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)

Both polyvalent and hybridoma-produced antibodies to fibronectin (Fn) were used to 'map' the immunoaccessible subsets of cell surface fibronectin on virus-transformed murine fibroblast SVT2 and rat neuroblastoma B104 cells. As one approach to this end, attachment and spreading responses of cells were measured on tissue culture substrata coated with antibody or with plasma fibronectin to compare their adhesive responses. Both SVT2 and B104 cells adhere poorly to polyvalent anti-Fn-coated substrata over short time intervals, but within several hours changes occur which permit cells to attach and spread as well on anti-Fn as on Fn (post-adsorption of the anti-Fn with Fn also generates a maximal response). This adhesive response could be completely prevented by predigesting the cells with Flavobacterium heparanase, but not with chondroitinase ABC, indicating that the cell surface Fn responsible for antibody-mediated adhesion is associated with heparan sulfate proteoglycans on the cell surface. The compositions of the substratum-attached material (left bound after EGTA-mediated detachment of cells) from cells attaching to anti-Fn or Fn were analysed by SDS-PAGE and found to be identical within the same cell type for the two different substrata. Three hybridoma-produced antibodies, which recognize different determinants on Fn, generated different adhesive responses for SVT2 or B104 cells when adsorbed to the substratum. SVT2 cells adhered well to antibody no. 32-coated substrata but poorly to antibodies 92 or 136; on the other hand, B104 cells responded similarly to all three antibodies over short times of attachment but much better to no. 32 after a several hour incubation. These experiments indicate that (1) much of the cell surface fibronectin is complexed with heparan sulfate proteoglycan and is initially inaccessible to bind to polyvalent antibody on the substratum to promote adhesion; (2) the surface of neuroblastoma cells contains a fibronectin-like molecule which is important in their substratum adhesion; and (3) monoclonal antibodies are valuable tools in 'mapping' the orientation of cell surface molecules like fibronectin by measuring adhesive responses to antibody-coated substrata.
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PMID:Adhesive responses of fibroblast and neuroblastoma cells to substrata coated with polyvalent or monoclonal antibody to fibronectin. 686 9

Vindesine, a semisynthetic derivative of vinblastine sulfate, was tested for antitumor activity and clinical toxicity in 36 children. The drug was administered to the initial 13 patients entered into the study a 2 mg/m2/day for five days by IV bolus. Because of severe neurotoxicity and life-threatening gastrointestinal toxicity, the regimen in 23 patients was modified to 4mg/m2 IV infusion over four hours, weekly. This latter regimen was well tolerated, with acceptable gastrointestinal, hematological, and neurotoxicity. One child with acute lymphocytic leukemia resistant to vincristine had a transient M1 remission bone marrow. Improvement or stable disease was noted in one patient each with Ewing's sarcoma, neuroblastoma, and Hodgkin's disease.
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PMID:Vindesine: a phase II study in childhood malignancies-a report for cancer and leukemia group B. 703 20

Newts with bilaterally amputated forelimbs were exposed to either continuous light (LL), total darkness (DD), or continuous light with the dorsal head epithelium painted with an India ink and Nile blue sulfate mixture (LL-II-NBS) that limited light penetration through the skull to the pineal. The LL-II-NBS animals regenerated their forelimbs more slowly then their counterparts in LL.
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PMID:The effect of limiting light to the pineal on the rate of forelimb regeneration in the newt. 707 56

A patient with olfactory neuroblastoma who had bone marrow metastasis at the time of diagnosis is presented. Previous therapy for this disease consisted of surgery and radiation. There is limited information relating to the efficacy of chemotherapy. Our patient was treated with combination chemotherapy (dacarbazine [DTIC-Dome], cyclophosphamide [Cytoxan], doxorubicin hydrochloride [Adriamycin], and vincristine sulfate [Oncovin]) and radiation to the primary site. Objective findings, more than two years after diagnosis, support a good partial response. Although a 50%, five-year survival time has been reported, the five-year cure rate is 18%. This report suggests that the role of combination chemotherapy should be further evaluated in certain patients with olfactory neuroblastoma.
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PMID:Olfactory neuroblastoma. Response to combination chemotherapy. 736 26

The amount of tubulin in a clone of neuroblastoma cells (Nb2a-AB-1) which undergoes microtubule-dependent neurite elongation has been determined. This clone undergoes shape differentiation without cessation of cell division, and both differentiated and nondifferentiated cells have the same cell cycle parameters. To quantitate tubulin pools, a radioimmunoassay was developed with a rabbit serum raised to sodium dodecyl sulfate-treated Tetrahymena axonemal tubulin. Using purified hog brain tubulin as labeled tracer and competitor, competition curves covering the range of 0.1 to 100 microgram/ml were obtained. Curves obtained using purified mouse brain or neuroblastoma tubulin as competitors were similar to those obtained with hog brain tubulin. The levels of competition obtained with hog tubulin, partially purified tubulin, or fixed microtubules were identical, indicating that the polymerization state of tubulin had no effect on measurements. Postmitochondrial supernatants derived either from cells grown in suspension culture (rounded morphology) or monolayer culture (neurite-bearing morphology) contained equivalent amounts of tubulin (3.6 +/- 0.5 pg/cell and 3.1 +/- 0.2 pg/cell, respectively); tubulin constituted 2.7% of the postmitochondrial supernatant protein in either cell type. These data indicated that cells utilizing microtubules primarily for mitosis or for cytoskeletal functions and mitosis show no net change in the total soluble tubulin pool.
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PMID:The quantitation of tubulin in neuroblastoma cells by radioimmunoassay. 743 Jan 49

Congo red and certain sulfated glycans are potent inhibitors of protease-resistant PrP accumulation in scrapie-infected cells. One hypothesis is that these inhibitors act by blocking the association between protease-resistant PrP and sulfated glycosaminoglycans or proteoglycans (e.g., heparan sulfate proteoglycan) that is observed in amyloid plaques of scrapie-infected brain tissue. Accordingly, we have investigated whether the apparent precursor of protease-resistant PrP, protease-sensitive PrP, binds to Congo red and heparin, a highly sulfated glycosaminoglycan with an inhibitory potency like that of heparan sulfate. Protease-sensitive PrP released from the surface of mouse neuroblastoma cells bound to heparin-agarose and Congo red-glass beads. Sucrose density gradient fractionation provided evidence that at least some of the PrP capable of binding heparin-agarose was monomeric. Free Congo red blocked PrP binding to heparin and vice versa, suggesting that these ligands share a common binding site. The relative efficacies of pentosan polysulfate, Congo red, heparin, and chondroitin sulfate in blocking PrP binding to heparin-agarose corresponded with their previously demonstrated potencies in inhibiting protease-resistant PrP accumulation. These results are consistent with the idea that sulfated glycans and Congo red inhibit protease-resistant PrP accumulation by interfering with the interaction of PrP with an endogenous glycosaminoglycan or proteoglycan.
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PMID:Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]. 751 Nov 69

The Alzheimer amyloid precursor (APP) protein is a member of a family of glycoproteins that includes the amyloid precursor-like proteins (APLPs). Previously, we showed that in C6 glioma cell cultures, secreted APP nexin II occurs as the core protein of a chondroitin sulfate proteoglycan (CSPG). Here, we report that among seven untransfected cell lines, expression of secreted APP CSPG was restricted to two cell lines of neural origin, namely, C6 glioma and Neuro-2a neuroblastoma (N2a) cells. Addition of dibutyryl cyclic AMP in N2a cultures, a treatment that induces the neuronal phenotype in these cells, resulted in a significant reduction in the amount of the secreted APP CSPG, although secretion of APP was only marginally affected. Growth in the presence of serum increased the size of the secreted APP CSPG, suggesting that the number and/or length of the chondroitin sulfate (CS) chains attached to the core APP varies with growth conditions. Extensive mapping with epitope-specific antibodies suggested that a CS chain is attached within or proximal to the A beta sequence of APP. In contrast to the restricted expression of the APP CSPG, expression of secreted APLP2 CSPGs was observed in all cell lines examined. After chondroitinase treatment, two core proteins of approximately 100 and 110 kDa were obtained that reacted with an APLP2-specific antiserum, suggesting that non-transfected cell lines contain at least two endogenous APLP2 CSPGs, probably derived by alternative splicing of the APLP2 KPI domain. The fraction of the APLP2 proteins in the CSPG form was dependent on the particular cell line examined.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Expression of the chondroitin sulfate proteoglycans of amyloid precursor (appican) and amyloid precursor-like protein 2. 761 33

In this study, the in situ phosphorylation and subsequent calcium-activated proteolysis of tau protein were examined in human neuroblastoma (LA-N-5) cells, which were differentiated into a neuronal phenotype. The phosphorylation of tau was increased by treating the cells with forskolin and rolipram, which elevate cyclic AMP levels, by treating with the phosphatase inhibitor okadaic acid, or by treating with a combination of both treatments. Phosphorylated tau migrated slightly slower on sodium dodecyl sulfate-polyacrylamide gels than tau from untreated cells. Immunostaining with the phosphate-sensitive monoclonal antibody Tau-1 was also decreased in cells treated with okadaic acid, indicating an increase in the phosphorylation of specific Ser-Pro motifs within the molecule. Calcium-dependent, in situ proteolysis of tau protein was induced by treating the cells with the calcium ionophore A23187. Tau protein was proteolyzed to a significantly lesser extent in cells treated with forskolin and rolipram, okadaic acid, or both than in cells in which phosphorylation was not increased. Partially purified tau protein from cells treated with a combination of forskolin, rolipram, and okadaic acid was also more resistant to proteolysis by calpain in vitro compared with tau isolated from control cells. These data suggest a possible role for phosphorylation in the regulation of tau metabolism and in pathological conditions in which the balance between protein kinases and phosphatases is disrupted.
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PMID:Phosphorylation of tau in situ: inhibition of calcium-dependent proteolysis. 761 52

Inflammation and the response to injury may play an important role in the process of amyloidosis in Alzheimer's disease. We investigated the effect of interleukin-1 (IL-1) and nerve growth factor (NGF) on the metabolism of neuroblastoma proteoglycans. IL-1 and NGF increased the net charge and the net secretion of neuroblastoma proteoglycans. NGF also specifically increased the relative amount of cell-associated and secreted heparan sulfate proteoglycans in these cells. We previously demonstrated that neuroblastoma heparan sulfate proteoglycan binds specifically to the amyloid beta-amyloid peptide involved in Alzheimer's disease. Heparan sulfate glycosaminoglycans synthesized by IL-1-stimulated cells demonstrated an increased relative binding affinity for the beta-amyloid peptide. Thus, IL-1 and NGF induce the hypersecretion and hypersulfation of neuroblastoma heparan sulfate proteoglycans which bind beta-amyloid. These studies link the process of inflammation and repair with alterations in the metabolism of heparan sulfate proteoglycans and amyloid formation in Alzheimer's disease and other disorders.
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PMID:Interleukin-1 and nerve growth factor induce hypersecretion and hypersulfation of neuroblastoma proteoglycans which bind beta-amyloid. 764 43

Recent studies showed that the Alzheimer amyloid precursor (APP) occurs as the core protein of a chondroitin sulfate proteoglycan (appican) in C6 glioma cells. In the present study we show that appican is present in both human and rat brain tissue. Cortical rat brain cell cultures were used to identify appican-producing cells. Soluble secreted and cell-associated appican was produced by mixed glial cultures but not by primary neuronal cultures. Among the three major glial cell types, astrocytes produced high levels of appican, while oligodendrocytes failed to produce any. Only low levels of this molecule were occasionally detected in microglial cultures. Expression of appican in astrocyte cultures was regulated by the composition of the growth media. N2a neuroblastoma cells also produced appican; however, treatment with dibutyryl cAMP which promotes neuronal differentiation in these cells inhibited its production without inhibiting synthesis of APP. In contrast to the restricted expression of appican, APP was present in all cultures, and its production was independent of appican synthesis. Neuronal cultures produced mainly APP695 while glial cultures produced the Kunitz type protease inhibitor containing APP. The astrocyte-specific expression of appican suggests a function distinct from the function of APP. Brain appicans may play a role in the development of Alzheimer disease neuropathology.
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PMID:The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures. 774 33


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