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)

Platelet aggregating activity of the NCG human neuroblastoma cell line was compared with that of the HL-60 human promyelocytic leukemia cell line. NCG, in intact cell suspensions and ultracentrifuged pellets, induced platelet aggregation most significantly in heparinized platelet rich plasma (PRP) containing 2.5 units/ml of heparin, but not in the presence of higher concentrations of heparin or 5 mM ethylenediamine-tetraacetate or in citrated PRP. NCG induced platelet aggregation was also inhibited by hirudin or (2R,4R)-4-methyl-1-[N2-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulfon yl)-L- arginyl]-2-piperidinecarboxylic acid (MD 805) in the same manner as that of tissue thromboplastin induced platelet aggregation. HL-60 cells did not induce platelet aggregation in our heparinized PRP assay systems; however, after treatment with neuraminidase HL-60 cells became active in aggregating platelets in either heparinized or citrated PRP. NCG demonstrated high procoagulant activity by either intact cell suspensions or ultracentrifuged pellets. The procoagulant activity of NCG was reduced in Factor VII deficient human plasma as it was in the results obtained by tissue thromboplastin. These results suggest that NCG induces platelet aggregation via thrombin generated through procoagulant activity which is shed in association with microvesicles demonstrated in the ultracentrifuged pellets. This type of platelet aggregating activity found in NCG is significantly different from that of HL-60.
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PMID:Platelet aggregating activity mediated by thrombin generation in the NCG human neuroblastoma cell line. 382 2

During a Phase I study of intravenous vitamin E-free alcohol (all-rac-alpha-tocopherol or Ephynal) in patients with neuroblastoma, we noticed a bleeding diathesis in two patients receiving 2300 mg/m2 daily for four or more days in succession. Both blood prothrombin time and accelerated partial thromboplastin times were prolonged. These spontaneously returned to normal levels three days after interrupting vitamin E infusions. It was also noted that factors VII, IX and X were decreased, which corresponded with the prolonged PT and APTT. It was found that by infusing menadiol sodium diphosphate just prior to the vitamin E, these inhibiting effects on procoagulant factors could be abrogated and high dosages of vitamin E-free alcohol safely given.
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PMID:The effect of intravenous vitamin E and menadiol sodium diphosphate on vitamin K dependent clotting factors. 647 8

Some tumor cells induce platelet aggregation in the bloodstream, which has been implicated in tumor metastasis. In this study, we investigated the mechanism of platelet aggregation induced by a human neuroblastoma cell line, GOTO. It was revealed that GOTO cells had tissue factor on their surface and converted factor X (FX) to FXa with the aid of factor VIIa. The produced FXa formed prothrombinase complex on the cells and activated prothrombin. From experiments on activity inhibition by specific monoclonal as well as polyclonal antibodies, it was concluded that factor V did not constitute this prothrombinase complex. Another cofactor known to constitute prothrombinase complex on some cells, effector cell protease receptor-1 (EPR-1), was not expressed on GOTO cells, suggesting that the cofactor composing FXa-dependent prothrombinase activity on GOTO cells is not factor V or EPR-1 but, rather, is an unknown molecule. Upon the culturing in the presence of 5-bromo-2'-deoxyuridine for 4 days, GOTO cells differentiated into Schwann-like cells, and both FXase and prothrombinase activities were greatly diminished. Flow cytometric analyses revealed that the decrease of FXase activity should be attributed to the decrease of tissue factor expression on GOTO cells. Because these activities greatly diminished upon cellular differentiation, the expression of both cofactor molecules may be related to the malignant and metastatic nature of the tumor cells.
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PMID:Factor X-dependent, thrombin-generating activities on a neuroblastoma cell and their disappearance upon differentiation. 936 54