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)

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

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

Experimental brain tumours were produced in cats by stereotactic implantation of 4 million suspended cells of a rat glioma clone into the internal capsule. Three weeks after implantation a spherical tumour developed with a diameter of up to 10 mm which was surrounded by vasogenic white matter oedema. In untreated animals water content in the peritumoural white matter increased form 69.1 +/- 0.9 to 80.0 +/0 0.8 ml/100 g w. w., and regional blood flow reciprocally decreased from 32.2 +/- 5.6 to 18.9 +/- 0.05 ml/100 g/min. A single injection of a crystalline suspension of 10 mg/kg dexamethasone given intramuscularly one week before the animals were killed, led to a significant amelioration of brain oedema. Peritumoural white matter water content decreased to 73.0 +/- 0.5 ml/100 g w w. and blood flow rose to 35.7 +/- 2.8 ml/100 g/min. These changes were accompanied by parallel shifts of electrolyte content buy did not correlate with EEG activity, as assessed by Fourier frequency analysis. Corticosteroids did not prevent extravasation of peroxidase or Evans blue across the tumour vessels. The beneficial effect, therefore, is attributed to either an acceleration of resorption or an inhibition of the spread of oedema from tumour into the peritumoural brain tissue.
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PMID:Corticosteroid therapy of experimental tumour oedema. 732 60

Previous studies have shown that serum proteins are taken up from extracellular oedema fluid by reactive astrocytes and by tumour astrocytes. The present investigation was designed to define the mechanism of this protein uptake. Two or 3-week-old explant cultures from 26 astrocytic gliomas, one anaplastic ependymoma, and five non-glial intracranial tumours were treated with either human IgG (12 mg/ml), human serum albumin, (44 mg/ml) or horseradish peroxidase (0.1--4.0 mg/ml) for 4--24 h. Human IgG and albumin were subsequently detected in cultured cells by the indirect peroxidase-antiperoxidase (PAP) method for light microscopy or by direct peroxidase conjugate technique for electron microscopy. Horseradish peroxidase activity was localised by treatment with diaminobenzidine and hydrogen peroxide. Results of the study show that human serum proteins and horseradish peroxidase are taken up by tumour astrocytes and ependymal cells, and by macrophages, but not by non-glial tumour cells nor by mesenchymal elements in the glioma cultures. Electron immunocytochemistry suggests that the serum proteins are taken up by smooth walled micropinocytic vesicles (approximately 80 nm in diameter) which fuse to form larger endocytic vesicles (200--300 nm); these vacuoles in turn fuse with secondary lysosomes to form cytoplasmic bodies 1.2--3 mum in diameter.
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PMID:Mechanisms of uptake and the fate of serum proteins and horseradish peroxidase in cultured human glioma cells. A light- and electron-immunocytochemical study. 744 81

The sulfhydryl agent, cysteamine (CSH), promotes the accumulation of autofluorescent, peroxidase-positive cytoplasmic granules in cultured astroglia akin to those which naturally accumulate in astrocytes of the aging periventricular brain. Both in vitro and in situ, CSH rapidly induces various heat shock proteins (HSP) in astrocytes long before granulation occurs. In the present study, we determined that CSH treatment resulted in an increase in HSP 27, HSP 90 and heme oxygenase (HO-1) at both the protein and mRNA level. We also showed that C6 glioma cells, unlike primary astrocytes, constitutively express HSP 27, HSP 90 and HO-1 at low levels. Moreover, CSH is incapable of eliciting further HSP expression or inducing granulation in the glioma cells. Our results support the hypothesis that the biogenesis of redox-active astrocytic inclusions in CSH-treated glial cultures and in the aging periventricular brain is dependent on an antecedent cellular stress response.
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PMID:Differential effects of cysteamine on heat shock protein induction and cytoplasmic granulation in astrocytes and glioma cells. 747 27

Formalin-fixed, paraffin-embedded surgical specimens from 140 primary human central nervous system tumors, including 51 meningiomas, 26 astrocytomas, 26 anaplastic astrocytomas, 9 glioblastomas, 1 gliosarcoma, 8 oligodendrogliomas, 5 ependymomas, 2 subependymomas, 9 medulloblastomas, and 3 paragangliomas, were immunostained using a streptavidin/peroxidase method and the PC10 monoclonal antibody, which recognizes an epitope on the proliferating cell nuclear antigen (PCNA). The following PCNA labeling index (LI) mean values were found for the above neoplasms: meningiomas, 3.80 +/- 7.35%; astrocytomas, 0.65 +/- 1.03%; anaplastic astrocytomas, 8.46 +/- 7.95%; glioblastomas, 10.26 +/- 11.21; gliosarcoma, 46.34%; oligodendrogliomas, 2.31 +/- 3.59%; ependymomas, 1.12 +/- 2.10%; medulloblastomas, 23.91 +/- 11.95%; and paragangliomas, 2.07 +/- 1.86%. Collectively, our findings indicate that while benign central nervous system tumors generally have low PCNA LI values, consistent over-expression of PCNA epitopes was noted in some examples, especially in a number of meningiomas. Among the malignant neuroectodermal tumors, medulloblastomas were found to have the highest PCNA LI values, corresponding to their histological grade of malignancy, and malignant glial tumors generally displayed significantly higher PCNA LI values, than their benign counterparts. Although in our study mean PCNA LI values seemed to reflect histological grading, large discrepancies were noted in all tumor groups. Our data, therefore, suggest than PCNA immunoreactivity can not be considered reliable for predicting the prognosis of the disease in individual cases.
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PMID:Proliferating cell nuclear antigen immunoreactivity in human central nervous system neoplasms. 768 17


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