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Query: UMLS:C0035412 (rhabdomyosarcoma)
 6,156 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Malignant fibrous histiocytomas (MFH) belong to the most frequent soft tissue tumours in adults and have to be discriminated from other tumours with similar morphology. Various tumour markers aid the differential diagnosis. Twenty cases of MFH were studied immunohistochemically using antibodies to vimentin, TPA, desmin, lysozyme, alpha 1-antitrypsin, alpha 1-antichymotrypsin, S-100 protein, neurone-specific enolase (NSE), laminin, fibronectin and ferritin. Vimentin and lysozyme were found in the tumour cells of all, alpha 1-antitrypsin of 18, alpha 1-antichymotrypsin of 19, fibronectin of 16 and ferritin of 12 cases. Antibodies of TPA, desmin, S-100 protein, NSE and laminin did not reveal positive immunoreactivity. Exclusion of spindle-cell carcinoma can be made by positive vimentin and negative TPA reactivity, of melanoma by negative S-100 reactivity, and of leio- and rhabdomyosarcoma by lack of desmin immunoreactivity. Schwannomas contain S-100 protein, but lack lysozyme, alpha 1-antitrypsin, alpha 1-antichymotrypsin and fibronectin. Pleomorphic liposarcomas cannot be distinguished from MFH on the basis of immunohistochemical staining. Vimentin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and fibronectin can, therefore, be regarded as useful markers in the differential diagnosis of MFH.
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PMID:[Immunohistochemical studies in the differential diagnosis of malignant fibrous histiocytoma]. 302 16

Human tumor cell lines, a rhabdomyosarcoma (RD), and a fibrosarcoma (HT-1080) were distinguished from normal human fibroblasts by tumorigenicity in athymic nude mice and immunosuppressed rats and hamsters, secretion of different types of collagen and procollagen molecules, and reduced amounts of fibronectin. The fibronectins secreted by both normal and tumor cells did not show any significant structural difference and were phosphorylated only on serine residue(s). However, fibronectin secreted by the tumor cells exhibited decreased electrophoretic mobility and was associated with as yet unidentified phosphorylated macromolecules.
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PMID:Human normal and tumor cell lines: comparison of fibronectins and collagens. 358 Sep 44

A series of 11 cloned cell lines derived from a primary, nickel-induced rat rhabdomyosarcoma was evaluated for their metastatic capacity (number of lung colonies following i.v. injection) and attachment kinetics to confluent pig endothelial cell monolayers grown in vitro. The morphology of the adhering cells was also studied by optical and scanning electron microscopy. Cells from all lines tested began to attach to the endothelial monolayers within 15 min of incubation at 37 degrees C, with 64% to 93% of the cells adhering after 2 h. Attachment rates at 30 min ranged from 29 to 48% for four lines classed as "weakly adhesive" (attachment, less than 50%) and from 53 to 78% for seven lines classed as "highly adhesive" (attachment, greater than 50%). Four clones of five displaying low lung-colonizing capacities also showed low attachment rates to endothelial monolayers in vitro. All of six highly colonizing lines studied had high attachment rates. A degree of positive correlation was observed between the amount of cell surface fibronectin as evaluated by immunofluorescence and the early phase attachment rates (and lung-colonizing capabilities) of the different cloned cell lines. Early (15 min) attachment of tumor cells to isolated extracellular matrix preparations proceeded at higher rates than to endothelial monolayers, and previously detected differences between high- and low-colonizing clones were less evident with these matrix substrates. Our results suggest possible interrelationships between specific cell adhesion properties and the metastatic potential of blood-borne tumor cells.
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PMID:Differential adhesiveness of rhabdomyosarcoma-derived cloned metastatic cell lines to vascular endothelial monolayers. 370 93

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

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 ability of high-density lipoprotein (HDL) to support the growth of an established tumor cell line exposed to defined medium supplemented with transferrin has been examined. Low-density A-431 carcinoma cells maintained on extracellular matrix- or fibronectin-coated dishes proliferated actively when exposed to a synthetic medium supplemented with HDL, 500 micrograms protein per ml. Epidermal growth factor added at concentrations above 0.5 ng/ml inhibited cell growth, while at concentrations above 5 ng/ml it was cytotoxic. Among the various substrata tested for their ability to support the active proliferation of low-density A-431 cells when exposed to transferrin and HDL, plastic was the least efficient. On fibronectin-coated dishes, cells ceased to proliferate after 8 population doublings, while on extracellular matrix-coated dishes cells could be passaged for 50 population doublings. In the case of colon carcinoma, rhabdomyosarcoma, and Ewing's sarcoma cells exposed to medium supplemented with transferrin, the addition to the cultures of HDL alone resulted in a growth rate and final cell density which were similar to those observed when cells were exposed to serum-supplemented medium. In the case of the mammary carcinoma cell lines MCF-7 and ZR-75-1, HDL also supported cell growth, although to a lesser extent than did serum. The present study therefore indicates that HDL is capable of supporting, either totally or partially, the in vitro proliferation of tumor cells.
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PMID:High-density lipoproteins and the proliferation of human tumor cells maintained on extracellular matrix-coated dishes and exposed to defined medium. 704 62

A 14K beta-galactoside-binding lectin (galectin-1) is present in many animal tissues. In a search for endogenous ligands, we surveyed galectin-1-binding proteins in human placenta. Extract of human placenta with 2 M urea was applied to a Sepharose 4B column conjugated with galectin-1 purified from frog (Rana catesbeiana) eggs. Two major proteins eluted with 100 mM lactose from the column-bound fraction showed apparent molecular masses of 220 and 180 kDa on SDS-PAGE under reducing conditions. Western blotting analysis using monoclonal antibodies indicated that these proteins were fibronectin and laminin, respectively. Most placental and amniotic fibronectins bound strongly to the column, whereas almost all plasma fibronectin passed through the column. The galectin-1, fibronectin and laminin were immunohistochemically shown to be co-localized in the extracellular matrix of placental tissue. In a cell attachment assay, rhabdosarcoma cells adhered to a plate coated with placental fibronectin, even in the presence of GRGDS peptide, if galectin-1 were also present. This adhesive effect of galectin-1 was inhibited by lactose. These results indicate that tissue fibronectin, as well as laminin, serve as endogenous ligands for galectin-1, suggesting that galectin-1 may play a role in assembly of the extracellular matrix, or in the control of cell adhesion based on lectin-extracellular matrix interaction.
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PMID:Tissue fibronectin is an endogenous ligand for galectin-1. 778 Feb 1

Sixty-seven childhood tumors were studied immunohistochemically for the extracellular matrix element type IV collagen, laminin, and fibronectin. Tumors included Ewing's sarcoma, primitive neuroectodermal tumor, small cell osteosarcoma, neuroblastoma or ganglioneuroblastoma, rhabdomyosarcoma, and lymphoma. It was found that small cell osteosarcoma was often positive for fibronectin but not type IV collagen or laminin, a new observation. In the lymphomas, matrix proteins were rarely found. Ewing's sarcoma was variably positive for type IV collagen and laminin, but fibronectin was absent. Extracellular laminin and fibronectin were found in one of two cases of primitive neuroectodermal tumor. In neuroblastoma and ganglioneuroblastoma, the matrix components were rarely found. These results, discrepant with findings in cultured cells, may reflect the altered capacity of tumors to produce these proteins in vitro, which suggests that caution should be exercised in drawing conclusions regarding the nature or histogenesis of tumors from data obtained with cultured tumor cells. Embryonal rhabdomyosarcoma frequently contained all matrix elements in the extracellular space and in a dotlike pattern in the cytoplasm; alveolar rhabdomyosarcoma rarely contained these proteins and never exhibited the dotlike pattern. The frequent finding of matrix proteins in embryonal rhabdomyosarcoma but only rarely in alveolar rhabdomyosarcoma and the unique immunostaining pattern in embryonal rhabdomyosarcoma may prove to be a useful adjunct in the diagnosis of childhood tumors.
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PMID:Extracellular matrix of small round cell tumors of childhood: an immunohistochemical study of 67 cases. 815 9

Fibronectin contains at least two distinct oligopeptide sequences serving as signals for the interaction with cell surface adhesion receptors termed integrins. One of these sequences, Arg-Gly-Asp-Ser (RGDS) tetrapeptide, was shown to be transferred to a truncated form of Staphylococcal IgG-binding protein (hereafter referred to as tSPA) with retention of its cell-adhesive activity [Maeda, T. et al. (1989) J. Biol. Chem. 264, 15165-15168]. We have extended the observation to another cell-adhesive sequence, Glu-Ile-Leu-Asp-Val-Pro-Ser-Thr (referred to as "CS1" sequence), to demonstrate that: i) the tSPA grafted with the sequence mediated adhesion of human lymphoma and rhabdomyosarcoma cells, mouse melanoma cells, but not of hamster fibroblasts; ii) antibodies against integrin alpha 4 and beta 1 subunits specifically inhibited cell adhesion mediated by the CS1-grafted tSPA; iii) a heterodivalent tSPA grafted with both RGDS and CS1 sequences at different sites was more potent in promoting cell adhesion than the monovalent tSPAs grafted with either sequence alone. These results indicate that not only the RGDS but also the CS1 sequence can be transferred to tSPA with retention of its cell-adhesive activity as well as its cell-type specificity, and that the grafted CS1 sequence is recognized by the same integrin isotype as the authentic sequence within intact fibronectin.
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PMID:Engineering of artificial cell-adhesive proteins by grafting EILDVPST sequence derived from fibronectin. 845 70

To assess directly the functional role of the integrin VLA-3 (alpha 3 beta 1), we transfected human alpha 3 cDNA into erythroleukemia (K562) cells and rhabdomyosarcoma (RD) cells. The resulting transfectants (KA3 and RA3) expressed alpha 3 beta 1 on the cell surface as confirmed using a panel of nine anti-alpha 3 monoclonal antibodies. Neither of the transfected cells exhibited increased adhesion to the extracellular matrix proteins fibronectin, laminin, and collagen. However, the KA3 transfectants did bind strongly to the extracellular matrix deposited by epidermal and carcinoma cell lines, allowing the cells to attach and spread. Binding to this cell-deposited ligand, probably containing epiligrin/kalinin, was specific to VLA-3 and could be inhibited by anti-alpha 3 antibodies and by EDTA, but not by RGD peptides. In marked contrast to other integrins (VLA-2 and VLA-4), VLA-3 showed high constitutive activity in K562 cells, but was minimally active in RD cells. Also contrasting with other beta 1 integrins, VLA-3 was minimally stimulated by the anti-beta 1 monoclonal antibody TS/216 under normal conditions. VLA-3-mediated adhesive function was well supported by either Mg2+ or Mn2+, but was almost completely abolished by the presence of 1 mM Ca2+. Surprisingly, this negative Ca2+ effect was completely overcome by the addition of the stimulatory anti-beta 1 monoclonal antibody TS2/16. Together, these results point to markedly distinct regulation for VLA-3 function compared to other beta 1 integrins. Also, all anti-VLA-3 antibodies were able to induce temperature-dependent homotypic cell aggregation of KA3 cells, but not K562 cells. However, this aggregation did not appear to be directly mediated by VLA-3 since it was not inhibited by EDTA. In addition, no enhancement of heterotypic cell-cell adhesion was observed in alpha 3-transfected cells.
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PMID:The function and distinctive regulation of the integrin VLA-3 in cell adhesion, spreading, and homotypic cell aggregation. 847 8


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