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)

The pathological findings, including immunohistochemical and electron microscopical findings, in three infants who died unexpectedly of cardiac tumor or cardiomyopathy are reported. The first was a 13-month-old boy with tuberous sclerosis and multiple rhabdomyomas of the heart, who presented with a postpartal cardiac murmur and moderate cardiomegaly. The further history was unknown. The rhabdomyoma nodules were composed of spider cells containing small amounts of desmin and myosin as well as isolated myofibrils. Microscopically small glioma nodules contained high amounts of GFAP. The second case, a boy 4 months of age, died of a large benign fibrous histiocytoma of the heart after an uneventful history. Tumor cells contained alpha-1-anti-chymotrypsin and lysozyme. The third case, a girl 2 months of age, died unexpectedly of histiocytoid cardiomyopathy. The affected cells contained fat droplets, glycogen granules, many leptomer myofibrils and small amounts of myosin and desmin.
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PMID:Unexpected infant death attributable to cardiac tumor or cardiomyopathy. Immunohistochemical and electron microscopical findings in three cases. 216 15

The phenomenon of glioma killing by lymphokine activated killer cells (LAK) was studied. We demonstrate that LAK cells generated by culturing the lymphokine interleukin-2 (IL-2) with peripheral blood lymphocytes from brain tumour patients destroys autologous glioma. The rat 9L glioma model was used to show that LAK killing was tumour-selective as glioma but not syngeneic normal brain tissue was destroyed. The susceptibility of both human and 9L rat glioma to LAK cell killing was markedly diminished by pretreating glioma cells with trypsin or chymotrypsin, but was unaffected by pretreatment with neuraminidase, glycosidases, sodium periodate or hydrocortisone. These results suggest that the cell surface determinant on glioma cells responsible for its tumour selective lysis by LAK is a protein sensitive to trypsin and chymotrypsin. The tumour-selective killing of glioma by LAK in vitro prompted the initiation of a Phase I study in which ten patients with malignant glioma have been treated with direct intracerebral injection of IL-2 or LAK without evidence of systemic or brain toxicity.
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PMID:Interleukin-2 and lymphokine activated killer (LAK) cells in the treatment of malignant glioma: clinical and experimental studies. 287 9

The killing of human glioma by lymphokine activated killer (LAK) cells was studied. LAK cells generated by culturing recombinant interleukin-2 (IL-2) with human peripheral blood lymphocytes (PBL) obtained from normal volunteers markedly lysed allogeneic glioma grown in tissue culture. Susceptibility of glioma to lysis by LAK cells was abrogated by pretreating the glioma cells with trypsin or chymotrypsin, but was unaffected by pretreatment with hydrocortisone, neuraminidase, glycosidases or sodium periodate. These results suggest that the cell surface determinant on human glioma cells responsible for its tumor selective lysis by LAK is a protein sensitive to trypsin and chymotrypsin.
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PMID:Lymphokine activated killer (LAK) cell mediated killing of human glioma: effect of pretreating glioma with various membrane modifying agents. 303 36

The interaction of cells with laminin and laminin fragments was studied in short-term cell attachment assays. Neurite-promoting chymotrypsin fragments of laminin were isolated using a monoclonal antibody which blocks neurite outgrowth on laminin. The fragments were shown, by electron microscopy after rotary shadowing and by immunological reactivity with different monoclonal antibodies, to contain only the distal end of the long arm. These fragments promoted the attachment and spreading of glioma, sarcoma, carcinoma, muscle, and endodermal cells to the same extent as intact laminin. The attachment was unaffected by peptides containing the RGD sequence. The morphology of the cells on the chymotrypsin fragments was indistinguishable from that on intact laminin but different from the morphology of the same cells on fibronectin. Light microscopy and scanning electron microscopy showed extensive process formation on laminin but not on fibronectin suggestive of increased cell motility in response to laminin. We conclude that the neurite-promoting domain of laminin contains a major site of interaction for non-neuronal cells and that this site induces a cellular response in certain non-neuronal cells that is unique to laminin.
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PMID:The neurite-promoting domain of human laminin promotes attachment and induces characteristic morphology in non-neuronal cells. 316 84

The killing of Fischer rat 9L glioma in vitro by lymphokine-activated killer (LAK) cells was studied. LAK cells generated by culturing Fischer spleen cells with recombinant interleukin 2 markedly lysed glioma cells but did not kill syngeneic normal brain tissue in a chromium release microcytotoxicity assay. Susceptibility of glioma to lysis by LAK cells was markedly diminished by pretreating the glioma cells with trypsin or chymotrypsin but was unaffected by pretreatment with neuraminidase, glycosidases, or sodium periodate. These results suggest that LAK cell killing of glioma is probably tumor-selective and that a crucial cell surface determinant on glioma cells responsible for its tumor-selective lysis by LAK is a protein sensitive to trypsin and chymotrypsin.
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PMID:Lymphokine activated killer (LAK) cell-mediated lysis of murine glioma: trypsin-chymotrypsin-sensitive glioma protein is responsible for tumor-selective recognition by LAK cells. 348 96

Monoclonal antibodies were produced against surface antigens of live cells from a human acute monocytic leukaemia cell line (THP-1). One clone, VIC-C2, when assayed by immunofluorescence microscopy, brightly stained the surface of THP-1 cells and the cytoplasm of Langerhans cells, fibroblasts and melanocytes in sections of human skin. The immunoreactive cytoplasmic structures were filamentous and resembled intermediate filaments. By double immunofluorescence microscopy using VIC-C2 and polyclonal antibodies to vimentin, the VIC-C2 antigen was shown to be located on intermediate filaments of cultured fibroblasts and to follow these filaments during various drug-induced rearrangements. As demonstrated by immunoprecipitation, antibody gel overlay and immunoblotting of two-dimensional polyacrylamide gels, VIC-C2 recognized two different antigens in extracts of THP-1 cells: one of Mr = 43 000 and pI = 7, the other of Mr = 57 000. In extracts from various cultured fibroblast cells only the 57 000 Mr antigen was detected. This 57 000 Mr protein was identified as vimentin by immunoblotting of rat glioma C6 cytoskeletons on two-dimensional gels. When vimentin was digested with chymotrypsin, only fragments containing parts of both helical rod pieces and the connecting non-helical spacer-region were strongly antigenic, whereas the helical rods alone were only weakly crossreactive. Moreover, immunoprecipitation revealed that VIC-C2 preferentially reacted with native compared to denatured vimentin.
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PMID:Monoclonal antibody to a 43 000 Mr surface protein of a human leukaemia cell line (THP-1) crossreacts with the fibroblast intermediate filament protein vimentin. 386 May 6

A macromolecule has been partially purified which influences the choice of the neurotransmitter synthesized by sympathetic neurons. Previous studies showed that culture medium conditioned by incubation on certain types of non-neuronal cells increased [3H]acetylcholine synthesis and accumulation from [3H]choline in primary cultures of neurons dissociated from neonatal rat superior cervical ganglion and grown in the virtual absence of non-neuronal cells. A concomitant decrease of [3H]catecholamines production was observed (Patterson, P. H., and Chun, L. L. Y. (1977) Dev. Biol. 56, 263-280). The active cholinergic factor in conditioned medium from C6 glioma or primary rat heart cultures has been purified about 1500-fold by a sequence of ammonium sulfate precipitation, DEAE-, CM-cellulose, and Sephadex G-100 chromatography. The partially purified factor is active at 1 microgram of protein/ml of culture medium and is eluted from Sephadex columns as a single peak of apparent Mr = 40,000-45,000. This material is insensitive to 0.2 M 2-mercaptoethanol, but is inactivated by 1 mM Na periodate. Its activity is partially decreased by treatment with a protease from Streptomyces griseus but is unaffected by neuraminidase. Material purified through the ammonium sulfate, DEAE- and CM-cellulose steps contains large amounts of trypsin- and chymotrypsin-inhibiting activities.
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PMID:A diffusible factor responsible for the determination of cholinergic functions in cultured sympathetic neurons. Partial purification and characterization. 611 Jun 68

Exorphins, peptides with opioid activity, have previously been isolated from pepsin hydrolysates of alpha-casein [Zioudrou, C., Streaty, R. A., & Klee, W. A. (1979) J. Biol. Chem. 254, 2446-2449]. Analysis of these peptides shows that they correspond to the sequences 90-96, Arg-Tyr-Leu-Gly-Tyr-Leu-Glu, and 90-95, Arg-Tyr-Leu-Gly-Tyr-Leu, of alpha-casein. These peptides, as well as two of their analogues Tyr-Leu-Gly-Tyr-Leu-Glu (91-96) and Tyr-Leu-Gly-Tyr-Leu (91-95), have now been synthesized and characterized. Their opioid activity was examined by three different bioassays: (a) displacement of D-2-alanyl[tyrosyl-3,5-3H]enkephalin-(5-L-methioninamide) and [3H]dihydromorphine from rat brain membranes; (b) naloxone-reversible inhibition of adenylate cyclase in homogenates of neuroblastoma x glioma hybrid cells; (c) naloxone-reversible inhibition of electrically stimulated contractions of the mouse vas deferens. The synthetic peptide of sequence 90-96 was the most potent opioid in all three bioassays and its potency was similar to that of the isolated alpha-casein exorphins. The synthetic peptides were totally resistant to hydrolysis by trypsin and homogenates of rat brain membranes, but were partially inactivated by chymotrypsin and subtilisin. The difference in opioid activity of alpha-casein exorphins may be related to differences in conformational flexibility observed by NMR spectroscopy.
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PMID:Opioid activities and structures of alpha-casein-derived exorphins. 631 43

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

Protease inhibitors regulate a variety of physiological and pathological processes including angiogenesis, embryo implantation, intravascular fibrinolysis, wound healing, and tumor invasion. Tissue factor pathway inhibitor (TFPI) 2 is a Mr 32,000 Kunitz-type serine protease inhibitor that inhibits plasmin, trypsin, chymotrypsin, cathepsin G, and plasma kallikrein but not urokinase-type plasminogen activator, tissue plasminogen activator, or thrombin. In this study, we determined the relative amounts of TFPI-2 in low-, intermediate-, and high-grade human glioma cell lines and tumor tissue samples. TFPI-2 protein and mRNA levels (measured by Western and Northern blotting) were highest in low-grade glioma cells (Hs683), lower in anaplastic astrocytoma cells (SW1088 and SW1783), and undetectable in high-grade glioma cells (SNB19). Analysis of TFPI-2 protein in human normal brain and in glioma tumor tissues for TFPI-2 revealed the highest levels in normal brain, lesser amounts in low-grade gliomas and anaplastic astrocytomas, and undetectable amounts in glioblastomas. In situ hybridization of TFPI-2 mRNA with normal brain tissues revealed the greatest positivity in neurons, with moderate positivity in both glial and endothelial cells and moderate, little, or no TFPI-2 mRNA in low-grade glioma, anaplastic astrocytoma, and glioblastoma tumor tissue samples, respectively. We also found that recombinant TFPI-2 inhibited the invasiveness of SNB19 glioblastoma cells in a Matrigel assay in a dose-dependent manner. Collectively, these results suggest that TFPI-2 has a regulatory role in the invasiveness of gliomas in vitro and in vivo.
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PMID:Expression of tissue factor pathway inhibitor 2 inversely correlates during the progression of human gliomas. 1129 50


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