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  • GENE-EXPRESSION  (4)
Keywords
  • 1
    Keywords: CELLS ; EXPRESSION ; INHIBITOR ; tumor ; BLOOD ; Germany ; INHIBITION ; KINASE ; SYSTEM ; DISEASE ; DISEASES ; ENZYMES ; GENE ; GENE-EXPRESSION ; GENES ; NF-KAPPA-B ; ACTIVATION ; IFN-GAMMA ; FAMILY ; AP-1 ; SKIN ; T-CELL ; T-CELLS ; cytokines ; gene expression ; CYCLOSPORINE-A ; PROMOTER ; UP-REGULATION ; DERIVATIVES ; PROTEIN-KINASES ; Jun ; KAPPA-B ; PERIPHERAL-BLOOD ; TNF-ALPHA ; asthma ; INHIBITORS ; PROGRAM ; RE ; IMMUNE-SYSTEM ; INFLAMMATORY CYTOKINES ; CYTOKINE PRODUCTION ; JNK ; KINASES ; FACTOR-ALPHA GENE ; IL-4 GENE
    Abstract: Aglaia (family Meliaceae) plants are used in traditional medicine (e.g., in Vietnam) for the treatment of inflammatory skin diseases and allergic inflammatory disorders such as asthma. Inflammatory diseases arise from inappropriate activation of the immune system, leading to abnormal expression of genes encoding inflammatory cytokines and tissue-destructive enzymes. The active compounds isolated from these plants are derivatives of rocaglamide. In this study we show that rocaglamides are potent immunosuppressive phytochemicals that suppress IFN-gamma, TNF-alpha, IL-2, and IL-4 production in peripheral blood T Cells at nanomolar concentrations. We demonstrate that rocaglamides inhibit cytokine gene expression at the transcriptional level. At the doses that inhibit cytokine production, they selectively block NF-AT activity without impairing NF-kappa B and AP-1. We also show that inhibition of NF-AT activation by rocaglamide is mediated by strong activation of JNK and p38 kinases. Our study suggests that rocaglamide derivatives may serve as a new source of NF-AT-specific inhibitors for the treatment of certain inflammatory diseases
    Type of Publication: Journal article published
    PubMed ID: 15905551
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  • 2
    Keywords: CANCER ; Germany ; IN-VIVO ; imaging ; VISUALIZATION ; GENE-EXPRESSION ; MAGNETIC-RESONANCE ; magnetic resonance imaging ; PROSTATE-CANCER
    Type of Publication: Journal article published
    PubMed ID: 12941791
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  • 3
    Keywords: APOPTOSIS ; CELLS ; EXPRESSION ; GROWTH ; INVASION ; tumor ; carcinoma ; IN-VIVO ; GENE ; GENE-EXPRESSION ; COMPLEX ; COMPLEXES ; DOMAIN ; INDUCTION ; cell cycle ; CELL-CYCLE ; CYCLE ; ALPHA ; antibodies ; antibody ; PROGRESSION ; gene expression ; SUBUNIT ; PLASMA ; MEMBRANE ; TUMOR PROGRESSION ; METASTASIS ; SIGNALING PATHWAYS ; CANCER-CELLS ; EXTRACELLULAR-MATRIX ; BETA ; LOCALIZATION ; ADHESION ; MIGRATION ; TRANSFORMATION ; PLASMA-MEMBRANE ; EPITHELIAL-CELLS ; INTEGRIN ; SUBUNITS ; GROWTH-FACTOR-BETA ; Ras ; ALPHA-6-BETA-4 INTEGRIN ; FACTOR-BETA ; MATRIX ; PROGRAM ; RE ; collagen ; extracellular matrix ; TRANSITION ; TGF-BETA ; EPITHELIAL-MESENCHYMAL TRANSITIONS ; plasma membrane ; MOLECULAR-MECHANISMS ; TGF beta ; EXTRACELLULAR-MATRIX PROTEINS ; laminin ; EMT ; fibronectin receptor ; laminin receptor
    Abstract: In nontumorigenic mammary epithelial cells (EpH4), transforming growth factor-beta (TGF beta 1) causes cell cycle arrest/apoptosis, but induces epitheliomesenchymal transition (EMT) in Ha-Ras-transformed EpH4 cells (EpRas). EMT is closely correlated with late-stage tumor progression and results in fibroblastic, migratory cells displaying a mesenchymal gene expression program (FibRas). EpRas and FibRas cells showed strongly increased cell substrate adhesion to fibronectin, collagens I/IV and laminin 1. Furthermore, Ras transformation caused enhanced or de-novo expression of the integrin subunits beta 1, alpha 2 and alpha 3, or alpha 5 and alpha 6, respectively, the latter subunits being even more strongly expressed in FibRas cells. Importantly, polarized EpRas cells expressed integrin subunits beta 1 and beta 6 at distinct (apical and lateral) membrane domains, while FibRas cells coexpressed these integrins and alpha 5 at the entire plasma membrane. During EMT, EpRas cells formed an alpha 5 beta 1 complex and deposited its ligand fibronectin into the extracellular matrix. Function-blocking alpha 5 antibodies attenuated migration, and caused massive apoptosis in EpRas cells undergoing TGF beta 1-induced EMT in collagen gels, but failed to affect EpRas- or FibRas-derived structures. We conclude that functional alpha 5b1 integrin is centrally implicated in EMT induction. Importantly, FibRas cells also failed to deposit the alpha 6 beta 4 ligand laminin 5, suggesting that alpha 6 beta 4 is no longer functional after EMT and replaced by mesenchymal integrins such as alpha 5 beta 1
    Type of Publication: Journal article published
    PubMed ID: 15688013
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  • 4
    Keywords: CANCER ; CELLS ; EXPRESSION ; CELL ; Germany ; MICROSCOPY ; IMAGES ; QUANTIFICATION ; SYSTEM ; TOOL ; DISEASE ; DISEASES ; GENE ; GENE-EXPRESSION ; GENES ; EFFICIENCY ; TISSUE ; gene transfer ; GENE-TRANSFER ; TISSUES ; SEQUENCE ; treatment ; FREQUENCY ; FREQUENCIES ; NUCLEI ; TARGET ; TRANSPORT ; gene expression ; EFFICIENT ; DELIVERY ; LOCALIZATION ; molecular ; review ; HELA-CELLS ; REPORTER GENE ; development ; analysis ; methods ; NUCLEAR ; cancer research ; PLASMID ; TOXICOLOGY ; DIVISION ; transfer efficiency ; German ; nuclear localization ; PLASMIDS ; scanning ; TRANSPORT-SYSTEM
    Abstract: An efficient gene transfer into target tissues and cells is needed for safe and effective treatment of genetic diseases like cancer. In this paper, we describe the development of a transport system and show its ability for transporting plasmids. This non-viral peptide-based BioShuttle-mediated transfer system consists of a nuclear localization address sequence realizing the delivery of the plasmid phNIS-IRES-EGFP coding for two independent reporter genes into nuclei of HeLa cells. The quantification of the transfer efficiency was achieved by measurements of the sodium iodide symporter activity. EGFP gene expression was measured with Confocal Laser Scanning Microscopy and quantified with biostatistical methods by analysis of the frequency of the amplitude distribution in the CLSM images. The results demonstrate that the "BioShuttle"-Technology is an appropriate tool for an effective transfer of genetic material carried by a plasmid.
    Type of Publication: Journal article published
    PubMed ID: 18026568
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