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)

We have previously shown that the [3H]saxitoxin binding site of the sodium channel is expressed independently of the [125I]scorpion toxin binding site in chick muscle cultures and in rat brain. In the present work, we studied the development of the sodium channel protein during chemically induced differentiation of N1E-115 neuroblastoma cells, using [3H]saxitoxin binding, [125I]scorpion toxin binding, and 22Na uptake techniques. When grown in their normal culture medium, these cells are mostly undifferentiated, bind 90 +/- 10 fmol of [3H]saxitoxin/mg of protein and 112 +/- 14 fmol of [125I]scorpion toxin/mg protein, and, when stimulated with scorpion toxin and batrachotoxin, take up 70 +/- 5 nmol of 22Na/min/mg of protein. Cells treated with dimethyl sulfoxide (DMSO) or hexamethylene-bis-acetamide (HMBA) differentiate morphologically within 3 days. At this time, the [3H]saxitoxin binding, the [125I]scorpion toxin binding, and the 22Na uptake values are not very different from those of undifferentiated cells. With subsequent time in DMSO or HMBA, these values continue to increase, a result indicating that the main period of sodium channel expression occurs well after the cells have assumed the morphologically differentiated state. The data indicate that the expression of sodium channels and morphological differentiation are independently regulated neuronal properties, that the attainment of morphological differentiation is necessary but not in itself sufficient for full expression of the sodium channel proteins, and that, in contrast to the chick muscle cultures and rat brain, the [3H]saxitoxin site and [125I]scorpion toxin site appear to be coregulated in N1E-115 cells.
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PMID:Development of sodium channel protein during chemically induced differentiation of neuroblastoma cells. 243 20

Differentiation of N1E-115 neuroblastoma cells into neuron-like cells, with extension of neurites and acquisition of excitable membranes, can be induced by dimethyl sulfoxide (DMSO). We have found this differentiation to be accompanied by an increase in tyrosine hydroxylase (TH) mRNA, an increase disproportionate to changes in mRNAs for other measured, non-neuron-specific genes. The mRNA increases slowly over several days and falls gradually after removal of DMSO. Nuclear run-on studies suggest that a change in the rate of transcription cannot explain the increase in steady-state mRNA levels. TH mRNA half-life does, however, increase. This suggests that regulation is exerted in this case not at the level of transcription but rather at that of mRNA stability.
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PMID:Regulation of tyrosine hydroxylase gene expression during differentiation of neuroblastoma cells. 288 36

The surface charge of neuroblastoma cells in different phases of the cell cycle was studied by the microelectrophoresis method. The surface charge increased by 50% on the average after addition of colchicine to the culture medium, by 20-30% after addition of dibutyryl-cAMP or removal of the serum from the medium and decreased by 30% after addition of DMSO. These changes correlated well with variations of the protein content per cell.
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PMID:[Relation between the surface potential of mouse neuroblastoma clone C1300 cells and the phase of the cell cycle]. 303 25

Murine erythropoiesis represents a favourable system in which to investigate the coordinate regulation of gene expression due to the availability of erythroid precursor cells at various stages of differentiation. In this report, we investigate the biosynthesis and cell specificity of two characteristic murine RBC membrane glycoproteins that resemble the human RBC glycophorins: a major component of apparent molecular mass 31 kD (glycophorin MA) and a minor 46 kD component (glycophorin MB). Both glycophorins bind to wheat germ lectin and share a common protein antigenic determinant recognised by a monoclonal antibody (GP 29.4), but they differ significantly in their carbohydrate components: whilst both glycophorins contain mainly O-linked sugars, glycophorin MA contains in addition at least one N-linked carbohydrate residue and terminal sialic acid residues. Pulse-chase in vivo labelling experiments combined with in vitro translations of glycophorin mRNAs show that the initial precursor to glycophorin MA is a 24.5 kD polypeptide which is subsequently processed and glycosylated to give the mature 31 kD molecule via a 21.5 kD polypeptide intermediate. Both glycophorins MA and MB are synthesized most actively in early to mid erythroblasts (e.g., Friend cells induced for 3 days with DMSO) but their synthesis is considerably reduced by the reticulocyte stage. However, of the other cell types tested (neuroblastoma, myeloma, fibroblasts, epithelial cells and T-lymphoma cells), none synthesizes glycophorin with the possible exception of a low level in thymus tissue. Thus murine glycophorins, in contrast to the RBC cytoskeletal proteins (spectrin, ankyrin, band 4.1) seem to be restricted to the erythroid cell lineage like human glycophorin.
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PMID:The cell specificity and biosynthesis of mouse glycophorins studied with monoclonal antibodies. 385 53

Giga-ohm seal whole cell recording technique was used to examine ionic currents changes induced by dimethylsulfoxide (DMSO) in neuroblastoma X glioma hybrid NG 108-15 cells. DMSO (0.5-1%) reversible blocks sodium, potassium and calcium currents and shifts by about 6 mV the sodium inactivation curve towards more negative voltages.
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PMID:Effects of dimethylsulfoxide on membrane currents of neuroblastoma x glioma hybrid cell. 395 50

It has been shown that agents that are known to be scavengers of hydroxyl radicals may induce differentiation and inhibit growth of murine neuroblastoma cells in tissue culture. The present study tests dimethyl sulfoxide as a differentiation agent of the human neuroblastoma cell lines LA-N-1 and murine neuroblastoma NIE-115. Results indicate that DMSO induces morphologic and biochemical differentiation of neuroblastoma cells coupled to growth inhibition and inhibition of colony formation in semi liquid tissue culture systems. DMSO treatment in vitro had no effect on tumorigenicity of NIE-115 cells. In vivo DMSO treatment of athymic nude mice with transplanted LA-N-1 human neuroblastoma tumors has not affected tumor size or animal survival. No diminishing effect of natural killer cell activity could be attributed to DMSO treatment.
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PMID:Dimethyl sulfoxide-induced differentiation does not alter tumorigenicity of neuroblastoma cells. 399 89

Neuroblastoma cells serve as a useful model of neuronal development because compounds such as dimethyl sulphoxide (DMSO) and dibutyryl cyclic AMP cause them to undergo a process of controlled differentiation in tissue culture, during which they can extend long processes, develop characteristic excitability mechanisms, synthesize neurotransmitters and form synapses. We have used the technique of fluorescence photobleaching recovery to study the lateral mobility of cell-surface constituents during the differentiation of neuroblastoma clone N1E-115 cells. The concanavalin A (Con A) binding sites appear as discrete patches distributed over the entire cell surface and exhibit lateral mobility in undifferentiated cells comparable with that of surface glycoproteins of other cells. After induction of differentiation, however, the vast majority of Con A binding sites become immobilized, and we present data which suggest that the mechanism of this immobilization may involve linkage to the internal actin network.
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PMID:Immobilization of concanavalin A receptors during differentiation of neuroblastoma cells. 626 Nov 53

The expression of a adenosine cyclic 3':5'-monophosphate (cAMP)-binding protein, regulatory subunit of the type I cAMP-dependent protein kinase (Rl), and its functional significance in the differentiation of N-18 mouse neuroblastoma cells were examined. 8-Azidoadenosine cyclic 3':5'-[32P]monophosphate, a photoaffinity-labeling analog of cAMP, and high-resolution sodium dodecyl sulfate-polyacrylamide gel electrophoresis were used to identify and quantitate cAMP-binding proteins in cell extracts. The induction of differentiation of N-18 mouse neuroblastoma cells, initiated either by adding dibutyryl adenosine cyclic 3':5'-monophosphate to the growth medium or by culturing cells in medium supplemented with 1% fetal calf serum, led to a 3-fold increase in the amount of 8-azidoadenosine cyclic 3':5'-[32P]monophosphate incorporated into Rl, when assayed in vitro. This increased incorporation was attributable to an increase in the amount of Rl rather than to an increase in the affinity of Rl for 8-azidoadenosine cyclic 4':5'-[32P]monophosphate. The subunit molecular weight, isoelectric point, and immunoreactivity of Rl were found to be identical to that of the regulatory subunit of the type I cAMP-dependent protein kinase purified from bovine skeletal muscle. The increase in Rl was not accompanied by an increase in the cAMP-dependent protein kinase activity. DEAE-cellulose column chromatography confirmed the induction of Rl as a free cAMP-binding protein in the differentiated neuroblastoma cells. The possibility of a growth-dependent regulation of Rl was also examined. Addition of 2% dimethyl sulfoxide to cultures of N-18 mouse neuroblastoma cells inhibited cell growth without increasing the specific activity of Rl. Dimethyl sulfoxide had no effect on neurite outgrowth or acetylcholinesterase activity, two parameters characteristic of differentiated cells. The fact that the induction of Rl coincided with differentiation of the neuroblastoma cells suggests that the expression of Rl may be used as a biochemical index of differentiation in these cells. The presence of a free cAMP-binding protein, not associated with cAMP-dependent protein kinase in neuroblastoma cells, raises important considerations concerning the action of cAMP in the regulation of growth and differentiation.
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PMID:Induction of the regulatory subunit of type I adenosine cyclic 3':5'-monophosphate-dependent protein kinase in differentiated N-18 mouse neuroblastoma cells. 627 81

Morphological features of neuroblastoma cells cultured in the presence of 1.0% dimethyl sulfoxide (DMSO) were investigated. The induced differentiation was characterized by appearance of long axon-like processes (neurites), cell size enlargement and inhibition of cell growth. Quantitative criteria for cell differentiation depending on survival time in the modified medium were estimated. The increase of total length of neurites was linear with time, the rate of their extension being 20.0 +/- 3 micron/h. The area of differentiated cell soma is 6-7 times higher than that of control cells. Increase of the DMSO concentration to 2.0% did not intensify neurite growth and enlargement of cell size but suppressed mitosis. Morphological criteria of cell differentiation are compared with probable functional changes in these cells.
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PMID:[Morphologic differentiation of neuroblastoma cells induced by dimethyl sulfoxide]. 649

The relative amounts of the different enolase isozymes present in neuroblastoma cells change during differentiation. When differentiation is induced by low serum in the presence of DMSO (dimethyl sulfoxide), there is a 50% decrease in the concentration of enolase activity associated with the form alpha alpha, and an increase in the activity associated with the gamma-containing isozymes (alpha gamma plus gamma gamma); in the absence of DMSO, there is no decrease in alpha alpha or in total enolase activity. In order to study the mechanism of the changes in alpha alpha, cells differentiated with low serum with and without DMSO were compared. Measurements of the concentration of the alpha antigen by microcomplement fixation and by immunotitration demonstrate that the decreased enolase activity in DMSO cells is due to a decreased concentration of the alpha antigen. Measurements of the relative rate of synthesis of the antigen show that the decreased concentration of the alpha antigen is due to a decreased rate of synthesis. Enolase in differentiated cells is sufficiently stable (t1/2 greater than 100 h) that a comparison of the relative rates of degradation has not been possible. The decreased synthesis of the alpha subunit of enolase that occurs under these conditions appears to be a useful model system for studying the de-expression of the alpha gene that occurs in vivo during neuronal differentiation.
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PMID:Changes in the expression of the alpha alpha form of enolase during neuroblastoma differentiation. 664 99


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