Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

By using a lectin-based screening method for cell-dependent variations of O-glycosylation of viral glycoprotein, we found that O-linked oligosaccharides of herpes simplex virus type 1 (HSV-1) glycoproteins in virus-infected mouse neuroblastoma (C1300) cells differed from those of HSV glycoproteins produced in other cells. Thus, O-linked oligosaccharides of HSV-1-specified glycoprotein C (gC-1), produced in GMK cells and a number of other cells, occurred mainly as trisaccharides or larger structures. In contrast, gC-1, produced in C1300 cells, contained O-linked monosaccharides and very few, if any, larger oligosaccharides of this class. A structural comparison between O-linked oligosaccharides of gC-1 from HSV-1-infected C1300 cells and from GMK cells showed that biosynthesis was interrupted prior to formation of a core disaccharide with terminal galactose, indicating a major early defect in O-glycosylation of glycoproteins in C1300 cells. A comparison of the content of galactosyltransferases between C1300 and GMK cells showed that C1300 cells lacked galactosyltransferases, including the specific enzyme engaged in formation of the core O-linked disaccharide mentioned, while other glycosyltransferases adding terminal sugars to O-linked oligosaccharides were present in equal amounts in both cell lines. These results indicated that HSV-1 is strictly dependent on host cell-specified factors for biosynthesis of O-linked oligosaccharides associated with viral glycoproteins.
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PMID:Host cell-induced differences in the O-glycosylation of herpes simplex virus gC-1. II. Demonstration of cell-specific galactosyltransferase essential for formation of O-linked oligosaccharides. 282 13

Recently a glycoprotein capable to induce tetrodotoxin-sensitive sodium permeability being incorporated to liposomes was purified from the cytoplasm of the bovine brain. It is shown that a monoclonal antibody derived against this protein binds intact murine neuroblastoma cells. Veratrine, neurotoxin referred to modulate the activity of voltage-gated sodium channels, is shown to compete with the antibody for the neuroblastoma surface epitope. It is postulated that molecular moiety bound with the antibody is either identical or spatially related to veratrine (veratridine) binding site.
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PMID:[Monoclonal antibodies to cytoplasmic tetrodotoxin-sensitive brain protein. The effect of veratrine on antibody binding to neuroblastoma cells]. 285 83

The expression of eight serologically and biochemically distinct human cell surface antigens defined by monoclonal antibodies was examined on a panel of rodent-human somatic cell hybrids. Cosegregation was observed for human chromosome 11, and surface expression of all eight antigens was studied. Serological analysis of hybrids containing defined segments of human chromosome 11 permitted the regional assignment of genes controlling antigens JF23 (90 kD glycoprotein), G344 (25 kD), T43 (85 kD), A124, and NP13 to chromosome 11pter-q13, and of genes controlling Q14 (130 kD), MC139 (35 kD), and K117 (25 kD) to chromosome 11q13-qter. K117, the putative human Thy-1 antigen, was expressed at high levels in chromosome 11-containing hybrids constructed with mouse neuroblastoma cells, but showed little or no expression in hybrids constructed with mouse L cells. A similar pattern of expression in hybrids was found for MC139, an antigen shared by neuroectoderm-derived cells and normal and malignant T lymphocytes. T43 is a marker of malignant tumors (but not benign tumors) derived from a number of T43- epithelia, and the regional assignment of the T43 locus on chromosome 11 raises questions about its possible involvement in the specific rearrangements of this chromosome seen in human malignancies.
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PMID:Role of human chromosome 11 in determining surface antigenic phenotype of normal and malignant cells. Somatic cell genetic analysis of eight antigens, including putative human Thy-1. 286 25

Fibronectin is a multifunctional glycoprotein which promotes the adhesion of a variety of cell types to extracellular matrices, including artificial tissue culture substrata. Biochemical analyses of substratum adhesion sites indicated important functions for cell-surface heparan sulphate proteoglycan (HS-PG) in directly mediating adhesive responses by the binding of heparan sulphate sequences to fibronectin. In addition, fibronectin has a binding domain for a cell surface 'receptor' (possibly a 140K glycoprotein) important in these responses. To differentiate the relative importance of these two binding activities, a proteolytically generated cell-binding fragment of fibronectin has been isolated which binds to the 140K 'receptor' but not to HS or to collagen. Platelet factor 4 (PF4), a tetravalent HS-binding protein, provides a model of the tetravalent HS-binding activity of fibronectin, as supported by affinity chromatography studies (these studies also reveal the complexity of HS-PG metabolism in adhesion sites). Responses are measured on substrata coated with the cell-binding fragment of fibronectin, intact fibronectin, or PF4, singly or in combination. Fibroblast-like BALB/c 3T3 cells form both close and tight-focal adhesive contacts with associated microfilament stress fibres on intact fibronectin. Whereas HS-PG binding appears to mediate the formation of close contacts and linear microfilament bundles, a cooperative relationship exists between the HS- and the cell-binding activities of the intact fibronectin molecule in the formation of focal contacts and stress fibres. Human dermal fibroblasts generate different adhesive responses on HS-binding or cell-binding substrata, which are dependent on whether cells have been grown in medium with ascorbate to maximize production of their own collagenous matrix. As with 3T3 cells, focal contact and stress fibre formations of dermal cells require both binding activities in the intact fibronectin molecule. A third system consists of neuroblastoma tumour cells which adhere and extend neurites on fibronectin. Cell-body adherence, but not neurite extension, occurs on HS-binding matrices whereas neurite extension requires only fibronectin's cell-binding activity; the responses of primary peripheral neurons were exactly the opposite and CNS neurons did not respond at all. These studies indicate the diversity of molecular mechanisms by which various cells interact with the multifunctional fibronectin molecule in order to perform specialized functions, as well as the independent or cooperative functions of heparan sulphate proteoglycan on the cell surface in mediating these responses.
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PMID:Heparan sulphate proteoglycan as mediator of some adhesive responses and cytoskeletal reorganization of cells on fibronectin matrices: independent versus cooperative functions. 294 46

Human neuroblastoma cells (Platt and La-N1) adhere and extend neurites on a ganglioside GM1-binding substratum provided by cholera toxin B (CTB). These adhesive responses, similar to those on plasma fibronectin (pFN), require the mediation of one or more cell-surface proteins [G. Mugnai and L. A. Culp (1987) Exp. Cell Res. 169, 328]. The involvement of two pFN receptor molecules in ganglioside GM1-mediated responses on CTB have now been tested. In order to test the role of cellular FN binding to its glycoprotein receptor integrin, a soluble peptide containing the Arg-Gly-Asp-Ser (RGDS) sequence was added to the medium. It did not inhibit attachment on CTB but completely inhibited formation of neurites; in contrast, the RGDS peptide minimally inhibited attachment or neurite formation on pFN. Once formed, neurites on CTB became resistant to the peptide. In order to test the role of cell-surface heparan sulfate proteoglycan (HS-PG), two approaches were used. First, the HS-binding protein platelet factor-4 (PF4) was used to dilute CTB or pFN on the substratum or, alternatively, added to the medium. Diluting the substratum ligand with PF4 had no effects on attachment on either CTB or pFN. However, neurite formation on CTB was readily inhibited and on pFN partially inhibited; the effects of PF4 were far greater than a similar dilution with nonbinding albumin. When PF4 was added to the medium of cells, attachment on either substratum was unaffected as was neurite outgrowth on pFN, revealing differences in PF4's inhibition as the substratum-bound or medium-borne component. In contrast, PF4 in the medium at low concentrations (1 microgram/ml) was highly inhibitory for neurite formation on CTB. The second approach utilized the addition of bovine cartilage dermatan sulfate proteoglycan (DS-PG), shown to bind to pFN as well as to substratum-bound CTB by ELISA, or cartilage chondroitin sulfate/keratan sulfate proteoglycan (CS/KS-PG) to the substratum or to the medium. At low concentrations, DS-PG but not CS/KS-PG actually stimulated neurite formation on CTB while at higher concentrations DS-PG completely inhibited attachment and neurite formation. While DS-PG partially inhibited attachment on pFN, it had no effect on neurite formation of the attached cells. Neuroblastoma cells adhered to some extent to substrata coated only with DS-PG, indicating "receptors" for PGs that permit stable interaction.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Ganglioside-dependent adhesion events of human neuroblastoma cells regulated by the RGDS-dependent fibronectin receptor and proteoglycans. 296 69

Antibodies specific for the insulin-like growth factor II (IGF-II) receptor were used to study its distribution in a number of rat tissues and cell lines in order to determine which cells might be responsive to local or circulating IGF-II. In cultured 18-54,SF and B104 neuroblastoma cells, plasma membrane and cytoplasmic staining corresponding to Golgi apparatus could be seen, consistent with the glycoprotein nature of this receptor. Antibody binding was also seen in the central nervous system, confined primarily to the choroid plexus, and the vascular and ependymal elements. Some staining was seen in the parenchyma of the brain, in addition to binding around nerve sheaths and axon bundles. There were high levels of immunoreactivity in all three lobes of the pituitary, including vascular and cellular elements. In liver, highest levels of immunoreactivity occurred in the sinusoidal cells. In lung, IGF-II receptor immunostaining was seen in the alveoli and around the bronchioles. Staining in kidney was observed in glomeruli, tubules, and Bowman's capsules. Lower levels of immunostaining were seen in skeletal muscle, located primarily around the muscle sheaths. Localization of IGF-II receptor to cells of known function in different tissues will help elucidate the role of this ligand-receptor system in regulating growth and metabolism.
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PMID:Distribution of insulin-like growth factor II receptor immunoreactivity in rat tissues. 296 77

High activity of renin was demonstrated in human neuroblastoma tissue. This activity was inhibited by specific antibody raised against human renal renin, indicating that it was not due to the nonspecific action of proteases. The specific activity of renin was 122.8 ng of angiotensin I generated mg of protein-1 h-1. It shared some biochemical features with well-known kidney renin, such as molecular weight, optimum pH, the presence of trypsin-activatable inactive renin, and glycoprotein nature. Furthermore, angiotensin-converting enzyme (ACE) activity (2.64 nmol mg of protein-1 min-1) was found in the tissue. This activity was inhibited by captopril, a specific ACE inhibitor, or by omission of chloride ion. These results suggest that true renin in addition to ACE exists in human neuroblastoma tissue.
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PMID:Renin and angiotensin-converting enzyme in human neuroblastoma tissue. 298 31

Readily detectable levels of renin activity were demonstrated in the human brain. This activity was inhibited by specific antibody raised against human renal renin, indicating that it was not due to the nonspecific action of proteases such as cathepsin D. The pineal gland was found to be the richest source of renin followed by the pituitary, hypothalamus and hippocampus. The substantia nigra, caudate nucleus, putamen and thalamus contained moderately high concentrations of renin. The brain renins from pineal and pituitary glands shared some biochemical features with well-known kidney renin, such as molecular weight (46,000 daltons for pineal renin; 37,000-45,000 daltons for pituitary renin), optimum pH (6.0-7.0), the presence of trypsin activatable inactive renin, and a glycoprotein nature. However, the electrofocusing pattern of renin from pituitary tissue (pI = 4.43, 5.77) differed from that of plasma and kidney enzymes heretofore reported, a discrepancy which could be interpreted as evidence for the endogeneous synthesis of renin in the brain tissue. Furthermore, a high activity of immunoreactive renin was found in human neuroblastoma tissue. The biochemical characteristics of the neuroblastomal renin were generally similar to the known properties of kidney renin in many respects, providing evidence of the presence of the renin-angiotensin system within human neuronal cells.
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PMID:Immunoreactive renin in human brain: distribution and properties. 299 58

The first enantiomeric pair of irreversible opioid ligands [(+)- and (-)-4] were synthesized in greater than 99.6% optical purity as determined by HPLC analysis of diastereoisomeric derivatives of the intermediate 3-methyl-N-phenyl-4-piperidinamine enantiomers. Single-crystal X-ray analysis of the (R,R)-L-(+)-tartaric acid salt of (-)-9 revealed the absolute configuration to be 3S,4R. The absolute configuration of (-)-3 [cis-(-)-3-methylfentanyl] and (-)-4 derived from (-)-9 is thus 3S,4R and that of (+)-3 and (+)-4 is 3R,4S. The (+) enantiomer of 4 (SUPERFIT) was shown to be highly potent and specific for acylation of delta opioid receptors (to the exclusion of mu) in rat brain membranes like its achiral prototype FIT and was about 10 times as potent as the latter in this assay. The (+)-4 was about 5 times as potent as FIT in acylation of delta receptors in NG108-15 neuroblastoma X glioma hybrid cells and about 50 times as potent as its enantiomer. Both FIT and (+)-4 behaved as partial agonists in inhibition of delta receptor coupled adenylate cyclase in NG108-15 membranes and (+)-4 was 5-10 times more potent than FIT and about 100 times more potent than its enantiomer in this assay. Dibromination of amine 12, catalytic exchange of bromine with tritium gas, and reaction of the labeled amine with thiophosgene afforded [3H]-(+)-4 with a specific activity of 13 Ci/mmol. Previous experiments indicated (+)-4 acylates the same 58 000-dalton glycoprotein previously shown to be acylated by FIT but with less nonspecific labeling. In view of the high potency and specificity of (+)-4 and the availability of its enantiomer, it seems likely that these compounds will prove to be valuable tools for study of the opioid receptor complex.
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PMID:Probes for narcotic receptor mediated phenomena. 12. cis-(+)-3-Methylfentanyl isothiocyanate, a potent site-directed acylating agent for delta opioid receptors. Synthesis, absolute configuration, and receptor enantioselectivity. 301 85

Nerve growth factor (NGF) is a polypeptide hormone which plays a central role in the development and growth of sympathetic and sensory neurons. The effects of NGF on target cells are mediated by a specific cell surface structure, nerve growth factor receptor (NGFr), which has been identified in human cells as a 75,000-mol-wt glycoprotein. We have used a monoclonal antibody to human NGFr to study cell-surface expression of the receptor on a panel of mouse-human neuroblastoma hybrids, and the serological typing results permit assignment of the gene coding for NGFr (NGFR) to chromosome 17q21-qter. In addition to mouse-human neuroblastoma hybrids, human NGFr was also detected on hybrids derived from fusions between mouse L-cell fibroblasts and human neuroblastoma and melanoma cells. Furthermore, induction of human NGFr expression was observed in hybrids derived from NGFr- human kidney epithelial cells and mouse L cells, but not in hybrids derived from human kidney epithelial cells and mouse RAG kidney carcinoma cells. These results suggest that cell-surface expression of human NGFr is controlled by trans-acting regulatory signals.
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PMID:Assignment of human nerve growth factor receptor gene to chromosome 17 and regulation of receptor expression in somatic cell hybrids. 302 Jul 11


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