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Query: UMLS:C1261473 (sarcoma)
 25,952 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

beta and gamma interferons were found to enhance the organization of microfilaments, intermediate filaments, and fibronectin in the murine sarcoma virus (MSV)-transformed cell line. Furthermore, both interferons increased the number of intermediate-type junctions. Sodium butyrate was also found to act in a similar way and, when associated with interferon, an additive effect was observed. In the cell line, cultured for many passages in the presence of beta interferon (MSV-IF+), the cytoskeletal network and the extra-cellular matrix were highly developed and were reminiscent of a normal cell. These results could explain some of the biological actions of interferon, such as increased cell adhesion to the substratum and decreased cell motility.
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PMID:Reorganization of the cytoskeleton by interferon in MSV-transformed cells. 618 63

Transformation of cells by oncogenic RNA viruses is related to a number of significant changes in cell morphology and functions. The most common features of transformed cells are essentially the decrease of cell adhesiveness and the loss of contact inhibition. These changes are probably associated with an alteration of the cytoskeleton together with a marked modification in the number and distribution of membrane and extracellular matrix components. BALB/c embryonic fibroblasts transformed by murine sarcoma virus Moloney strain (MSV) are characterized by a disorderly growth pattern with a high proliferative rate and a colony forming capacity in soft agar. After a continuous treatment of MSV-transformed cells with interferon, these cells recover a normal phenotype and contact inhibition and are unable to form colonies in agar. Furthermore, reverse transformation is correlated with a polymerization of cytoskeleton constituents and a neosynthesis of two major matrix components: collagen and fibronectin. This experimental model leads to a new concept of the physiological role of interferon, such as mediator of the regulation of cell phenotype and antitumor protection.
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PMID:[Role of interferon in the phenotypic reversion of transformed cells: loss of malignancy]. 619 Jan 22

We used antibodies raised against both a heparan sulfate proteoglycan purified from a mouse sarcoma and a chondroitin sulfate proteoglycan purified from a rat yolk sac carcinoma to study the appearance and distribution of proteoglycans in cultured cells. Normal rat kidney cells displayed a fibrillar network of immunoreactive material at the cell surface when stained with antibodies to heparan sulfate proteoglycan, while virally transformed rat kidney cells lacked such a surface network. Antibodies to chondroitin sulfate proteoglycan revealed a punctate pattern on the surface of both cell types. The distribution of these two proteoglycans was compared to that of fibronectin by double-labeling immunofluorescent staining. The heparan sulfate proteoglycan was found to codistribute with fibronectin, and fibronectin and laminin gave coincidental stainings. The distribution of chondroitin sulfate proteoglycan was not coincidental with that of fibronectin. Distinct fibers containing fibronectin but lacking chondroitin sulfate proteoglycan were observed. When the transformed cells were cultured in the presence of sodium butyrate, their morphology changed, and fibronectin, laminin, and heparan sulfate proteoglycan appeared at the cell surface in a pattern resembling that of normal cells. These results suggest that fibronectin, laminin, and heparan sulfate proteoglycan may be complexed at the cell surface. The proteoglycan may play a central role in assembly of such complexes since heparan sulfate has been shown to interact with both fibronectin and laminin.
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PMID:Codistribution of heparan sulfate proteoglycan, laminin, and fibronectin in the extracellular matrix of normal rat kidney cells and their coordinate absence in transformed cells. 621 62

Various forms of heparan sulfate proteoglycan were solubilized from the mouse Engelbreth-Holm-Swarm (EHS) sarcoma by extraction with 0.5 M NaCl, collagenase digestion and extraction with 4 M guanidine. They could be separated into high (greater than or equal to 1.65 g/ml) and low (1.38 g/ml) buoyant density variants. The high-density form from the NaCl extract and collagenase digest had Mr = 130000 and So20,W = 4.5 S and contained 4-10% protein, indicating Mr = 5 000-12 000 for the protein core. This proteoglycan exhibited polydispersity as shown by rotary shadowing electron microscopy and ultracentrifugation. An average molecule consisted of four heparan sulfate chains (Mr = 29 000) each with a length of 32 +/- 10 nm. The low-density form (Mr about 400 000) could not be completely purified and contained about 50% protein. As shown by radioimmunoassay, the various proteoglycans shared similar protein cores. Labeling of the tumor in vivo or in vitro demonstrated preferential incorporation of radioactive sulfate in the high-density form. The high-density proteoglycan interacted in affinity chromatography by virtue of its heparan sulfate chains with laminin, fibronectin, the globular domain NC1 and the triple helix of collagen IV. These interactions were abolished at moderate concentrations of NaCl (0.1-0.2 M) and in the presence of heparin, chondroitin sulfate or dextran sulfate. Interactions with the globule NC1 could also be demonstrated by velocity band centrifugation in sucrose gradients and a binding constant of about 10(6) M-1 was derived.
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PMID:Structure and interactions of heparan sulfate proteoglycans from a mouse tumor basement membrane. 623 80

The possibility has been investigated that 1) the supplements required for the growth of the Madin Darby Canine Kidney (MDCK) cell line in serum-free Medium K-1 are indeed requirements for the growth of normal kidney cells in vitro, and 2) that alterations in these growth requirements are associated with malignant transformation. Consistent with the hypothesis that MDCK cells resemble normal kidney cells in culture, primary cultures of baby mouse kidney epithelial cells grow in Medium K-1 and respond to the 5 components in the medium. The growth properties of Moloney sarcoma virus (MSV)-transformed MDCK cells in defined media have been examined. Unlike MDCK cells, MSV-transformed MDCK cells form tumors in adult nude mice. Although they still respond to the 5 factors in Medium K1, the optimal dosage for insulin is lower for the MSV transformants than for MDCK cells. The MSV transformants also have an additional requirement for growth in Medium K-1-fibronectin. Variants of MDCK cells have been isolated that have lost the PGE1 requirement for growth in defined medium. These variant cells have acquired 1) the ability to form tumors in adult nude mice and 2) an alteration affecting cAMP metabolism, in addition to PGE1 independence.
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PMID:Alterations in growth requirements of kidney epithelial cells in defined medium associated with malignant transformation. 626 6

Mouse embryo Mus musculus castaneous epithelial cells, transformed with Moloney murine sarcoma virus (MSV) or with ecotropic murine leukemia virus (MuLV), were analyzed for production of pericellular matrix glycoproteins. The nontransformed, MSV-transformed, and MuLV-transformed cells produced fibronectin, laminin, type I collagen, and small amounts of type III collagen when studied by immunofluorescence using specific antibodies. The virus-transformed epithelial cells produced enhanced amounts of fibronectin into their growth media. Nontransformed M. musculus castaneous epithelial cells mainly produced type I collagen, as shown by metabolic labeling and polypeptide analysis. A significant increase in the glycoprotein production was seen by the MuLV-transformed cells, whereas small changes in the collagen production were apparent after MSV transformation. MuLV-transformed cells produced increased amounts of type I collagen and also some collagenous polypeptides that comigrated with procollagen type IV chains. The ratio of the procollagen type I chains deposited in the matrix was altered in transformed cells. Radioactive surface labeling of the cells revealed changes of the high-molecular-weight glycoproteins in both the MSV- and the MuLV-transformed cells. Unlike virus-transformed fibroblastic cells, these transformed epithelial cells deposited and retained connective tissue glycoproteins in their pericellular matrices. The results indicate that viral transformation modulates the pericellular matrix and surface glycoproteins of cultured mouse epithelial cels. The ability of virus-transformed epithelial cells to deposit pericellular matrices is a major difference between them and virus-transformed fibroblastic cells.
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PMID:Pericellular matrix and cell surface glycoproteins of virus-transformed mouse epithelial cells. 627 76

Mouse embryo epithelial cells MMC-E were transformed by novel fibrosarcoma-inducing murine sarcoma virus 3611-MSV. The cells were analyzed for the production and deposition of pericellular glycoproteins by immunofluorescence and by radioactive metabolic and cell surface labeling techniques followed by analysis in polyacrylamide gels and fluorography. The pericellular fibronectin matrix was lost, but unlike in virus-transformed fibroblastic cells, the production of fibronectin was not affected. The major differences detected were decrease in collagen production and initiation of synthesis of two major glycoproteins with Mr 58,000 and 60,000. Cell surface carbohydrate labeling indicated that after 3611-MSV transformation the cells expressed Mr 100,000 and 68,000 polypeptides. The present and previous results show that viral transformation of epithelial cells induces different transformed phenotypes that are associated with distinct alterations in pericellular glycoproteins.
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PMID:Transformation of MMC-E epithelial cells by acute 3611-MSV: inhibition of collagen synthesis and induction of novel polypeptides. 630 14

Human plasma fibronectin bound to confluent cell layers of cultured human-skin fibroblasts in two distinct pools. Initial binding of fibronectin occurred in a deoxycholate-soluble pool (Pool I). Binding in Pool I was reversible and reached a steady state after 3 h. After longer periods of incubation, fibronectin became bound in a deoxycholate-insoluble pool (Pool II). Binding in Pool II was irreversible and proceeded at a linear rate for 30 h. After 30 h of incubation, a significant proportion of fibronectin bound in Pool II was present as disulfide-bonded multimers. HT1080 cells, a human sarcoma cell line, did not bind fibronectin in either pool. Also, isolated cell matrices prepared by deoxycholate extraction did not bind fibronection. Binding of fibronectin in Pool I of normal fibroblasts occurred via specific, saturable receptors. There were 128,000 binding sites per cell, and KDiss was 3.6 X 10(-8) M. Fluorescence microscopic localization of fibronectin bound in Pool I and Pool II was performed using fluorescein-conjugated fibronectin. Fluorescent staining in Pool I was present in a punctate pattern and in short, fine fibrils. Pool II fluorescence was exclusively in coarse, dense fibrils. These data indicate that plasma fibronectin may become incorporated into the tissue extracellular matrix via specific cell-surface receptors.
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PMID:Binding of plasma fibronectin to cell layers of human skin fibroblasts. 630 61

Our interest was aroused by the recent report by Huttner [ Huttner , W. B. (1982) Nature (London) 299, 273-276] on general sulfation of tyrosine residues of proteins in normal and malignantly transformed tissues. Here we report on the reduction of sulfation in embryonic rat fibroblasts, line 3Y1, infected with Rous sarcoma virus or Fujinami sarcoma virus. In view of the instability of tyrosine O-sulfate in strong acid, the protein sulfation was tested for after incubation with [35S]sulfate and exhaustive Pronase hydrolysis. We found in general a reduction of sulfation in transformed tissue. It was greatest in the fibroblasts permanently transformed with Rous sarcoma virus. When fibroblasts transformed by the temperature-sensitive Fujinami sarcoma virus, line ts225 -3Y1, were used for comparison of sulfation at nonpermissive and permissive temperatures, the latter showed a strong reduction. Furthermore, we tested these cells for the uptake of inorganic [35S]sulfate. Uptake appeared highly reduced in the permanently infected fibroblasts, but ts225 -3Y1 grown at permissive and nonpermissive temperatures exhibited no difference. Uptake at both temperatures was comparable to uptake by normal 3Y1 cells. A recently much investigated cell surface protein, fibronectin, was reported to be lost on malignant transformation and to contain sulfate in an undetermined location. We found that ts225 -3Y1 cells grown at permissive temperature released fibronectin that contained tyrosine O-sulfate.
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PMID:Decrease of tyrosine-O-sulfate-containing proteins found in rat fibroblasts infected with Rous sarcoma virus or Fujinami sarcoma virus. 632 24

In culture fibroblasts, endothelial cells and smooth muscle cells from arterial wall are stimulated by thrombin and factor XIII, whereas fibronectin inhibits the proliferation of these cells. Experiments with tumor cells show growth stimulation of sarcoma cells and HeLa cells by thrombin and factor XIII. While growth of sarcoma cells is inhibited by fibronectin, HeLa cells are stimulated by fibronectin in physiological concentrations. Possible mechanisms of these effects and relations to in vivo-phenomena are discussed.
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PMID:[Thrombin, factor XIII and fibronectin as regulators of the proliferation of tumor cells and vascular wall cells]. 634 11


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