Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0035412 (rhabdomyosarcoma)
 6,156 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extracellular matrix proteins synthesized and secreted by adherent human tumor cell lines were analyzed using metabolic labelling with glycine and proline in the presence of ascorbate, polypeptide analysis and polyacrylamide gel electrophoresis, affinity chromatography, collagenase digestion, and immunofluorescence staining. The results showed a characteristic pattern of matrix proteins for each tumor cell type. Tumor cell lines of mesenchymal origin produced mostly interstitial types (I and II) of collagen and fibronectin. Carcinoma cell lines secreted only basement membrane proteins, type IV collagen, laminin and fibronectin, but not interstitial collagen. A melanoma and a rhabdomyosarcoma cell line produced type V of procollagen that has not previously been described in cell culture. Neuroblastoma cells were shown to be phenotypically heterogeneous also with respect to matrix protein production. We propose that the analysis of extracellular matrix proteins may serve as an adjunct in the classification of human tumors.
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PMID:Extracellular matrix proteins characterize human tumor cell lines. 627 24

Although thyrotoxicosis and orbital complications of acute ethmoid or frontal sinusitis are among the most common causes of unilateral exophthalmos, inflammatory pseudotumor is frequently accompanied by progressive acute unilateral proptosis. Because the associated chemosis, scleral erythema, and ophthalmoplegia constitute a spectrum of clinical findings present in numerous inflammatory orbital disorders and systemic diseases, the diagnosis of inflammatory pseudotumor is one of exclusion, often requiring orbital biopsy. Four patients without evidence of sinusitis, endocrinopathy, collagen vascular disease, or Wegener's granulomatosis are described. The diagnosis of orbital pseudotumor was disclosed by computed axial tomography, thus avoiding orbitotomy. The finding of scleral and choroidal thickening with enhancement following intravenous contrast injection represents a select group of patients with orbital pseudotumor and differentiates them from patients with endocrine exophthalmopathy or neoplasms. This noninvasive technique is extremely valuable because early diagnosis is critical for successful treatment. All four patients responded dramatically to high-dose corticosteroid therapy. In the absence of significant clinical response, however, Wegener's granulomatosis, lymphoma, and rhabdomyosarcoma, especially in younger patients, must be carefully excluded. Orbital exploration or decompression or both are used when proptosis, headache, or orbital pain does not resolve promptly, visual acuity deteriorates, or the diagnosis remains unknown.
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PMID:Computerized axial tomography in inflammatory pseudotumor of the orbit. 682 19

Chemotaxis of human embryo fibroblasts and rhabdomyosarcoma cells was studied in a blind well Boyden chamber using fibronectin as a chemoattractant. The cell strains studied show a differential response to fibronectin, a fact which may mirror the origin of the cells, that means normal skin or tumor associated tissue, respectively. Furthermore, we detected another chemoattractive fraction synthesized and secreted by fibroblasts in addition to fibronectin and collagen derived fragments. Initial experiments demonstrated the proteinous nature of the component(s) and provided some information on the biochemical features.
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PMID:A study on fibroblast chemotaxis using fibronectin and conditioned medium as chemoattractants. 683 71

The A204 cell line, derived from a human rhabdomyosarcoma, was studied in culture for its capacity to synthesize collagen types and other extracellular matrix proteins. The cells synthesized and secreted into the culture medium collagenous proteins with apparent molecular weights of 220,000 and 150,000. These were identified as the pro alpha 1 and pro alpha 2 chains of type V collagen by immunoprecipitation and by peptide mapping. The pro alpha 1(V) chain was made in excess of a 2:1 ratio for pro alpha 1(V) to pro alpha 2(V), and a fraction of the pro alpha 1(V) chains together with all of the pro alpha 2(V) chains participated in intermolecular disulfide bonding. The chains were extensively glycosylated at hydroxylysyl residues in ascorbate-supplemented cultures. A fraction of the secreted pro alpha 1(V) chains was processed to the p alpha 1(V) form, but further processing in the culture medium was very slow and the type V collagen molecules deposits in the extracellular matrix apparently retained large non-triple helical domains. Since the A204 cell line does not produce other collagen types, it may prove useful in further studies of the biosynthesis of type V procollagen.
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PMID:Biosynthesis of type V procollagen by A204, a human rhabdomyosarcoma cell line. 704 31

The invasion and migration occurring in primary neoplastic tissue explants were studied by using a three-dimensional collagen matrix model, subsequent time-lapse videomicroscopy, and computer-assisted cell tracking. We show that not only single cells but groups of clustered cells comprising 5 to more than 100 cells detach from the primary tumor lesion and migrate within the adjacent extracellular matrix. These clusters were highly polarized, resulting in a high directional persistence of migration. Locomoting cell clusters were observed in primary cultures from invasive oral squamous cell carcinomas (6 of 9), ductal breast carcinomas (2 of 3), and rhabdomyosarcoma (1 of 1), whereas normal oral mucosa (0 of 4) was cell cluster negative. Thus, locomoting cell clusters could be a novel and potentially important mechanism of cancer cell invasion and metastasis.
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PMID:Migration of coordinated cell clusters in mesenchymal and epithelial cancer explants in vitro. 755 28

Collagens V and XI are thought to form a core around which the major interstitial collagens, I and II, respectively, are organized during fibrillogenesis. We previously reported the presence of a heterotypic form of collagens V and XI, [alpha 1(XI)]2 alpha 2(V), in cultures of A204 rhabdomyosarcoma cells [Kleman, J.-P., Hartmann, D. J., Ramirez, F., & van der Rest, M. (1992) Eur. J. Biochem. 210, 329-335]. This collagen forms a matrix which remains highly insoluble, even when cells were cultured in the presence of beta-aminopropionitrile, an inhibitor of lysyl oxidase and thereby of "classical" collagen cross-linking. When the cells were cultured in the presence of putrescine, a competitive inhibitor of transglutaminase-catalyzed protein cross-linking, a drastic increase in collagen solubility was observed. This result indicates that a transglutaminase contributes to the covalent stabilization of the collagen matrix of these cells. A204 rhabdomyosarcoma cells express tissue transglutaminase as revealed by specific antibodies, and enzyme activity was detected in the cell layer during culture and in cell extracts. Both collagens V and XI are specific glutaminyl substrates for tissue transglutaminase in vitro, as shown by incorporation of [3H]putrescine. The highly homologous alpha 1 chains of collagens V and XI were the major targets for the cross-linking. Trypsin cleaved the [3H] label from the alpha 1 chain of collagen V, demonstrating that the cross-linking occurs in the non triple helical propeptide domains.
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PMID:Transglutaminase-catalyzed cross-linking of fibrils of collagen V/XI in A204 rhabdomyosarcoma cells. 757 69

We have isolated cDNAs and completed for the first time the primary structure for a novel collagenous chain that was partially characterized earlier and named alpha 1(Y) chain [Yoshioka, H. et al. (1992) Genomics 13, 884-886]. The size of the coding region was unexpectedly small compared with the length of the mRNA (> 10 kb), owing to the presence of a long 3' untranslated region (> 5 kb). The predicted polypeptide contained 1,142 amino acid residues with a 23-residue signal peptide consisting of 5 collagenous domains of 70-224 residues in length, interspersed and flanked with 6 noncollagenous (NC) domains. The primary structure is distinct from those of the 32 known collagen alpha-chains of types I through XVIII. Therefore, we designate this newly discovered collagen chain the alpha 1 chain of type XIX collagen. Sequence analysis suggested that this chain belongs to the recently discovered group of collagens known as FACITs (fibril associated collagens with interrupted triple-helices). Northern blotting analysis demonstrated hybridization of the cDNA to a large mRNA species (> 10 kb) extracted from a rhabdomyosarcoma cell line (CCL 136). We also isolated numerous truncated cDNA clones of which the 3' parts were different from the "proto" type of the mRNA of > 10-kb size. Sequence comparison between cDNAs and corresponding genomic DNA fragments indicated that unusual splicing events occurred through insufficient recognition at acceptor sites. Expression of the gene was extremely infrequent in the rhabdomyosarcoma cell line; it could be restricted to certain animal tissues both temporally and spatially during early development.
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PMID:The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains a long unusual 3' untranslated region and displays many unique splicing variants. 777 80

Human collagen (COL) cDNA clones were isolated from a library representing transcripts synthesized by an established rhabdomyosarcoma (RH) cell line. The 0.6-kb insert of the first isolate encodes a discontinuous collagenous sequence not homologous to type I-XVI COL chains. Sequencing of a second clone with a 4-kb insert revealed an open reading frame (ORF) of 2154 nucleotides. The deduced amino acid (aa) sequence begins with an 186-aa noncollagenous region containing seven cysteines (Cys). Several of the Cys and surrounding aa residues can be aligned with those in type XVI, XII and IX COL. Due to the presence of two long interruptions, the 524-aa collagenous region is separated into three subdomains that each have smaller interruptions of 1-6 aa. The protein terminates with an 8-aa noncollagenous peptide including an unusual single Cys which would be expected to form an interchain disulfide bond. Results of Northern blot hybridization suggest that the new COL chain may be uncommonly large since the clone identified a low-abundance RNA at least 12.4 kb in size. The gene coding for RH COL is located on human chromosome 6. It is now important to elucidate the role of this unusual COL in the infrastructure of extracellular matrix.
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PMID:Human cDNA clones transcribed from an unusually high-molecular-weight RNA encode a new collagen chain. 791 3

Sequential morphological changes in tumor capillaries of istransplanted R1H rat rhabdomyosarcoma were observed weekly by transmission electron microscopy during fractionated radiotherapy (75 Gy/25 fractions/5 weeks). During the first 2 weeks of irradiation (up to 30 Gy), edema of the tumor capillary wall was induced. Swollen endothelial cells bulged into the vascular lumen and were surrounded by a widened subendothelial space with increase amounts of collagen fibrils (subendothelial edema). The endothelial lining was preserved up to the 3rd week of irradiation (45 Gy). Prolonged irradiation was associated with progressive destruction of the vascular wall including shrinkage, gradual loss of cell contacts, disappearance of the normal chromatin pattern, and increase of cytoplasmic vacuoles in endothelial cells as well as disruption of basal laminae. One week after the end of radiotherapy (75 Gy), the tumor capillaries showed complete necrosis. Progressive damage to tumor capillaries in the course of fractionated radiotherapy might have adverse effects on blood supply and thus on tumor oxygenation.
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PMID:Ultrastructural studies on tumor capillaries of a rat rhabdomyosarcoma during fractionated radiotherapy. 797 91

We previously isolated a clone from a human rhabdomyosarcoma (RH) cDNA library coding for a collagen chain different from those constituting the 18 reported types (Myers, J. C., Sun, M. J., D'Ippolito, J. A., Jabs, E. W., Neilson, E. G., and Dion, A. S. (1993) Gene (Amst.) 123, 211-217). The sequence translated to a 186-amino acid noncollagenous region, a 524-residue three-subdomain collagenous region, and a presumed 8-amino acid COOH-terminal peptide. To further elucidate the primary structure of this collagen, we have now determined the sequence of additional cDNA clones. Overlapping 3' clones, found to diverge exactly where the noncollagenous 8-residue COOH sequence began, encode two additional collagenous subdomains of 168 and 70 residues and a 19-residue COOH-terminal peptide. Analysis of genomic DNA spanning the region in question revealed several 45- and 51-base pair exons linked by 4 introns totaling over 5 kilobases (kb). A 2-kb intron, absent from the clones coding for the extended collagenous region, was used in Northern blot hybridization to detect an apparently prevalent splicing intermediate 2 kb larger than the major 12.4-kb RH transcript. Therefore, the triple-helical region of this collagen chain is likely to be composed of 832 amino acids divided into five collagenous subdomains separated by 20-44 residue interruptions. Two interruptions are similar in sequence and position to those located in the type XVI chain. Furthermore, the arrangement of 2 cysteines near the COOH terminus and two imperfections in collagenous subdomain 1 are conserved in the related subclass composed of type IX, XII, XIV, and XVI collagens. However, in contrast to the COOH-terminal interchain bridging in this latter collagen group, molecular modeling strongly predicts that the cysteines in RH collagen participate in intrachain disulfide bonds. Taken together, the data clearly show that RH collagen does not represent another chain of one of the known collagen types. We propose that it be designated the alpha 1 chain of type XIX collagen.
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PMID:The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to alpha 1(XVI). 803 3


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