Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027819 (neuroblastoma)
 27,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To assess the usefulness of immunocytochemical analysis of bone marrow in patients with neuroblastoma, marrow smears from 33 staging procedures in 12 patients were examined using an indirect immunoalkaline phosphatase technique with monoclonal antibodies raised against human neural tissue. Marrow aspirate and trephine collagenase digest specimens from individual sites were each tested with the monoclonal antibody UJ13A and with a pool of three related antibodies. The results were compared with morphological assessment of conventionally stained aspirates and trephine specimens taken at the same time. Immunostaining suggested the presence of tumour in seven of 18 staging procedures in which conventional techniques had shown infiltration. Tumour infiltration was also suggested in four of 10 staging procedures with suspicious trephine specimens, but in none of three with relatively innocent histological and cytological features. Immunological investigation provides no additional information about the presence of infiltration if conventional microscopy has shown definite tumour. When histological appearances are suspicious, immunostaining of stored aspirate smears or collagenase digest specimens may provide evidence of infiltration. There are insufficient data to comment on the value of immunostaining when conventional techniques reveal "normal" marrow, but the impression gained from this study is that immunostaining has a limited role in the detection of metastatic neuroblastoma, which yet remains to be defined.
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PMID:Immunocytochemical examination of bone marrow in disseminated neuroblastoma. 169 Feb 23

We have used cell-culture techniques to investigate growth-factor production by human meningioma cells. Meningioma tissue was dispersed with collagenase and the cells grown to high density in tissue-culture flasks. The cultures were used to generate conditioned medium (MEN-CM), which was used to cultivate IMR32 cells (a human neuroblastoma line) and freshly dispersed primary meningioma cells. MEN-CM profoundly stimulated the in vitro growth of both IMR32 and meningioma cells. In addition, H3-thymidine uptake by cultured meningioma cells was increased in a dose-dependent manner by varying concentrations of MEN-CM. A neutralizing anti-body against platelet-derived growth factor (PDGF) completely abolished the stimulatory effects of MEN-CM, whereas an antibody against TGF-alpha was without effect. The mitogenic activity of MEN-CM, as assayed by promotion of H3-thymidine uptake by cultured meningioma cells, eluted from a Sephadex G-100 column in 3 peaks corresponding to molecular weights of greater than or equal to 150, 56 and 28 kDa. Our results show that proliferation of human meningiomas may be under autocrine control via secretion of PDGF-like molecules.
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PMID:Autocrine control of human meningioma proliferation: secretion of platelet-derived growth-factor-like molecules. 191 38

Apamin, a bee venom polypeptide, is reported to block the Ca2+-dependent K+ channel in smooth muscle, hepatocyte, and neuroblastoma cells. In embryonic chick hearts, it was found to block the Ca2+ channel. We report here that apamin (10(-9)-10(-7) M) hyperpolarizes the resting membrane potential and shortens the duration of the action potential (AP) in the fast response of adult guinea pig ventricular papillary muscles. This peptide also depresses the isoproterenol or Ba2+-induced slow response APs in the presence of high K+ (21.6 mM) Tyrode solution, without affecting the resting potential. The most striking effect of apamin on the slow response was to shorten the duration of AP with only slight decreases in the maximal rate of increase (Vmax) of the AP, a nonlinear measure of Ca2+ currents. These findings suggest that apamin increases membrane K+ conductance in the mammalian ventricular myocardium. However, in enzymatically isolated single ventricular cells and at wide range of concentrations (10(-7)-10(-11) M), apamin did not affect the AP configuration and did not alter the membrane Ca2+ or K+ current, perhaps because of a loss of apamin sensitivity secondary to enzymatic digestion of the tissue with collagenase.
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PMID:Possible increases in potassium conductance by apamin in mammalian ventricular papillary muscles: a comparison with the effects on enzymatically isolated ventricular cells. 247 13

Collagens are a heterogeneous family of structural proteins synthesized by many cultured cells including tumor cells. The synthesis of these proteins by three human tumor types commonly encountered in children [neuroblastoma, rhabdomyosarcoma, and nephroblastoma (Wilms' tumor)] was investigated in short-term cultures of freshly excised tumor explants grown on extracellular matrices. Analysis of the incorporation of [3H]proline into collagenase-sensitive proteins indicated significant collagen production by several Wilms' tumors and rhabdomyosarcomas, while neuroblastomas did not synthesize this structural protein. All eight Wilms' tumor specimens analyzed secreted type IV procollagen. Interstitial types I and III collagens were also produced by these tumors, but in most cases, the alpha 1 (I): alpha 2 ratio was much higher than the 2:1 ratio expected for type I collagen, indicating a major change in the control of type I collagen production. Rhabdomyosarcomas were very heterogeneous with regard to collagen secretion and synthesized either a single collagen isotype (type III), several collagens including types I, III, and IV, or no detectable collagen. Our data represent a first quantitative and qualitative analysis of collagen synthesis by primary tumor cultures and reveal much more heterogeneity in collagen biosynthesis by these tumors than reported previously with established cell lines. They also indicate significant alterations in the expression of type I collagen genes in Wilms' tumors.
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PMID:Collagen synthesis by short-term explants of pediatric tumors. 298 85

Three novel components of neuromuscular junctions have been identified by use of monoclonal antibodies (McAb) against glycoproteins obtained from a mouse neuroblastoma X human dorsal root ganglion cell hybrid line. Antigen distribution was assessed by fluorescent immunohistochemistry on frozen sections of human intercostal muscle counterstained with labeled alpha-bungarotoxin to identify neuromuscular junctions. Antigen SOS 6 stained exclusively in the neuromuscular junction, whereas antigens SOS 5 and SOS 13 were highly enriched in the junction but also stained extrasynaptic regions. These antigens can be distinguished from previously described components of the neuromuscular junction by their molecular weights, insensitivity to collagenase treatment, and solubility in 0.1% Triton X-100. Indirect evidence suggests that these species-specific antigens are located in the postsynaptic muscle membrane, but location in the junctional basal lamina or subsarcolemmal region cannot be excluded.
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PMID:Novel antigens at the neuromuscular junction. 351 Feb 28

We have identified a tissue-kallikrein-binding protein in human serum and in the serum-free culture media from human lung fibroblasts (WI-38) and rodent neuroblastoma X glioma hybrid cells (NG108-15). Purified and 125I-labelled tissue kallikrein and human serum form an approximately 92,000-Mr SDS-stable complex. The relative quantity of this complex-formation is measured by densitometric scanning of autoradiograms. Complex-formation between tissue kallikrein and the serum binding protein was time-dependent and detectable after 5 min incubation at 37 degrees C, with half-maximal binding at 28 min. Binding of 125I-kallikrein to kallikrein-binding protein is temperature-dependent and can be inhibited by heparin or excess unlabelled tissue kallikrein but not by plasma kallikrein, collagenase, thrombin, urokinase, alpha 1-antitrypsin or kininogens. The kallikrein-binding protein is acid- and heat-labile, as pretreatment of sera at pH 3.0 or at 60 degrees C for 30 min diminishes complex-formation. However, the formed complexes are stable to acid or 1 M-hydroxylamine treatment and can only be partially dissociated with 10 mM-NaOH. When kallikrein was inhibited by the active-site-labelling reagents phenylmethanesulphonyl fluoride or D-Phe-D-Phe-L-Arg-CH2Cl no complex-formation was observed. An endogenous approximately 92,000-Mr kallikrein-kallikrein-binding protein complex was isolated from normal human serum by using a human tissue kallikrein-agarose affinity column. These complexes were recognized by anti-(human tissue kallikrein) antibodies, but not by anti-alpha 1-antitrypsin serum, in Western-blot analyses. The results show that the kallikrein-binding protein is distinct from alpha 1-antitrypsin and is not identifiable with any of the well-characterized plasma proteinase inhibitors such as alpha 2-macroglobulin, inter-alpha-trypsin inhibitor, C1-inactivator or antithrombin III. The functional role of this kallikrein-binding protein and its impact on kallikrein activity or metabolism in vivo remain to be investigated.
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PMID:Identification of a new tissue-kallikrein-binding protein. 364 93

Characterization of muscarinic acetylcholine receptors in acinar cells from rat pancreas and lacrimal and parotid glands was achieved by binding of the reversible muscarinic antagonist [3H]quinuclidinyl benzilate (QNB) and the specific alkylating reagent [3H]propylbenzilylcholine mustard (PrBCM) to intact acini or dispersed acinar cells. Binding studies with [3H]QNB showed that acinar cells from pancreas contain 26,400, from parotid 21,400, and from lacrimal gland 25,700 binding sites/cell. To assess molecular size of the receptor in each gland, acini were prepared by digestion with purified collagenase and singly dispersed acinar cells were prepared by a combination of digestion with crude collagenase, hyaluronidase, and alpha-chymotrypsin and divalent cation chelation using EDTA. Muscarinic receptors on acini or dispersed cells were covalently labeled with 5 nM [3H]PrBCM, solubilized directly in hot sodium dodecyl sulfate buffer, and resolved by polyacrylamide gel electrophoresis. When solubilized acini were electrophoresed, a major labeled peak was observed on gels along with a smaller peak of lower apparent molecular weight. For pancreatic acini, the apparent molecular weights of these peaks were 117,600 and 85,700; for parotid acini, 104,800 and 74,500; and for lacrimal acini, 87,200 and 63,100. Addition of muscarinic antagonists to the labeling medium abolished both peaks. When dispersed acinar cells were labeled, the larger peak was eliminated, and all radioactivity was concentrated in a single peak: 87,600 for pancreas, 78,000 for parotid gland, and 62,800 for lacrimal gland. Digestion of prelabeled acini with the mixture of enzymes used to produce dispersed acinar cells similarly shifted all radioactivity into this second peak. Limited digestion of acini or dispersed cells with 1 mg/ml of papain resulted in the disappearance of these higher molecular weight peaks and the appearance of a broad peak at Mr = 40,000. Cells of nonepithelial origin, IM-9 lymphocytes and NG108 neuroblastoma X glioma hybrids, also were labeled with [3H]PrBCM and electrophoresed.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Muscarinic acetylcholine receptor structure in acinar cells of mammalian exocrine glands. 398 Apr 74

Neurite outgrowth in cultured neuroblastoma cells is inhibited in cells grown on a collagen substratum as compared to those grown on glass. Rapid, synchronized initiation of neurite outgrowth occurs after hydrolysis of the underlying collagen with collagenase. Axonated cultures exhibit an increased RNA and protein content as compared to cultures grown on collagen.
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PMID:Neuroblastoma: synchronization of neurite outgrowth in cultures grown on collagen. 434 Jul 59

Extracellular matrix proteins synthesized and secreted by adherent human tumor cell lines were analyzed using metabolic labelling with glycine and proline in the presence of ascorbate, polypeptide analysis and polyacrylamide gel electrophoresis, affinity chromatography, collagenase digestion, and immunofluorescence staining. The results showed a characteristic pattern of matrix proteins for each tumor cell type. Tumor cell lines of mesenchymal origin produced mostly interstitial types (I and II) of collagen and fibronectin. Carcinoma cell lines secreted only basement membrane proteins, type IV collagen, laminin and fibronectin, but not interstitial collagen. A melanoma and a rhabdomyosarcoma cell line produced type V of procollagen that has not previously been described in cell culture. Neuroblastoma cells were shown to be phenotypically heterogeneous also with respect to matrix protein production. We propose that the analysis of extracellular matrix proteins may serve as an adjunct in the classification of human tumors.
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PMID:Extracellular matrix proteins characterize human tumor cell lines. 627 24

The incorporation of methionine, lysine, and leucine into protein was studied in Ca2+-depleted and Ca2+-restored preparations of C-6 glial tumor cells in minimal medium. Although incorporation proceeded at linear rates in both preparations for more than 1 h and into the same spectrum of proteins, Ca2+-restored cells incorporated amino acid 5- to 10-fold more rapidly than Ca2+-depleted cells. Addition of approximately 200 microM Ca2+ in excess of chelator was required to achieve maximal rates of incorporation in Ca2+-depleted preparations. Stimulation by Ca2+ was rapid in onset (several minutes) and slowly reversible by chelator. Ca2+ was uniquely potent and specific among physiologically occurring cations in conferring such stimulation. Stimulation of amino acid incorporation by Ca2+ occurred over a broad range of pH and osmolarities and was facilitated by Mg2+. The effects of Ca2+ in stimulating amino acid incorporation were not traceable to changes in cAMP metabolism, amino acid uptake, protein catabolism, cell ATP or GTP content, or aminoacylation of transfer RNA. Actinomycin D (1 microgram/ml) did not block the stimulatory effects of Ca2+ although puromycin and cycloheximide did. The stimulatory effects of Ca2+ on protein synthesis were not restricted to C-6 in minimal medium. Protein synthesis was reduced by ethylene glycol bis(B-aminoethyl ether)-N,N,N',N'-tetraacetic acid 40 to 75% in C-6 glioma, GH3 pituitary tumor, PC-12 adrenal tumor, N2A neuroblastoma, and HeLa cells incubated under simulated growth conditions with various enriched media and sera. Ca2+-depleted S49 lymphoma, CHO ovarian tumor, and normal, dispersed chicken embryo cells in enriched medium responded to Ca2+ restoration with increased rates of protein synthesis as did collagenase-dispersed normal rat liver cells in minimal medium. Protein synthesis in rabbit reticulocyte lysates was also inhibited by Ca2+-selective chelators or by Ca2+ removal by parvalbumin affinity chromatography and the inhibition was reversed by Ca2+. These findings are consistent with the existence of a Ca2+ requirement in the translational phase of protein synthesis in eukaryotic cells.
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PMID:Identification of a Ca2+ requirement for protein synthesis in eukaryotic cells. 631 27


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