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  • Germany  (13)
  • 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: 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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  • 4
    Keywords: CELLS ; tumor ; CELL ; Germany ; human ; SYSTEM ; PROTEIN ; PATIENT ; MATURATION ; ACID ; ACIDS ; TRANSPORT ; IDENTIFICATION ; resistance ; PLASMA ; MEMBRANE ; MUTATION ; LOCALIZATION ; EXCHANGE ; PLASMA-MEMBRANE ; DEGRADATION ; HEPATOCYTE CANALICULAR ISOFORM ; AMINO-ACIDS ; QUANTITATIVE-ANALYSIS ; DRUG-RESISTANCE ; MULTIDRUG-RESISTANCE ; ABCC2 ; ATP-dependent transport ; CONJUGATE EXPORT PUMP ; deficient protein maturation ; ENDOPLASMIC-RETICULUM ; GENE CAUSES ; HEPG2 CELLS ; MRP2 ; multidrug resistance protein 2 ; MULTIDRUG-RESISTANCE PROTEIN-2 ; ORGANIC ANION-TRANSPORTER ; protein trafficking ; SUBSTRATE-SPECIFICITY
    Abstract: Absence of a functional multidrug resistance protein 2 (MRP2; symbol ABCC2) from the hepatocyte canalicular membrane is the molecular basis of Dubin-Johnson syndrome, an inherited disorder associated with conjugated hyperbilirubinemia in humans. In this work, we analyzed a relatively frequent Dubin- Johnson syndrome mutation that leads to an exchange of two hydrophobic amino acids, isoleucine 1173 to phenylalanine (MRP2I1173F), in a predicted extracellular loop of MRP2. HEK- 293 cells stably transfected with MRP2I1173F cDNA synthesized a mutant protein that was mainly core-glycosylated, predominantly retained in the endoplasmic reticulum, and degraded by proteasomes. MRP2I1173F did not mediate ATP-dependent transport of leukotriene C-4 (LTC4) into vesicles from plasma membrane and endoplasmic reticulum preparations while normal MRP2 was functionally active. Human HepG2 cells were used to study localization of MRP2I1173F in a polarized cell system. Quantitative analysis showed that GFP-tagged MRP2I1173F was localized to the apical membrane in only 5% of transfected, polarized HepG2 cells compared with 80% for normal MRP2-GFP. Impaired protein maturation followed by proteasomal degradation of inactive MRP2I1173F explain the deficient hepatobiliary elimination observed in this group of Dubin-Johnson syndrome patients
    Type of Publication: Journal article published
    PubMed ID: 12388192
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  • 5
    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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  • 6
    Keywords: ANGIOGENESIS ; CANCER ; GROWTH-FACTOR ; tumor ; Germany ; RECRUITMENT ; HEMATOPOIETIC STEM-CELLS ; microenvironment ; chemokine ; RE ; TUMORIGENESIS ; progenitor ; MARROW-DERIVED CELLS ; MCP-1 ; MOBILIZATION ; neovascularization
    Type of Publication: Journal article published
    PubMed ID: 16326806
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  • 7
    Keywords: CELLS ; Germany ; PROTEIN ; PROTEINS ; METABOLISM ; desmosome ; COMPLEX ; COMPLEXES ; MESSENGER-RNA ; FAMILY ; BINDING ; PARTICLES ; IDENTIFICATION ; NUMBER ; STRESS ; EPITHELIAL-CELLS ; INVOLVEMENT ; OXIDATIVE STRESS ; INITIATION ; JUNCTIONS ; RE ; DESMOSOMAL PLAQUE ; TRANSLATION ; INTERCELLULAR-JUNCTIONS ; PLAQUE PROTEINS ; BAND-6 PROTEIN ; MENTAL-RETARDATION PROTEIN ; P120 CATENIN ; PROCESSING BODIES ; TRANSLATION INITIATION
    Abstract: Recent studies on the subcellular distribution of cytoplasmic plaque proteins of intercellular junctions have revealed that a number of such proteins can also occur in the cyto- and the nucleoplasm. This occurrence in different, and distant locations suggest that some plaque proteins play roles in cytoplasmic and nuclear processes in addition to their involvement in cell-cell adhesive interactions. Plakophilin (PKP) 3, a member of the arm-repeat family of proteins, occurs, in a diversity of cell types, both as an architectural component in plaques of desmosomes and dispersed in cytoplasmic particles. In immuno-selection experiments using PKP3-specific antibodies, we have identified by mass spectrometric analysis the following RNA-binding proteins: Poly (A) binding protein (PABPC1), fragile-X-related protein (FXR1), and ras-GAP-SH3-binding protein (G3BP). Moreover, the RNA-binding proteins codistributed after sucrose gradient centrifugation in PKP3-containing fractions corresponding to 25-35 S and 45-55 S. When cells are exposed to environmental stress (e.g., heat shock or oxidative stress) proteins FXR1, G3BP, and PABPC1 are found, together with PKP3 or PKP1, in "stress granules" known to accumulate stalled translation initiation complexes. Moreover, the protein eIF-4E and the ribosomal protein S6 are also detected in PKP3 particles. Our results show that cytoplasmic PKP3 is constitutively associated with RNA-binding proteins and indicate an involvement in processes of translation and RNA metabolism
    Type of Publication: Journal article published
    PubMed ID: 16407409
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  • 8
    Keywords: CANCER ; CELLS ; GROWTH ; GROWTH-FACTOR ; tumor ; carcinoma ; Germany ; human ; MICROSCOPY ; DIAGNOSIS ; PROTEIN ; PROTEINS ; TUMORS ; COMPLEX ; COMPLEXES ; INDUCTION ; KERATINOCYTES ; SKIN ; ASSOCIATION ; immunohistochemistry ; skin cancer ; CARCINOMA-CELLS ; LOCALIZATION ; ADHESION ; intermediate filaments ; CARCINOMAS ; INVOLVEMENT ; squamous cell carcinoma ; beta-catenin ; epidermis ; human hair follicle ; HUMAN EPIDERMIS ; SKIN-CANCER ; CATENIN ; basal cell carcinoma ; HUMAN SKIN ; EPIDERMAL-GROWTH-FACTOR ; INNER-ROOT-SHEATH ; RE ; keratinocyte ; TUMORIGENESIS ; HAIR FOLLICLE ; SKIN CANCERS ; cell adhesion ; hair ; INTERCELLULAR-JUNCTIONS ; BCC ; DESMOSOMAL PLAQUE PROTEINS ; ADHERENS JUNCTIONS ; CELL-CARCINOMA ; E-CADHERIN EXPRESSION ; actin-binding protein ; INTERCELLULAR-ADHESION
    Abstract: Isoform E2 of drebrin, an actin-binding protein originally identified in neuronal cells, has recently been identified in diverse non-neuronal cells, mostly in association with cell processes and intercellular junctions. Here, we report on the presence of drebrin in normal human skin, epithelial skin cancers, and cultured keratinocytes. Keratinocytes of normal epidermis contain almost no drebrin but the protein is readily seen in hair follicles. By immunohistochemistry and immunoblot, basal cell carcinomas (BCC) are rich in drebrin, and confocal laser scanning and immunoelectron microscopy show accumulation at adhering junctions, in co-localization with actin and partially with plaque proteins. In squamous cell carcinomas, keratoacanthomas, and in epidermal precancers, drebrin is heterogeneously distributed, appearing as mosaics. Primary keratinocyte cultures contain significant amounts of drebrin enriched at adhering junctions. When epithelium-derived cells devoid of drebrin are transfected with drebrin-enhanced green fluorescent protein, constructs accumulate in the cell periphery, and immunoprecipitation shows complexes with actin. During epidermal growth factor induced formation of cell processes, drebrin retains this junction association, as observed by live cell microscopy. Our results suggest novel functions of drebrin such as an involvement in cell-cell adhesion and tumorigenesis and a potential value in diagnosis of BCC
    Type of Publication: Journal article published
    PubMed ID: 16185277
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  • 9
    Keywords: PEPTIDE ; CELLS ; tumor ; TUMOR-CELLS ; AGENTS ; Germany ; SYSTEM ; TOOL ; SITE ; DRUG ; TISSUE ; ACTIVATION ; SEQUENCE ; treatment ; CLEAVAGE ; TRANSPORT ; TUMOR PROGRESSION ; DELIVERY ; specificity ; LIVING CELLS ; TUMOR CELLS ; PRECURSORS ; CATHEPSIN-B ; RE ; GLIOMA ; GLIOMA-CELLS ; DRUG-DELIVERY ; TUMOR-CELL ; drug targeting ; glioblastoma multiforme ; TOOLS ; cathepsin B ; intracellular targeting ; METHYL-ESTER ; solid phase peptide synthesis ; SPPS ; transmembrane transport
    Abstract: Goal in pharmaceutical research is achievement of necessary drug concentrations in the target organ, effective treatment with safe delivery of genetic agents, while sparing normal tissue and minimizing side effects. A new "BioShuttle"-delivery system harbouring a cathepsin B cutting site, a nuclear address sequence and a functional Peptide was developed and tumor cells were treated. Transport and subcellular activation were determined by confocal laser scanning microscopy permitting the conclusion: BioShuttle-conjugates prove as efficient tools for genetic interventions by selective and topical activation of therapeutic peptide precursors by enzymatic cleavage. As shown here for glioma cells and the cathepsin B cleavable site, living cells can be treated with high specificity and selectivity for diagnostic and therapeutic purposes. (c) 2006 Elsevier B.V. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16730647
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  • 10
    Keywords: CELLS ; Germany ; human ; PROTEIN ; RNA ; CULTURED-CELLS ; DNA ; CONTRAST ; DYNAMICS ; MELANOMA ; MIGRATION ; cytoskeleton ; LIVING CELLS ; BODY ; ORGANIZATION ; CELL-MIGRATION ; RE ; assembly ; F-ACTIN ; LEVEL ; cell migration ; laminin ; function ; branching ; actin-binding protein ; ACTIN ; FILAMENTS ; MOVEMENTS ; ARP2/3 COMPLEX ; DENDRITIC FILOPODIA ; DEPOLYMERIZING FACTOR ; EDGES ; lamellipodium ; LEADING-EDGE ; microspikes ; MIGRATING CELLS ; MYOSIN-II ; tropomyosin
    Abstract: The actin-binding protein (ABP) drebrin, isoform E2, is involved in remodelling of the actin cytoskeleton and in formation of cell processes, but its role in cell migration has not yet been investigated. Therefore, we have studied the organization of drebrin in motile cultured cells such as murine B16F1 melanoma and human SV80 fibroblast cells, using live cell confocal microscopy. In cells overexpressing DNA constructs encoding drebrin linked to EGFP, numerous long, branched cell processes were formed which slowly retracted and extended, whereas forward movement was halted. In contrast, stably transfected 1316171 cells containing drebrin-EGFP at physiological levels displayed lamellipodia and were able to migrate on laminin. Surprisingly, in such cells, drebrin was absent from anterior lamellipodia but was enriched in a specific juxtanuclear zone, the "drebrin-enriched zone" (DZ), and in the tail. in leading edges of SV80 cells, characterized by pronounced actin microspikes, drebrin was specifically enriched along posterior portions of the microspikes, together with tropomyosin. Drebrin knock-down by small interfering RNAs did not impair movements of SV80 cells. our results confirm the role of drebrin E2 in the formation of branching processes and further indicate that during cell migration, the protein contributes to retraction of the cell body and the tail but not to lamellipodia formation. In particular, the novel, sizable juxtanuclear DZ structure will have to be characterized in future experiments with respect to its molecular assembly and cell biological functions. (c) 2006 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16780834
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