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)

Recently the authors have identified a major component of Rosenthal fibers as alpha B-crystallin, a major lens protein. In the current study the authors investigated the expression of alpha B-crystallin in four cultured glioma cell lines and in 115 human neuroectodermal tumors. alpha B-crystallin was expressed differentially by those glioma cell lines, but not by neuroblastoma cell lines. Northern blot analysis revealed two distinct messages for alpha B-crystallin in C-6, whereas only a single message in U-373MG and G26-24. In human surgical specimens positive immunostaining was frequently observed in the following brain tumors: pilocytic astrocytoma of the juvenile type, anaplastic astrocytoma, glioblastoma multiforme, and subependymal giant cell astrocytoma. The astrocytic elements of mixed oligoastrocytomas, glioblastomas with sarcomatous components, and gangliogliomas were likewise strongly stained. In contrast, little immunoreactivity was observed in ependymal and choroid plexus tumors. Thus, alpha B-crystallin is mainly expressed by astrocytic tumors among neuroectodermal neoplasms, without regard to the presence of Rosenthal fibers.
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PMID:Preferential expression of alpha B-crystallin in astrocytic elements of neuroectodermal tumors. 165 7

The distribution of the glial fibrillary acidic protein (GFAP) was investigated in sections of 131 paraffin-embedded brain neoplasms obtained at surgery or at autopsy. The unlabeled antibody immunoperoxidase (peroxidase-antiperoxidase, PAP) method was used. Equally good results were obtained from 17-year-old material and from recent material derived at surgery or autopsy and fixed with Bouin fluid or phosphate-buffered formalin. The perikaryons and processes of reactive astrocytes showed the most intense stain for GFAP. Positive reaction to antibody against GFAP of varying intensity was demonstrated in astrocytomas of various grades of malignancy (32 of 32), glioblastoma multiforme (10 of 10), subependymal giant cell astrocytoma (1 of 1), ependymoma (2 of 10), subependymoma (4 of 4), and astrocytes in mixed neoplasms (8 of 8). In two neoplasms diagnosed as malignant astrocytomas and in four neoplasms diagnosed as glioblastoma multiforme, GFAP stain was limited to a few neoplastic cells. Usually the stain was more intense over processes than in perikaryons, with the exception of gemistocytic astrocytomas and the giant cells in glioblastoma multiforme, which showed an equally intense stain over perikaryons and processes. The periphery of Rosenthal fibers was intensely positive for GFAP. In astrocytic neoplasms the number of GFAP-positive cells and the intensity of the stain were inversely proportional to the degree of malignancy. In the following neoplasms the reaction for GFAP was negative: oligodendroglioma (3), oligodendroblastoma (1), medulloblastoma (3), medulloepithelioma (1), neuroblastoma (1), pineocytoma (1), typical teratoma of the pineal (1), fibrosarcoma (1), pituitary adenoma (2), craniopharyngioma (1), chordoma (1), chemodectoma of globus jugulare (1), metastatic carcinoma (17), and lymphoma (8). In one of 18 meningiomas, endogenous peroxidase activity was seen in mast cells. All meningiomas studied were negative for GFAP. In one of six neurinomas a positive reaction for GFAP was detected over processes. The authors concluded that the immunostain for GFAP is useful in the diagnoses of astrocytic neoplasms and of mixed gliomas.
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PMID:Immunocytochemical study of the glial fibrillary acidic protein in human neoplasms of the central nervous system. 628 Nov 68

It is known that NGF-responsive cells bind NGF at cell surface receptors in a specific and saturable fashion and there are two separate kinds of receptor-ligand binding interactions as judged by Rosenthal analyses. Following isolation of nerve growth factor receptors from embryonic chicken sensory ganglia, rat pheochromocytoma cells and human neuroblastoma cells, equilibrium binding studies were carried out and two different equilibrium binding constants similar to that described for whole cells were determined. This evidence is consistent with the hypothesis that there are two different receptors for NGF which have been conserved.
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PMID:Binding constants of isolated NGF-receptors from different species. 631 Dec 10

The binding characteristics of dihydroartemisinin to neural tissues and cells in culture were studied by incubating differentiating C6 and NB2a cells and rat cerebral cortex homogenate with 1 to 200 microM 14C-labelled dihydroartemisinin with or without 2 microM haemin for 24 h. The role of protein thiol and amine groups in dihydroartemisinin binding was assessed by pre-incubation of the cortex homogenate with sodium cyanate and/or iodoacetamide. Rosenthal plots of binding data demonstrated that there were two discrete phases of dihydroartemisinin binding. Haemin increased the total binding of dihydroartemisinin to both cortex and cell proteins. In each preparation, haemin increased Bmax of the high affinity binding sites and also increased kD of NB2a high affinity binding sites and decreased kD of cortex low affinity binding sites. The effects of haemin on the binding parameters of cortex resembled its effects on C6 cells rather than NB2a cells. NB2a high and low affinity binding sites had a greater affinity for dihydroartemisinin than those of either rat cortex or C6 cells. Iodoacetamide and sodium cyanate reduced binding to cortex proteins by approximately 70%. Co-incubation of 14C-dihydroartemisinin with arteether reduced binding of dihydroartemisinin but co-incubation with desoxyartemisinin did not. These studies demonstrate that the known haemin-induced increase in toxicity of dihydroartemisinin to differentiating neuroblastoma cells is accompanied by a corresponding increase in dihydroartemisinin binding to cell proteins, that protein thiol and amine groups react with the products of the reaction between dihydroartemisinin and haemin and point to a relationship between the toxicity of artemisinin derivatives and protein binding.
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PMID:Binding of dihydroartemisinin to differentiating neuroblastoma cells and rat cortical homogenate. 962 46