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)

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

Coelectrophoresis in two-dimensional gels of rat glial fibrillary acidic protein (GFA) and 32P-labeled whole cell extracts of rat C-6 glioma cells showed that the GFA migrated in close proximity to a previously noted phosphoprotein, 50K-6.1, of these cells. GFA electrophoresed as a 50K polypeptide with at least four charge variants, the most acidic of which coelectrophoresed with 50K-6.1. Exposure of the C-6 cultures to dibutyryl cyclic AMP (dbcAMP) for 48 h increased the relative abundance of the endogenous polypeptide associated with 50K-6.1 by threefold, consistent with the hypothesis that 50K-6.1 was GFA. Norepinephrine stimulated 50K-6.1 phosphorylation 3.2-fold in dbcAMP-induced cultures. Peptide mapping with V8 protease and subtilisin was used to test the hypothesis that GFA and 50K-6.1 were identical polypeptides. With V8 protease, the peptides generated from the [35S]methionine labeled putative GFA spot of the C-6 cells were indistinguishable from the stained bands derived from authentic GFA in mixed samples of the two proteins. Likewise, the 35S-labeled acidic satellite to the putative GFA spot also yielded a peptide map that matched that of the authentic GFA. 32P-labeled peptides derived from the 50K-6.1 protein were a subset of those from authentic GFA. With three subtilisin concentrations, 32P-labeled 50K-6.1 was degraded to peptides which were again a subset of the stained GFA peptides. A cytoskeletal fraction from 32P-labeled C-6 cells contained a 50K phosphoprotein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Glial fibrillary acidic protein: norepinephrine stimulated phosphorylation in intact C-6 glioma cells. 669 99

Glia maturation factor (GMF)-like activity which induces DNA synthesis and morphological differentiation of density-inhibited glioblasts was detected in various glial tumor cells. A polypeptide from C6 cells (rat astrocytoma) which has a molecular weight range of 40,000-50,000 showed the highest activity. This factor also induced DNA synthesis in glioma cells (354A and LRM55) and fibroblast (Swiss 3T3). The activity was susceptible to heat treatment at 70 degrees C for 5 min, or to proteases such as trypsin, chymotrypsin, papain, and subtilisin, but it was devoid of esteropeptidase activity. The isoelectric point was found to be 5.3. Subcellular fractionation localized the activity in cytosomal and microsomal fractions. These properties closely resemble those of GMF from pig and bovine brain.
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PMID:The induction of glial proliferation by an astrocytoma-derived growth factor resembling glia maturation factor. 681 7

Extracts of neuroblastoma X glioma hybrid cells 108CC15 and their parental lines were investigated for the presence of vasoactive intestinal polypeptide (VIP). With the aid of a radioimmunoassay and a receptor binding assay, VIP activity was found in the hybrid cells, to a lesser extent in neuroblastoma cells, but not in glioma cells. These results suggest a neuronal function of VIP. Since the hybrid cells also contain acetylcholine and opioids, they may be useful in studies of co-release of neurohormones.
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PMID:Vasoactive intestinal polypeptide: presence in neuroblastoma X glioma hybrid cells. 687 74

The expression on several established human glioma cell lines of two well-defined differentiation antigens, HLA-DR and the common acute lymphoblastic leukemia antigen (CALLA) has been demonstrated. Rabbit anti-CALLA antiserum and monoclonal anti-Ia antibodies specifically lysed glioma cells in the presence of complement. Absorption of anti-CALLA antiserum and anti-Ia antibodies by glioma cells abolished their cytotoxicity against blasts isolated from a common acute lymphoblastic leukemia. Immunoprecipitation of solubilized glioma cells by monoclonal anti-Ia antibodies revealed two polypeptide chains of 28 and 33 kDa, whereas the anti-CALLA antiserum precipitated a single polypeptide chain of 100 kDa.
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PMID:Expression of HLA-DR and common acute lymphoblastic leukemia antigens on glioma cells. 695 72

In search of tumor-associated components in human melanomas and gliomas, plasma membranes were isolated from these tumors and compared morphologically, biochemically and immunologically with those from normal human brain. The preparations exhibited a comparable ultrastructure of empty vesicles of various form and size. The melanoma membrane consisted of at least 15 protein components and the glioma membrane consisted of at least 24 protein components, four of which were absent in the membrane of normal tissue, as revealed by polyacrylamide gel electrophoresis. The four tumor-associated polypeptides could be solubilized together with a few other membrane components by the non-ionic detergent Triton-X100 and were used as an antigen source for immunologic characterization of melanoma and glioma membranes. A rabbit antiserum prepared against these solubilized membrane components from melanoma were absorbed with plasma membranes from a variety of normal tissue including erythrocytes, lymphocytes, spleen, liver, lung, kidney, placenta and brain. The absorbed antiserum reacted with the membrane extract of all the 11 melanomas tested so far; in addition it cross-reacted with an identically prepared extract from all the 15 gliomas tested. Membrane extracts from other tumors, such as kidney and mammary carcinoma, were negative in this respect. Furthermore, a rabbit antiserum prepared against Triton extract from glioma membranes yielded after exhaustive absorption an immune precipitate not only with the specimens from the 15 other gliomas but also with those from the 11 melanomas. Electrophoretic analysis of the immune precipitate formed by the immunoglobulin fraction of the absorbed rabbit antiserum and the Triton-X100 extract from melanoma membranes exhibited six polypeptide bands, two of which appear antigen-derived as they were missing in the profile of the immunoglobulin pattern. A comparable electrophoretic pattern was obtained with the immune precipitate of the glioma antigen specimen. The molecular weight of these two polypeptides was estimated on the basis of their electrophoretic mobility to be 55,000 and 10,000 daltons, respectively. The electrophoretic immunologic findings argue for a common membrane component in human melanoma and glioma patients. Using the Triton extract from melanoma membranes as an antigen source, precipitating antibodies could be detected in the immunoglobulin fraction of 16 of the 24 sera from melanoma patients and in that of 15 of the 23 glioma patients by means of counter-current electrophoresis. Sera from a variety of cancer patients with diseases other than melanoma or glioma as well as from patients without cancer were negative in this respect.
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PMID:Humoral immune response in melanoma and glioma patients: a solubilized melanoma-membrane component as a tool for detecting circulating antibodies. 729 90

Phospholipase C-beta 1 (PLC-beta 1) exists as two immunologically indistinguishable polypeptides of 150 and 140 kDa and is encoded in rat brain by two distinct transcripts of 5.4 and 7.2 kilobases (kb). cDNA corresponding to the entire 5.4-kb transcript as reported previously reveals an open reading frame that is capable of coding a 1216-amino acid polypeptide (Suh, P. G., Ryu, S. H., Moon, K. H., Suh, H. W., and Rhee, S. G. (1988) Cell 54, 161-169). We have now isolated cDNAs corresponding to the entire 7.2-kb transcript from a rat brain cDNA library. The 7.2-kb transcript differs from the previously reported 5.4-kb transcript by possessing both an additional 118 nucleotides located near the end of the coding sequence and a 1738-nucleotide extension of the 3'-flanking region. The presence of the 118-nucleotide insert in the cumulative 7.2-kb sequence gives rise to an open reading frame that is capable of coding a 1173-amino acid polypeptide (PLC-beta 1b), the carboxyl-terminal sequence of which differs from that of the 1216-amino acid polypeptide (PLC-beta 1a) derived from the 5.4-kb transcript. Antibodies were raised against synthetic peptides corresponding to the carboxyl-terminal portions of PLC-beta 1a and PLC-beta 1b. Immunoblot analysis with these isozyme-specific antibodies revealed that both PLC-beta 1a and PLC-beta 1b are expressed in rat brain and C6Bu-1 glioma cells and that PLC-beta 1a and PLC-beta 1b correspond to the previously identified 150- and 140-kDa PLC-beta 1 enzymes, respectively. Analysis of PLC-beta 1 genomic DNA indicates that PLC-beta 1a and PLC-beta 1b are derived from a single gene by alternative RNA splicing.
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PMID:Two forms of phospholipase C-beta 1 generated by alternative splicing. 751 Jun 82

We have found that the gene expression of the ninth member of the fibroblast growth factor (FGF) family, FGF9 was induced during retinoic acid(RA)-induced neuronal differentiation of murine embryonal carcinoma P19 cells. We have reported here the nucleotide sequence of the mouse FGF9 cDNA. The murine cDNA showed 92.4% nucleotide sequence homology to the human FGF9 cDNA and 98.2% homology to that of rats. This mouse FGF9 cDNA encoded a polypeptide consisting of 208 amino acids with amino acid sequence identical to that of rats. Only one amino acid was replaced compared to the human homolog. The highly conserved sequence homology of FGF9 suggests its functional importance. FGF9 was originally isolated from a culture medium of a human glioma cell line as a growth-promoting factor for glial cells [5]. Upon induction of neuronal differentiation by forming cell aggregates with 10(-6) M RA, the gene expression of FGF9 was increased biphasically during the first 96 hours when cells were aggregating and from 168 hours to 192 hours followed by plating onto a tissue culture dish as glia-like cells proliferated. Neither undifferentiated P19 cells nor the cells aggregated without RA remaining undifferentiated expressed FGF9. This indicates that RA regulates the gene expression of FGF9 that may play an important role in neuronal differentiation in both early and late developmental process.
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PMID:Retinoic acid induces gene expression of fibroblast growth factor-9 during induction of neuronal differentiation of mouse embryonal carcinoma P19 cells. 765 83

The expression of polypeptide growth factors and their receptors by certain malignant human cell lines and the ability to grow these tumors as xenografts in murine hosts provides a useful setting to investigate the efficacy of antitumor agents. Exon 6 of the platelet-derived growth factor A-chain predicts a highly basic region consisting of 18 amino acids. Previously, we demonstrated that a synthetic peptide bearing this sequence interacts with a large population of binding sites at the cell surface and inhibits the binding and mitogenesis stimulated by several polypeptide growth factors (Khachigian et al J Biol Chem 267: 1660-1666, 1992; Khachigian and Chesterman, J Biol Chem 267: 7478-7482, 1992). In this report, we show that the exon 6 peptide can inhibit the mitogenic response of cultured human U-118 malignant glioma cells to normal human serum. When these cells are grown as subcutaneous xenografts in athymic nude mice, repeated intratumoral administration of the peptide results in dose-dependent growth inhibition. Indeed, injection of 0.48 mg of peptide five times a week abrogated growth during the entire course of treatment. Mouse weight or behavior did not differ significantly between control and treatment groups. Moreover, histologic examination of the tumors following treatment did not indicate necrosis. Thus, the exon 6 peptide can inhibit glioma cell proliferation both in culture and in an animal model without apparent side effects.
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PMID:Platelet-derived growth factor A-chain synthetic peptide inhibits human glioma xenograft proliferation in nude mice. 776 3

We have identified and sequenced a new gene from human cells that is responsive to DNA damage and retinoic acid treatment, and it is highly expressed in brain and reproductive organs (BRE). This BRE gene encodes an mRNA of 1.7-1.9 kb, with an open reading frame of 1,149 bp, and gives rise to a deduced polypeptide of 383 amino acid residues. Treatment of fibroblast cell with UV and 4-nitroquinoline-1-oxide caused more than 90% and 50% decreases in BRE mRNA, respectively. Similar decreases in BRE expression were observed in RA-treatment of the brain glioma cell U-251 and the promyelocytic cell HL-60. Decrease in BRE mRNA was also observed in a squamous carcinoma cell, 1483, that showed X-ray resistance and has a more aggressive tumorigenic phenotype, but BRE expression was unchanged in cells after growth inhibition. These data indicate that BRE is a house-keeping gene and it may play a role in homeostatis or in certain pathways of differentiation in cells of neural, epithelial and germ line origins.
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PMID:Identification of a brain- and reproductive-organs-specific gene responsive to DNA damage and retinoic acid. 782 98


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