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  • EXPRESSION  (7)
  • 1
    Keywords: PROTEINS ; EXPRESSION ; CELL ; Germany ; BIOLOGY ; keratin ; INTERMEDIATE-FILAMENTS ; cytoskeleton ; RE ; review ; GENE DOMAIN ; FOLLICLE ; HUMAN TYPE-I ; intermediate filament ; HAIR FOLLICLE ; keratins ; ALPHA-KERATIN ; COMPANION LAYER ; EPITHELIAL KERATIN ; hair ; hair keratins ; INNERMOST CELL LAYER ; OUTER ROOT SHEATH ; RESOLUTION 2-DIMENSIONAL ELECTROPHORESIS
    Abstract: Intermediate filaments are a large family of proteins that are the cytoskeletal elements involved in a number of skin, liver, neuromuscular, cardiac, eye and hair diseases. Intermediate filament genes are regulated in a tissue-and cell type-specific manner and their polymerized protein products protects the cells and tissue they are part of against a variety of mechanical and nonmechanical stresses. This book provides a comprehensive resource of methodology essentials, describing a variety of essential tools and assays for studying intermediate filaments. The book provides user-friendly advice and protocols covering all aspects of intermediate filaments including protein isolation and structure, protein and gene regulation, relationship to disease and apoptosis, and associated proteins. Both mammalian and non-mammalian systems and animal models are covered, making this book a must-have for any investigator wishing to study IF genes or their protein products. This book covers intermediate filaments from crystallography, protein chemistry, cell and molecular biology, microrheology, gene regulation, to animal models and human disease. It is practical and user-friendly with detailed 'how-to-protocols and tricks of the trade'. It includes detailed tables of useful reagents, vendors and web links. Synopsis Intermediate filaments are a large family of proteins that are the cytoskeletal elements involved in a number of skin, liver, neuromuscular, cardiac, eye and hair diseases. Intermediate filament genes are regulated in a tissue- and cell type-specific manner and their polymerized protein products protects the cells and tissue they are part of against a variety of mechanical and nonmechanical stresses. This book provides a comprehensive resource of methodology essentials, describing a variety of essential tools and assays for studying intermediate filaments. The book provides user-friendly advice and protocols covering all aspects of intermediate filaments including protein isolation and structure, protein and gene regulation, relationship to disease and apoptosis, and associated proteins. Both mammalian and non-mammalian systems and animal models are covered, making this book a must-have for any investigator wishing to study IF genes or their protein products. This book covers intermediate filaments from crystallography, protein chemistry, cell and molecular biology, microrheology, gene regulation, to animal models and human disease. It is practical and user-friendly with detailed 'how-to-protocols' and 'tricks of the trade'. It includes detailed tables of useful reagents, vendors and web links.
    Type of Publication: Book chapter
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  • 2
    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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  • 3
    Keywords: EXPRESSION ; tumor ; Germany ; human ; MICROSCOPY ; SUPPORT ; liver ; primary ; hepatocytes ; DOWN-REGULATION ; ASSOCIATION ; ISOFORM ; STAGE ; UP-REGULATION ; DECREASE ; MEMBRANE ; LOCALIZATION ; MULTIDRUG-RESISTANCE PROTEIN ; HUMAN LIVER ; ORGANIZATION ; ABCC2 ; CONJUGATE EXPORT PUMP ; MRP2 ; ELIMINATION ; HUMAN-LIVER ; CANALICULAR MEMBRANES ; CHOLESTATIC RAT-LIVER ; CROSS-LINKING ; OBSTRUCTIVE CHOLESTASIS ; organic anion transporters,radixin,multidrug resistance protein,primary biliary cirrhosis,immunofluo
    Abstract: Background/Aims: Expression and localization of human hepatocellular transporters and of radixin, cross-linking actin with some membrane transporters, may change in cholestatic liver diseases.Methods: We investigated the uptake transporters OATP2 (SLC21A6), OATP8 (SLC21A8), and NTCP (SLC10A1), the export pumps MRP2 (ABCC2), MRP3 (ABCC3), MRP6 (ABCC6), and P-glycoproteins (ABCB1, ABCB4, ABCB11), and radixin, in non-icteric primary biliary cirrhosis (PBC stages I-III) and control human liver needle-biopsies using immunofluorescence microscopy and semi-quantitative RT-PCR.Results: Expression and localization of all transporters were unchanged in PBC I-II. Immunostaining intensities of uptake transporters decreased in PBC III with a concomitant decrease in mRNA levels. Immunostaining intensities and mRNA levels of export pumps were similar in controls and PBC I-III, however, irregular MRP2 immunostaining suggested redistribution of MRP2 into intracellular structures in PBC III. Areas of irregular MRP2 immunostaining showed largely reduced radixin immunostaining, whereas normal hepatocytes had MRP2 and radixin confined to the canalicular membrane. Disrupted localization of radixin and MRP2 supports the concept that radixin contributes to the canalicular localization of MRP2.Conclusions: Down-regulation of uptake transporters may contribute to the impaired hepatobiliary elimination in advanced PBC, and partially altered localization of MRP2 may reflect the onset of changes leading to icteric PBC. (C) 2003 European Association for the Study of the Liver. Published by Elsevier B.V. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 14568249
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  • 4
    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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  • 5
    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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  • 6
    Keywords: EXPRESSION ; HEPATOCELLULAR-CARCINOMA ; PROTEIN ; PROMOTER ; HETEROZYGOSITY ; MUTATIONS ; WILD-TYPE P53 ; osteosarcoma ; MDM-2 ONCOGENE ; P19(ARF)
    Abstract: The genesis of hepatocellular carcinoma is promoted by changes in the regulatory MDM2-P14ARF system. The incidence of such changes has to date not been analysed in non-tumourous livers showing regenerative proliferation. In the present study, 24 cirrhotic livers of alcohol-, autoimmue disorder- or HCV-caused genesis were screened for MDM2-P14ARF alterations at the level of protein, DNA and mRNA. Using confocal laser scanning microscopy, the absence of MDM2 and P14ARF expression was detected in all samples except three HCV-infected livers (four livers) which contained hepatocytes overexpressing MDM2 (P14ARF) protein. In two of the samples lacking P14ARF expression, laser microdissection and PCR demonstrated deletion of the P14ARF gene. The P14ARF gene amplified from other specimens did not carry mutations. MDM2 splicing variants were present in tissues from alcohol- and autoimmune disorder-induced cirrhoses. Sequencing of full-size mRNA revealed a MDM2 mis-sense mutation in an alcohol-induced cirrhosis. One sample contained regenerative nodules with genetic instability occurring at MDM2 locus D12S83 according to the data of automatic PCR fragment analysis. In summary, this study gives first evidence for different types of MDM2 and P14ARF alterations in cirrhotic livers. We suggest that the changes impair the regulatory MDM2-P14ARF system, thus possibly favouring regenerative proliferation and transformation.
    Type of Publication: Journal article published
    PubMed ID: 11953887
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  • 7
    Keywords: EXPRESSION ; NITRIC-OXIDE ; kidney ; MEMBRANE ; physiology ; SMOOTH-MUSCLE ; CONJUGATE EXPORT PUMP ; CYCLIC-GMP ; MOAT-C ; SILDENAFIL
    Abstract: PURPOSE: The intracellular messenger cyclic guanosine monophosphate (cGMP) has an important role in regulating smooth muscle tone. An increase in intracellular cGMP levels is a prerequisite for penile erection. Inhibition of cGMP degradation by cGMP specific phosphodiesterase 5 has been used for treating erectile dysfunction. In addition to degradation by phosphodiesterase, cGMP is exported from cells by multidrug resistance protein 5 (MRP5), also called ABCC5, which we recently identified as an adenosine triphosphate dependent export pump for cGMP. MRP5 is potently inhibited by substances known as phosphodiesterase inhibitors, including sildenafil and trequinsin. Therefore, we analyzed whether MRP5 is expressed in tissues of the human genitourinary system and whether MRP5 and phosphodiesterase 5 proteins are localized in the same cell types. MATERIALS AND METHODS: Localization of MRP5 and phosphodiesterase 5 was analyzed by immunofluorescence microscopy in cryosections of various tissues of the human genitourinary system. RESULTS: MRP5 and phosphodiesterase 5 were co-expressed in smooth muscle cells of the corpus cavernosum, ureter, urethra and bladder. In addition, MRP5 and phosphodiesterase 5 were localized in epithelial cells of the mucosa in the ureter and urethra, and in blood vessels of the lamina propria. CONCLUSIONS: The co-expression of MRP5 and phosphodiesterase 5 in smooth muscle cells of the genitourinary system indicates 2 distinct pathways for cGMP removal. Thus, MRP5 inhibition represents a new approach for enhancing cGMP levels in smooth muscle cells and developing drugs for erectile dysfunction.
    Type of Publication: Journal article published
    PubMed ID: 11956491
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