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Human Colon Carcinoma Cells (human + colon_carcinoma_cell)

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Chemistry50%

Terms modified by Human Colon Carcinoma Cells

  • human colon carcinoma cell line
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    Selected Abstracts

    In vivo and in vitro Interactions between Human Colon Carcinoma Cells and Hepatic Stellate Cells

    CANCER SCIENCE, Issue 12 2000
    Sadatoshi Shimizu
    Stromal reaction is important for the growth of cancer both in primary and metastatic sites. To demonstrate this reaction during the hepatic metastasis of human colon carcinoma, we histologically investigated alterations to the distribution and phenotype of hepatic stellate cells (HSCs), the only mesenchymal cells in the liver parenchyma, using a nude mouse model. Intrasplenically injected colon carcinoma LM-H3 cells migrated into the space of Disse and underwent proliferation, in close association with hepatocytes and HSCs, at 2 days. At 14 days, HSCs were accumulated around the tumor mass and expressed ,-smooth muscle actin, a marker for HSC activation. We next investigated in vitro the growth factors involved in the interactions between LM-H3 cells and HSCs. Conditioned medium of rat HSCs which underwent culture-induced activation contained platelet-derived growth factor (PDGF)-AB, hepatocyte growth factor (HGF) and transforming growth factor (TGF),, and could augment LM-H3-cell proliferation and migration. Neutralizing antibodies against PDGF-AA and PDGF-BB and those against PDGF-BB and HGF inhibited proliferation and migration, respectively, of LM-H3 cells, whereas antibody against TGF-, had no effect. LM-H3 cells expressed PDGF receptors-, and -, and c-met. Conditioned medium of LM-H3 cells contained PDGF-AB, and could enhance HSC proliferation and migration. This augmenting effect was suppressed by treatment with anti-PDGF-AB antibody. The present study has demonstrated that bidirectional interactions involving PDGF and HGF take place in vitro between colon carcinoma cells and HSCs, raising the possibility that similar interactions might be involved in the stromal reaction during hepatic metastasis. [source]

    TSC-box is essential for the nuclear localization and antiproliferative effect of XTSC-22

    DEVELOPMENT GROWTH & DIFFERENTIATION, Issue 3 2007
    Akiko Hashiguchi
    Transforming growth factor- ,1-stimulated clone 22 (TSC-22) encodes a leucine zipper-containing protein that is highly conserved among various species. Mammalian TSC-22 is a potential tumor suppressor gene. It translocates into nuclei and suppresses cell division upon antiproliferative stimuli. In human colon carcinoma cells, TSC-22 inhibits cell growth by upregulating expression of the p21 gene, a cyclin-dependent kinase (Cdk) inhibitor. We previously showed that the Xenopus laevis homologue of the TSC-22 gene (XTSC-22) is required for cell movement during gastrulation through cell cycle regulation. In this report, we investigated the molecular mechanism of the antiproliferative effect of XTSC-22. Reverse transcriptase-polymerase chain reaction (RT-PCR) analysis suggested that XTSC-22 did not affect the expression levels of the p21 family of Cdk inhibitors or other cell cycle regulators. Analysis of deletion mutants of XTSC-22 revealed that nuclear localization of the N-terminal TSC-box is necessary for cell cycle inhibition by XTSC-22. Further experiments suggested that p27Xic1, a key Cdk inhibitor in Xenopus, interacts with XTSC-22. Because p27Xic1 is a cell cycle inhibitor with a nuclear localization signal, it is possible that XTSC-22 suppresses cell division by translocating into the nucleus with p27Xic1, where it may potentiate the intranuclear action of p27Xic1. [source]

    Group IID heparin-binding secretory phospholipase A2 is expressed in human colon carcinoma cells and human mast cells and up-regulated in mouse inflammatory tissues

    FEBS JOURNAL, Issue 11 2002
    Makoto Murakami
    Group IID secretory phospholipase A2 (sPLA2 -IID), a heparin-binding sPLA2 that is closely related to sPLA2 -IIA, augments stimulus-induced cellular arachidonate release in a manner similar to sPLA2 -IIA. Here we identified the residues of sPLA2 -IID that are responsible for heparanoid binding, are and therefore essential for cellular function. Mutating four cationic residues in the C-terminal portion of sPLA2 -IID resulted in abolition of its ability to associate with cell surface heparan sulfate and to enhance stimulus-induced delayed arachidonate release, cyclooxygenase-2 induction, and prostaglandin generation in 293 cell transfectants. As compared with several other group II subfamily sPLA2s, which were equally active on A23187- and IL-1-primed cellular membranes, sPLA2 -IID showed apparent preference for A23187-primed membranes. Several human colon carcinoma cell lines expressed sPLA2 -IID and sPLA2 -X constitutively, the former of which was negatively regulated by IL-1. sPLA2 -IID, but not other sPLA2 isozymes, was expressed in human cord blood-derived mast cells. The expression of sPLA2 -IID was significantly altered in several tissues of mice with experimental inflammation. These results indicate that sPLA2 -IID may be involved in inflammation in cell- and tissue-specific manners under particular conditions. [source]

    Glycoproteomics and glycomics investigation of membrane N -glycosylproteins from human colon carcinoma cells

    PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 16 2008
    Anne-Sophie Vercoutter-Edouart Dr.
    Abstract Aberrant glycosylation of proteins is known to profoundly affect cellular adhesion or motility of tumoral cells. In this study, we used HT-29 human colon epithelial cancer cells as a cellular model of cancer progression, as they can either proliferate or differentiate into enterocyte phenotype. A glycoproteomic approach based on Con A lectin-affinity chromatography, SDS-PAGE and MS analysis, allowed the identification of membrane N -glycoproteins from Triton X-100-solubilized proteins from membrane preparation. Among them, 65% were membrane proteins, and 45% were known to be N -glycosylated, such as , chains integrin and dipeptidyl isomerase IV. By lectin-blot analysis, significant changes of ,-2,3- and ,-2,6-sialylation of membrane glycoproteins were observed between proliferating and differentiated HT-29 cells. From these results, nano-LC-MS/MS analysis of the tryptic digests of the corresponding bands was performed and led to the identification of several transmembrane glycoproteins, like members of the solute carrier family and adhesion proteins. Finally, we compared N -glycans profiles and monosaccharide composition of proliferating and enterocyte-like HT-29 cells using MALDI-MS and GC-MS analyses of permethylated derivatives. This glycomic approach allowed to underscore significant changes in N -glycans structure, in particular the expression of atypical N -acetylglucosamine (GlcNAc)-ended N -glycans in enterocyte-like HT-29 cells. [source]