ag 4-1 (NS1) myeloma cells and splenocytes immunized to human glioma cell line D-54 MG. MCAs 2F3 , 4C7 , and 5B7 were analyzed by cell surface radioimmunoassay (CS-RIA), quantitative absorption, indirect immunofluorescence, and peroxidase-anti-peroxidase (PAP) immunohistology of unfixed tissue samples. MCA 2F3 exhibits the most highly restricted pattern of reactivity we have observed, reacting only with 5/12 glioblastoma cell lines and 1/4 fetal skin lines by CS-RIA, and to 9/11 glioblastoma tissue samples by PAP and absorption analysis; this MCA is totally nonreactive with melanomas, neuroblastomas, meningiomas, and control non-central nervous system tumors, and to adult and fetal tissues including brain, thymus, spleen, liver, lung, heart, gut, skin, and muscle by PAP analysis. MCAs 4C7 and 5B7 demonstrate neuroectodermal tumor cross-reactivity profiles, reacting with either melanomas ( 5B7 ) or melanomas and neuroblastomas ( 4C7 ); both are reactive with fetal skin, brain, and thymus of less than or equal to 16 weeks of gestational age. Other than this latter fetal antigen reactivity, these MCAs share the same negative reactivity profile described above for MCA 2F3 . Data from experiments using control or 0.02% EDTA-treated confluent cell monolayers of D-54 MG as antibody absorbents showed that the antigens detected are present in the extracellular matrix material remaining following cell removal. The data presented here establish that these highly restrictive anti-human glioma cell line MCAs are expressed in primary human gliomas; that the markers defined are developmental in nature, in that they are expressed by human fetal tissue, but not by adult tissue; and that in conjunction with previously characterized specificities, these markers of antigenic heterogeneity will be valuable in model system studies of therapeutic response heterogeneity.
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PMID:Characterization of three restricted specificity monoclonal antibodies raised against the human glioma cell line D-54 MG. 637 21

The aim of this work was to elucidate the direction and time-course of transport processes which may affect the accumulation of oedema associated with experimental brain tumours. Astrocytomas were produced in BD-IX rats by intracerebral injection of cultured neoplastic glial cells. The cell line used was cloned from a culture of a primary mixed glioma induced by transplacental administration of N-ethyl-N-nitrosourea (ENU). At various times after cell injection the protein tracer horseradish peroxidase (HRP) was given to tumour-bearing rats, either intravenously or into the lateral ventricles of the brain. The movement of the HRP into tumours and surrounding brain either from blood or from ventricular cerebrospinal fluid (CSF) was studied by light and electron microscopy at various intervals after the injection of the tracer. The time-course of subsequent clearance of the HRP from the tumours and surrounding brain was also investigated. After intravenous injection, HRP rapidly penetrated all vascularized tumours and became evenly distributed within 10-20 min. The HRP remained present in sufficient quantity within the tumours to maintain this intensity for several hours, after which it gradually disappeared, showing no reaction product after 12 h. After intraventricular injection, HRP penetrated periventricular brain tissue up to a maximal distance 1-2 mm within 2 min, and the reaction product remained visible in this region for at least 20 min. In all tumour-bearing animals, HRP penetrated further into periventricular tumour tissue than into adjacent brain tissue. In large tumours HRP reaction product was seen up to 7 mm from the ventricular ependymal lining, although permeation to this distance took up to 10 min.
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PMID:The vasculature of experimental brain tumours. Part 3. Permeability studies. 647 Jul 45

In rats experimental brain tumors were produced by intracerebral implantation of a glioma cell clone. Peritumorous edema was investigated by light and electron microscopy, using exogenous tracers [human serum albumin (HSA), horseradish peroxidase] and immuno-histochemical methods for localization of endogenous serum proteins. An infiltration by serum proteins was observed in peritumoral grey and white matter. Peroxidase was found in pinocytotic vesicles of vascular endothelial cells, in pericytes and diffusely in the extracellular space. High concentrations of endogenous rat serum proteins and exogenous human serum albumin were also found in neurons of the grey matter and in oligodendrocytes of the white matter. A cellular uptake of extravasated proteins, therefore, may contribute to edema resolution.
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PMID:Experimental brain tumors and edema in rats. III. Peritumorous edema. 654 42


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