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Query: UMLS:C0027819 (neuroblastoma)
 27,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The continuous turnover of membrane phospholipids requires a steady supply of biosynthetic precursors. We evaluated the effects of decreasing extracellular Na+ concentration on phospholipid metabolism in cultured neuroblastoma (N1E 115) cells. Incubating cultures with 145 to 0 mM NaCl caused a concentration-dependent inhibition of [32P]phosphate uptake into the water-soluble intracellular pool and incorporation into phospholipid. Phospholipid classes were differentially affected; [32P]phosphate incorporated into phosphati-dylethanolamine (PE) and phosphatidylcholine (PC) was consistently less than into phosphatidylinositol (PI) and phosphatidylserine (PS). This could not be attributed to decreased phospholipid synthesis since under identical conditions, there was no effect on arachidonic acid or ethanolamine incorporation, and choline utilization for PC synthesis was increased. The effect of Na+ was highly specific since reducing phosphate uptake to a similar extent by incubating cultures in a phosphate-deficient medium containing Na+ did not alter the relative distribution of [32P]phosphate in phospholipid. Of several cations tested only Li+ could partially (50%) replace Na+. Incubation in the presence of ouabain or amiloride had no effect on [32P]phosphate incorporation into phospholipid. The differential effects of low Na+ on [32P]phosphate incorporation into PI relative to PC and PE suggests preferential compartmentation of [32P]phosphate into ATP in pools used for phosphatidic acid synthesis and relatively less in ATP pools used for synthesis of phosphocholine and phosphoethanolamine, precursors of PC and PE, respectively. This suggestion of heterogeneous and distinct pools of ATP for phospholipid biosynthesis, and of potential modulation by Na+ ion, has important implications for understanding intracellular regulation of metabolism.
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PMID:Compartmentation of phosphorylated precursors of phospholipid biosynthesis in cultured neuroblastoma cells. 311 15

To investigate the timing of inositol lipid turnover in relation to the cell cycle, inositol phosphates and lipids were measured in neuroblastoma (Neuro-2A) cells that were prelabeled with [3H]inositol and synchronized by a mitotic shakeoff technique. Distinct early and late phases of inositol phosphate production were identified. The early peak occurs between the 2nd and 4th hour after mitosis near the G1/S transition. A later peak occurs around the peak of S phase (DNA synthesis) at 7-8 h after mitosis. These findings suggest that activation of phosphatidylinositol turnover generates signals that play a role in cell cycle progression.
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PMID:Cell cycle dependence of inositol phosphate levels in neuroblastoma cells. 317 26

In vivo 31P-magnetic resonance spectra (MRS) were obtained by the surface coil method from rat glioma, human glioblastoma, and human neuroblastoma inoculated subcutaneously in CD Fisher rats and hamsters, and the effects of chemotherapy, photoradiation therapy, and radiofrequency hyperthermia as well as 60Co-irradiation were evaluated by sequentially observing spectral changes. In the 31P-spectra of tumour tissue, the nucleoside triphosphate (NTP), phosphomonoesters (PME) peaks were high and the phosphocreatine peak was low compared to those of normal brain. When the antitumour agents were given and were effective, NTP peaks decreased, and inorganic phosphate increased remarkably within several hours after the treatment. 1H-magnetic resonance imaging (MRI) were also obtained in some cases. Necrotic regions was detected by the 1H-MRI as image changes which appeared later than those detected by MRS. It proved practical to monitor the effect of therapy by employing either 31P-MRS or 1H-MRI. However, the image changes which demonstrated the effect of the therapy used closely resembled those changes which occurred with the onset of necrosis in tumour tissue during tumour growth. Several problems for future application of these techniques to human brain tumours are also mentioned.
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PMID:The investigation of experimental brain tumours using 31P-MRS and 1H-MRI. 321 41

1. The role of inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG) as possible mediators of the membrane current responses of NG108-15 neuroblastoma x glioma hybrid cells to bradykinin (BK, Brown & Higashida, 1988b) has been tested using intracellular ionophoresis of InsP3 and external application of phorbol dibutyrate (PDBu) and 1-oleoyl-2-acetylglycerol (OAG). 2. Intracellular ionophoresis of InsP3 into cells clamped at -30 to -50 mV produced (i) a transient outward current, (ii) a transient outward current followed by an inward current, or (iii) an inward current. All currents were accompanied by an increased input conductance. 3. The transient outward current reversed at between -80 and -90 mV. The reversal potential was shifted to more positive potentials on raising extracellular [K+], suggesting that it resulted from an increased K+ conductance. 4. The outward current was inhibited by apamin (0.4 microM) or d-tubocurarine (0.2-0.5 mM); these drugs also inhibit the outward current produced by BK or by intracellular Ca2+ injections (Brown & Higashida, 1988 a, b). The outward current was also slowly reduced in 0 mM [Ca2+] or 0.5 mM [Cd2+] plus 2 mM [Co2+] solution. 5. Ionophoretic injection of inositol 1,3,4-trisphosphate and inositol 1,3,4,5-tetrakisphosphate, guanosine trisphosphate or inorganic phosphate did not evoke an outward current but produced only an inward current with an increased conductance, reversing at between -10 and -20 mV. 6. Bath application of PDBu (10 nM-1 microM) or OAG (1-10 microM) produced an inward current with a fall in input conductance. The inward current was voltage dependent and was accompanied by an inhibition of the time-dependent current relaxations associated with activation or deactivation of the voltage-dependent K+ current, IM. 7. PDBu did not clearly reduce the Ca2+ current or the Ca2+-dependent K+ current recorded in these cells. During superfusion with PDBu, the outward current produced by intracellular ionophoresis of InsP3 was greatly enhanced. 8. The results support the view that the two membrane current responses to BK might both result from accelerated membrane phosphatidylinositide hydrolysis. One product, InsP3, releases Ca2+ and activates an apamin-curare-sensitive outward K+ current; this effect is imitated by intracellular InsP3 ionophoresis. The second product, DAG; activates protein kinase C to inhibit the voltage-dependent K+ current IM and generate an inward current; this effect is imitated by external application of PDBu or OAG.
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PMID:Inositol 1,4,5-trisphosphate and diacylglycerol mimic bradykinin effects on mouse neuroblastoma x rat glioma hybrid cells. 326 93

Immunological analysis is complementary of morphological analyses in the detection of neuroblastoma BM metastases. It attests the neuroblastic nature of rare pseudolymphocytic isolated cells. The combination of immunocytochemical technique (alkaline phosphate) and double-immunofluorescence technique allows the detection of as few as 10(-5) residual neuroblastoma cells. At the time of bone marrow harvest, it permits a precise evaluation of malignant cells in the graft.
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PMID:[Value of immunological analysis for the detection of residual neuroblasts in the bone marrow]. 328 77

Effects of pertussis toxin or cholera toxin on carbachol-stimulated inositol-1-phosphate ([3H]IP1) accumulation were studied using the human neuroblastoma cell line (SH-SY5Y). The maximal carbachol-stimulated [3H]IP1 accumulation in the SH-SY5Y cells was decreased from 51.4 fmol/10(6) cells to 42.4 fmol/10(6) cells (P less than 0.05) and 22.1 fmol/10(6) cells (P less than 0.01) in the absence and presence of 1 microgram/ml and 10 micrograms/ml pertussis toxin, respectively while the EC50 values did not change. Cholera toxin (1 mg/ml) did not alter carbachol-stimulated [3H]IP1 accumulation in these cells. These results suggest that a pertussis toxin sensitive G-protein may be involved in muscarinic receptor-phosphatidylinositol hydrolysis coupling in SH-SY5Y cells.
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PMID:Muscarinic receptor-mediated hydrolysis of phosphatidylinositols in human neuroblastoma (SH-SY5Y) cells is sensitive to pertussis toxin. 339 Jul 5

Purified brain tubulin subjected to an exhaustive phosphatase treatment can be rephosphorylated by casein kinase II. This phosphorylation takes place mainly on a serine residue, which has been located at the carboxy-terminal domain of the beta-subunit. Interestingly, tubulin phosphorylated by casein kinase II retains its ability to polymerize in accordance with descriptions by other authors of in vivo phosphorylated tubulin. Moreover, the V8 phosphopeptide patterns of both tubulin phosphorylated in vitro by casein kinase II and tubulin phosphorylated in vivo in N2A cells are quite similar, and different from that of tubulin phosphorylated in vitro by Ca/calmodulin-dependent kinase II. On the other hand, we have found an endogenous casein kinase II-like activity in purified brain microtubule protein that uses GTP and ATP as phosphate donors, is inhibited by heparin, and phosphorylates phosphatase-treated tubulin. Thus it appears that a casein kinase II-like activity should be considered a candidate for the observed phosphorylation of beta-tubulin in vivo in brain or neuroblastoma cells.
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PMID:Tubulin phosphorylation by casein kinase II is similar to that found in vivo. 347 37

A method for determining serum catecholamine metabolites such as vanillylmandelic acid (VMA), 3-methoxy-4-hydroxyphenyl glycol (MHPG) and homovanillic acid (HVA) in neuroblastoma by using high performance liquid chromatography and electrochemical detector is described. The separation of catecholamine metabolites was performed on a reverse phase column with an eluting system containing citric acid-potassium hydrogen phosphate buffer and methanol as the organic modifier. The experimental results showed that VMA and HVA levels in the serum of neuroblastoma patients were 15-30 times higher than that of the normal control group. The same phenomenon also occurred in patients with stage II neuroblastoma. Serum VMA, MHPG and HVA levels reduced to normal in patients suffering from neuroblastoma after surgery. Serum catecholamine metabolites analysed by using HPLC/ECD is more simple, sensitive and reliable than that by usual urine assay and might be used for the diagnosis of neuroblastoma even in early stage.
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PMID:Determination of serum catecholamine metabolites in neuroblastoma by high performance liquid chromatography with electrochemical detection. 350 18

Preclinical pharmacologic studies of caracemide [N-acetyl-N-(methylcarbamoyloxy)-N'-methylurea; CAR] have demonstrated a marked instability of this compound in the presence of either phosphate buffer (pH 7.4) or human plasma. Using [1-14C-acetyl]CAR and [3H-methylcarbamoyloxy]CAR, three CAR degradation products were identified: product A, N-(methylcarbamoyloxy)acetamide; product B: N-(methylcarbamoyloxy)-N'-methylurea; and product C: N-hydroxy-N'-methylurea. CAR degradation in human plasma was demonstrated by high-performance liquid chromatography (HPLC) to occur in a time- and temperature-dependent manner. A 30-min incubation (37 degrees) of CAR (10(-4) M) with human plasma resulted in degradation of more than 55% of parent compound; at 1 hr, more than 75% of original CAR was degraded. Incubation of [1-14C-acetyl]CAR with rat brain homogenate resulted in the formation of 14CO2. This reaction was partially inhibited by coincubation with physostigmine (10(-3) M). CAR inhibited acetylcholinesterase activity in neuroblastoma cells with an IC50 of 14 microM. In mechanism of action studies, CAR was found to inhibit ribonucleotide reductase activity but only at nine times the IC50 of hydroxyurea. In contrast to hydroxyurea, CAR was found to be non-cell-cycle phase-specific and non-cross-resistant with two CHO cell lines resistant to hydroxyurea. These data demonstrate the instability of CAR; moreover, they suggest that its mechanism of cytotoxicity is distinctly different from that of hydroxyurea and that the neurotoxicity associated with CAR administration may be caused in part by inhibition of acetylcholinesterase activity.
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PMID:Biochemical pharmacology of N-acetyl-N-(methylcarbamoyloxy)-N'-methylurea (caracemide; NSC-253272). 352 74

Serum-free cultured neuroblastoma cells (clone NlE-115) have been shown to absorb emulsified glucosylceramide, glucosylceramide glucosidase, an activator protein for the enzyme, and phosphatidylserine from a synthetic medium. Uptake of the enzyme was augmented by phosphatidylserine, and vice versa. Uptake of the enzyme-lipid complex was further augmented by the activator protein. It appears likely that the activator forms a complex only with the enzyme-lipid complex, not with the individual components. Two uptake mechanisms for the enzyme seem to be involved, one of which (the complex with activator proteins and acidic lipid) is sensitive to mannosyl phosphate groups. Hydrolysis of absorbed glucosylceramide was slow unless the medium was supplemented with the acidic phospholipid or glucosidase. The most rapid disappearance of stored glycolipid took place when the ternary mixture was added to the cell medium, enzyme + activator protein + phosphatidylserine. These findings may be relevant to enzyme replacement therapy for Gaucher disease.
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PMID:Uptake by neuroblastoma cells of glucosylceramide, glucosylceramide glucosidase, its stimulator protein, and phosphatidylserine. 373 Apr 7


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