chondroitin-sulfates and Cell-Transformation--Viral

chondroitin-sulfates has been researched along with Cell-Transformation--Viral* in 11 studies

Reviews

2 review(s) available for chondroitin-sulfates and Cell-Transformation--Viral

ArticleYear
Cell-surface glycosaminoglycans.
    Annual review of biochemistry, 1984, Volume: 53

    Topics: Animals; Cell Membrane; Cell Transformation, Neoplastic; Cell Transformation, Viral; Cells, Cultured; Chemical Phenomena; Chemistry; Chondroitin Sulfates; Collagen; Fibronectins; Glycosaminoglycans; Humans; Hyaluronic Acid; Laminin; Proteoglycans

1984
Developmental roles of hyaluronate and chondroitin sulfate proteoglycans.
    Society of General Physiologists series, 1977, Volume: 32

    Topics: Animals; Cartilage; Cell Differentiation; Cell Movement; Cell Transformation, Viral; Chick Embryo; Chondroitin; Chondroitin Sulfates; Collagen; Cornea; Extremities; Hyaluronic Acid; Hyaluronoglucosaminidase; Lipid Metabolism; Morphogenesis; Proteoglycans; Time Factors

1977

Other Studies

9 other study(ies) available for chondroitin-sulfates and Cell-Transformation--Viral

ArticleYear
Interleukin-1 beta-modulated gene expression in immortalized human chondrocytes.
    The Journal of clinical investigation, 1994, Volume: 94, Issue:6

    Immortalized human chondrocytes were established by transfection of primary cultures of juvenile costal chondrocytes with vectors encoding simian virus 40 large T antigen and selection in suspension culture over agarose. Stable cell lines were generated that exhibited chondrocyte morphology, continuous proliferative capacity (> 80 passages) in monolayer culture in serum-containing medium, and expression of mRNAs encoding chondrocyte-specific collagens II, IX, and XI and proteoglycans in an insulin-containing serum substitute. They did not express type X collagen or versican mRNA. These cells synthesized and secreted extracellular matrix molecules that were reactive with monoclonal antibodies against type II collagen, large proteoglycan (PG-H, aggrecan), and chondroitin-4- and chondroitin-6-sulfate. Interleukin-1 beta (IL-1 beta) decreased the levels of type II collagen mRNA and increased the levels of mRNAs for collagenase, stromelysin, and immediate early genes (egr-1, c-fos, c-jun, and jun-B). These cell lines also expressed reporter gene constructs containing regulatory sequences (-577/+3,428 bp) of the type II collagen gene (COL2A1) in transient transfection experiments, and IL-1 beta suppressed this expression by 50-80%. These results show that immortalized human chondrocytes displaying cartilage-specific modulation by IL-1 beta can be used as a model for studying normal and pathological repair mechanisms.

    Topics: Antigens, Viral, Tumor; Cartilage; Cell Line; Cell Transformation, Viral; Chondroitin Sulfates; Collagen; Cycloheximide; Fluorescent Antibody Technique; Gene Expression; Humans; Immunohistochemistry; Interleukin-1; Phenotype; Proteoglycans; Ribs; RNA, Messenger; Simian virus 40

1994
Sulfation of chondroitin sulfate secreted by baby hamster kidney cells and their polyoma virus-transformed counterparts.
    Journal of biochemistry, 1985, Volume: 98, Issue:4

    Sulfation of glycosaminoglycans (GAGs) secreted by baby hamster kidney (BHK) cells and the polyoma virus-transformants (PY-BHK) was investigated. It has been reported that chondroitin sulfate (CS) of cell membranes from PY-BHK cells is undersulfated compared to that from BHK cells (Cancer Res. 43, 2712-2717, 1983). In the first series of experiments of the present study, cells were incubated with [3H]glucosamine and [35S]sulfate, and GAGs isolated from the culture medium were examined. GAG composition was comparable between the BHK and PY-BHK cultures. Disaccharide analysis of the chondroitinase ACII digests of the hyaluronate lyase-resistant materials showed a high proportion (68% for BHK and 47% for PY-BHK) of delta Di-0S, with delta Di-4S (32% for BHK and 53% for PY-BHK) as the major sulfated disaccharide on the basis of 3H-radioactivities. The beta-D-xyloside treatment did not alter the degree of undersulfation of the CS of either culture. In the second series of experiments, disaccharide analysis of the chondroitinase ABC digests of unlabeled GAGs demonstrated similar disaccharide composition for the two cell types. The BHK and PY-BHK preparations showed 28 and 17% (mol percent) of delta Di-0S, 58 and 72% of delta Di-4S, and 14 and 11% of delta Di-6S, respectively. These results indicate a considerable degree of undersulfation of secretory CS from both cells, and a slightly higher degree, if any, of under-sulfation of secretory CS from BHK cells if compared between the two cell types, which is in contrast to the results reported for membrane CS.

    Topics: Animals; Cell Line; Cell Transformation, Viral; Chondroitin; Chondroitin Sulfates; Chondroitinases and Chondroitin Lyases; Cricetinae; Disaccharides; Glycosaminoglycans; Kidney; Polyomavirus; Sulfurtransferases

1985
Endogenous hyaluronate-cell surface interactions in 3T3 and simian virus-transformed 3T3 cells.
    The Journal of biological chemistry, 1984, Aug-10, Volume: 259, Issue:15

    3T3 cells have a large, pericellular coat which contains 30 times more hyaluronate than the amount of cell surface hyaluronate associated with simian virus 40-transformed 3T3 (SV-3T3) cells. On the other hand, SV-3T3 cells have high affinity binding sites for exogenously added hyaluronate, whereas 3T3 cells have much lower affinity sites. Removal of cell surface hyaluronate from SV-3T3 cells by treatment with hyaluronidase caused a reproducible increase in their maximum binding capacity for exogenous hyaluronate but no significant change in binding affinity or specificity. For 3T3 cells, however, the maximum amount of binding decreased and the affinity of binding increased after hyaluronidase treatment. When endogenous cell surface hyaluronate was labeled metabolically and then the cells incubated in the presence of exogenous unlabeled hyaluronate, the labeled cell surface hyaluronate was quantitatively displaced from the SV-3T3 cells but was not displaced from the 3T3 cells. Chondroitin sulfate and heparin did not displace cell surface hyaluronate from either cell type. Membranes isolated from SV-3T3 cells bound hyaluronate specifically and with high affinity, whereas membranes from 3T3 cells did not consistently bind a significant amount of hyaluronate. We conclude from these studies that the retention of endogenous hyaluronate on the surface of SV-3T3 cells is mediated by binding sites similar to those detected by the addition of exogenous hyaluronate, and the mechanism of retention of endogenous hyaluronate on the surface of 3T3 cells differs from SV-3T3 cells.

    Topics: Animals; Cell Line; Cell Transformation, Viral; Chondroitin Sulfates; Fibroblasts; Heparin; Hyaluronic Acid; Hyaluronoglucosaminidase; Kinetics; Mice; Osmolar Concentration; Simian virus 40; Surface Properties

1984
Transformation by Rous sarcoma virus induces similar patterns of glycosaminoglycan synthesis in chick embryo skin fibroblasts and vertebral chondroblasts.
    The Journal of biological chemistry, 1983, Jan-25, Volume: 258, Issue:2

    Chick embryo skin fibroblasts and vertebral chondroblasts were infected with a temperature-sensitive mutant of Rous sarcoma virus, LA24A, and were grown at permissive (36 degrees C) and nonpermissive (41 degrees C) temperatures. During exponential growth, infected and parallel uninfected cultures were labeled with D-[3H]glucosamine, and newly synthesized glycosaminoglycans were identified by anion exchange chromatography and by selective enzymatic and chemical degradations. Control fibroblasts synthesized low levels of hyaluronic acid (HA), and dermatan sulfate (DS), moderate levels of heparan sulfate (HS), and high levels of chondroitin sulfate (CS). In contrast, control chondroblasts synthesized very low levels of HA and DS, no HS, and very high levels of CS. Following transformation and growth at 36 degrees C, both cell types showed a dramatic increase in HA synthesis and a significant decrease in CS synthesis. In addition, transformed chondroblasts initiated the synthesis of HS and increased their synthesis of DS to levels that matched those of transformed fibroblasts. The CS chains synthesized by control chondroblasts were partially undersulfated, while those synthesized by both normal and transformed fibroblasts were fully sulfated. Upon transformation, chondroblasts grown at 36 degrees C initiated the synthesis of fully sulfated CS chains. Most of the above biosynthetic alterations were completely reversed when infected cells were grown at 41 degrees C, indicating that they were dependent on the transforming gene product of LA24A. Clearly, the profound differences that distinguish normal fibroblasts from normal chondroblasts are lost upon transformation, and these two types of terminally differentiated cells converge toward a common, though not identical, biosynthetic program for glycosaminoglycans.

    Topics: Animals; Avian Sarcoma Viruses; Cartilage; Cell Transformation, Viral; Chick Embryo; Chondroitin Sulfates; Dermatan Sulfate; Fibroblasts; Glycosaminoglycans; Heparitin Sulfate; Hyaluronic Acid; Sarcoma, Avian; Skin

1983
Selective solubilization of hyaluronic acid from fibroblast substratum adhesion sites.
    The Journal of biological chemistry, 1982, Dec-10, Volume: 257, Issue:23

    Topics: Animals; Cell Adhesion; Cell Transformation, Viral; Cells, Cultured; Chondroitin Sulfates; Fibroblasts; Glycoproteins; Guanidine; Guanidines; Heparitin Sulfate; Hyaluronic Acid; Hyaluronoglucosaminidase; Mice; Mice, Inbred BALB C; Simian virus 40; Solubility

1982
Role of sulfated mucopolysaccharides in cell recognition and neoplastic transformation.
    Anais da Academia Brasileira de Ciencias, 1980, Volume: 52, Issue:1

    Topics: Adult; Animals; Cell Division; Cell Transformation, Neoplastic; Cell Transformation, Viral; Cells, Cultured; Chemical Phenomena; Chemistry; Chondroitin Sulfates; Dogs; Glycosaminoglycans; Guinea Pigs; Heparitin Sulfate; Humans; Liver; Mice; Rabbits; Regeneration; Swine; Tissue Distribution

1980
Effect of growth conditions on the content of the major groups of carbohydrates in chick embryo fibroblasts.
    Cancer research, 1979, Volume: 39, Issue:7 Pt 1

    The levels of glycogen, hyaluronic acid, chondroitin sulfates, N-acetylneuraminic acid, all of the monosaccharide components of the glycoprotein and glycolipid fractions, and the monosaccharide pools were measured in cultured chick embryo fibroblasts. Under all growth conditions, the glycogen plus the glucose phosphate pool contained approximately 50% of total monosaccharide content of the cells. However, marked qualitative and quantitative alterations were found in the glycoprotein, glycolipid, and mucopolysaccharide fractions when growing cells reached confluence, when the growth temperature was shifted from 36 to 41 degrees, or when the cells were transformed with Rous sarcoma virus. From 65 to 95% of the total monosaccharide residues in these complex carbohydrates were found in the glycoprotein fraction, while the glycolipids contained only 5 to 10% of the residues, and the mucopolysaccharides contained 5 to 25%. Changes in the complex carbohydrates in normal cells following changes in cell density or growth temperature were so great that they obscured any transformation-dependent changes that might have occurred consistently in the virus-infected cells under different growth conditions.

    Topics: Animals; Avian Sarcoma Viruses; Carbohydrate Metabolism; Cell Division; Cell Transformation, Viral; Cells, Cultured; Chick Embryo; Chondroitin Sulfates; Fibroblasts; Glycogen; Hot Temperature; Hyaluronic Acid; Monosaccharides; Sialic Acids

1979
Shedding of hyaluronate from the cell surface of Rous sarcoma virus-transformed chondrocytes.
    The Journal of biological chemistry, 1979, Sep-10, Volume: 254, Issue:17

    Transformation of cultured chick embryo chondrocytes with Rous sarcoma virus gives rise to increased incorporation of isotopic precursors into hyaluronate and decreased incorporation into chondroitin 6-sulfate. Chemical measurements of these glycosaminoglycans showed corresponding changes. Comparison of the kinetics of production of glycosaminoglycan by normal and Rous sarcoma virus-transformed chondrocytes demonstrated (i) that the rate of accumulation in the medium was similar in both cultures, and (ii) that approximately 50% of total glycosaminoglycan produced by the normal chondrocytes, but only 10% of that from the transformed cells, accumulated in the cell layer. Prelabel-chase experiments indicated that cell surface-associated hyaluronate, as measured by release from the cell layer by trypsin treatment, was shed rapidly into the medium and accounted for all of the hyaluronate which accumulated in the medium. Thus we conclude (i) that accumulation of cell surface-associated glycosaminoglycan is dramatically reduced in Rous sarcoma virus-transformed chondrocytes, and (ii) that hyaluronate produced by the transformed chondrocytes is first deposited in the cell-associated extracellular compartment and then rapidly shed into the medium, rather than being secreted directly into the medium.

    Topics: Animals; Avian Sarcoma Viruses; Carbohydrates; Cartilage; Cell Membrane; Cell Transformation, Viral; Cells, Cultured; Chick Embryo; Chondroitin Sulfates; DNA; Glycosaminoglycans; Hyaluronic Acid; Kinetics

1979
Two functionally distinct pools of glycosaminoglycan in the substrate adhesion site of murine cells.
    The Journal of cell biology, 1978, Volume: 79, Issue:3

    Footpad adhesion sites pinch off from the rest of the cell surface during EGTA-mediated detachment of normal or virus-transformed murine cells from their tissue culture substrates. In these studies, highly purified trypsin and testicullar hyaluronidase were used to investigate the selective destruction or solubilization of proteins and polysaccharides in this substrate-attached material (SAM). Trypsin-mediated detachment of cells or trypsinization of SAM after EGTA-mediated detachment of cells resulted in the following changes in SAM composition: (a) solubilization of 50-70% of the glycosaminoglycan polysaccharide with loss of only a small fraction of the protein, (b) selective loss of one species of glycosaminoglycan-associated protein in longterm radiolabeled preparations, (c) no selective loss of the LETS glycoprotein or cytoskeletal proteins in longterm radiolabeled preparations, and (d) selective loss of one species of glycosaminoglycan-associated protein, a protion of the LETS glycoprotein, and proteins Cd (mol wt 47,000 and Ce' (mol wt 39,000) in short term radiolabeled preparations. Digestion of SAM with testicular hyaluronidase resulted in: (a) almost complete solubilization of the hyaluronate and chondroitin sulfate moieties from long term radiolabeled SAM with minimal loss of heparan sulfate, (b) solubilization of a small portion of the LETS glycoprotein and the cytoskeletal proteins from longterm radiolabeled SAM, (c) resistance to solubilization of protein and polysaccharide in reattaching cell SAM which contains principally heparan sulfate, and (d) complete solubilization of the LETS glycoprotein in short term radiolabeled preparations with no loss of cytoskeletal proteins. Thus, there appear to be two distinct pools of LETS in SAM, one associated in some unknown fashion with hyaluronate-chondroitin sulfate complexes, and a second associated with some other component in SAM, perhaps heparan sulfate. These data, together with other results, suggest that the cell-substrate adhesion process may be mediated principally by a heparan sulfate--LETS complex and that hyaluronate-chondroitin sulfate complexes may be important in the detachability of cells from the serum-coated substrate by destabilizing LETS matrices at posterior footpad adhesion sites.

    Topics: Animals; Cell Adhesion; Cell Line; Cell Separation; Cell Transformation, Neoplastic; Cell Transformation, Viral; Chondroitin Sulfates; Glycoproteins; Glycosaminoglycans; Heparitin Sulfate; Hyaluronic Acid; Mice; Neoplasm Proteins; Solubility

1978
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