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)

Intestinal obstruction is a common postoperative complication and is usually related to peritoneal adhesion formation. A less well-recognized cause is postoperative intussusception (POI). Thirty-six instances of POI in children (aged 1 month to 18 years) were treated between 1970 and 1987. POI followed Nissen fundoplication in 9 patients, neuroblastoma resection in 5, small-bowel procedures in 4, inguinal herniorrhaphy in 3, pull-through procedures in 3, ureterostomy in 2, thoracic procedures in 2, ventral hernia in 1, nephrectomy in 1, hepatic resection in 1, Heller myotomy in 1, ventriculo-atrial shunt in 1, and gastrocystoplasty in 1. Initial symptoms included bilious vomiting or increased nasogastric drainage (after initial return of gut function) in 26 patients, abdominal distension in 24, irritability in 10, intermittent pain in 7, palpable abdominal mass in 2, rectal bleeding in 2, and lethargy in 1. The symptoms occurred 1 to 24 days (mean, 8 days) after the initial surgery. Plain abdominal radiographs revealed multiple air-fluid levels in 31 and an "adynamic ileus" in five patients. Barium contrast techniques could successfully reduce two ileocolic and one distal ileo-ileal lesions. The remainder necessitated operative management. Manual reduction was possible in 29 cases, and four children with diagnostic delay required bowel resection and an anastomosis for intestinal necrosis. The site of intussusception was ileo-ileal in 23 patients, jejunojejunal in 6, ileocolic in 5, and jejuno-ileal in 2. The diagnosis of POI should be considered in children with signs of bowel dysfunction in the early postoperative period. Contrast studies are of limited value, since most cases are confined to the small bowel. A high index of suspicion and prompt laparotomy will usually allow manual reduction of the lesion. Diagnostic delay may result in bowel necrosis.
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PMID:Postoperative intussusception: experience with 36 cases in children. 317 73

Neuronal hybrid cells established by somatic cell fusion are useful for studies of neuronal properties at the molecular level (Hammond, D.N., Lee, H.J., Tonsgard, J.H. and Wainer, B.H., Development and characterization of clonal cell lines derived from septal cholinergic neurons, Brain Res., 512 (1990) 190-200; Wainwright, M.S., Perry, B.D., Won, L.A., O'Malley, K.L., Wang, W.Y., Ehrlich, M.E. and Heller, A., Immortalized murine strial neuronal cell lines expressing dopamine receptors and cholinergic properties, J. Neurosci., 15 (1995) 676-688). The somatic cell fusion method requires a fusion partner which is unable to survive in the selection medium if it does not fuse with primary cells to isolate the hybrid cells. Hypoxanthine guanine phosphoribosyltransferase (HPRT)-deficient partner cells and hypoxanthine, aminopterin and thymidine (HAT) selection medium are commonly used for this procedure (Harlow, E. and Lane, D. (Eds.), Antibodies: a Laboratory Manual, Cold Spring Harbor Laboratory Publications, New York, 1988, pp. 139-243). The present method requires neither HPRT-deficient cells nor HAT medium. Primary neurons are fused with the C1300 neuroblastoma cells pretreated with emetine (Grollman, A.P., Inhibitors of protein biosynthesis, J. Biol. Chem., 243 (1968) 4089-4094), an inhibitor of ribosomes and actinomycin D (Perry, R.P., Selective effects of actinomycin D on the intracellular distribution of RNA synthesis in tissue culture cells, Exp. Cell Res., 29 (1963) 400-406), an inhibitor of ribosomal RNA (rRNA) synthesis, before fusion. By this treatment, we are able to isolate hybrid cells after fusion because non-fused C1300 cells die due to the loss of active ribosomes and protein synthesis, whereas C1300 cells fusing with primary cells survive due to the supply of intact ribosomes and rRNA from primary cells. This method produces neuronal hybrids at high efficiency.
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PMID:Method for production of neuronal hybridoma using emetine and actinomycin D. 938 57

The vanilloid-like TRP-channel VRL-1 (TRPV2) is a nonselective cation channel expressed by primary sensory neurons and non-neuronal tissues [Caterina, M.J., Rosen, T.A., Tominaga, M., Brake, A.J and Julius, D. (1999) Nature 398, 436-441]. It is one of the six members of the vanilloid-like TRP-channel family which is now termed the TRPV family [Montell, G., Birnbaumer, L., Flockerzi, V., Bindels, R.J., Brutford, E.A., Caterina, M.J., Clapham, D.E., Harteneck, C., Heller, S., Julius, D., Kojima, I., Mori, Y., Penner, R., Prawitt, D., Scharenberg, A.M., Schultz, G., Shimizu, N. and Zhu, M.X. (2002) Mol. Cell 2, 229-231]. As it is a temperature-gated channel, VRL-1 appears to be functionally related to VR1. In contrast to VR1, VRL-1 is activated at a higher temperature threshold and it does not respond to capsaicin or protons. Here we describe the expression of VRL-1 in the rat dorsal root ganglion-derived cell line F-11, a hybridoma of mouse neuroblastoma (N18TG2) and rat dorsal root ganglion cells. We found by RT-PCR that F-11 cells express not only the rat VRL-1, but also its mouse orthologue in a single cell. The F-11 parental cell line N18TG2 also expressed murine VRL-1. Due to its neuronal character, the DRG-derived F-11 cell line provides an experimental system for the study of VRL-1 biochemistry. However, one has to be aware that both the mouse and the rat protein are expressed simultaneously. Furthermore we cloned VRL-1 from rat brain and analyzed its glycosylation and localization in comparison to the endogenously expressed protein in F-11 cells. In contrast to the endogenous VRL-1 the overexpressed protein is glycosylated. Similar to VR1 the glycosylation is N-linked as shown by an deglycosylation assay. Immunofluorescence analysis of the endogenous VRL-1 in F-11 cells gives only weak signals in the cytoplasm whereas the overexpressed rat VRL-1 appears mainly at the plasma membrane.
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PMID:Dual expression of mouse and rat VRL-1 in the dorsal root ganglion derived cell line F-11 and biochemical analysis of VRL-1 after heterologous expression. 1462 91