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  • DKFZ Publication Database  (30)
  • 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 ; MICROSCOPY ; IMAGES ; PROTEINS ; PAIRS ; ANTIGEN ; ANTIGENS ; FIELD ; PARTICLES ; IDENTIFICATION ; US ; LOCALIZATION ; immunocytochemistry ; QUANTITATIVE-ANALYSIS ; FLUORESCENCE ; SECTIONS ; electron microscopy ; automated detection ; gold particles ; IMMUNOGOLD ; immunolabeling ; slow-scan cooled CCD camera
    Abstract: This work presents a computerized method to identify, detect, evaluate, and, by colored overlay, present gold particle pairs in electron microscopy (EM), even in wide-field views. Double gold immunolabeled specimens were analyzed in a LEO 912 electron microscope equipped with a 2k x 2k-pixel slow-scan cooled CCD camera connected to a computer with analySIS 3.1 PRO image processing software. The acquisition of a high-resolution and high-dynamic-range image by the camera allowed correct segmentation of the gold particles, separating them from other cell structures and from the substrate. Particle identification was performed by a classification module designed by us. Based on shape and size, the computer recognized the group of small particles and classified them as either singular or clustered and differentiated these from the single bigger type. The final image shows the particle types separated and colored, and indicates the total number of objects encountered in the specific region of interest. Moreover, a montage tool allowed us to obtain final representative images of large microscopic fields, which on analysis by the Gold Finder module provided information on the distribution and localization of antigens comparable to that provided by the wide-field light microscope images. (C) 2003 Elsevier Science (USA). All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 12648569
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  • 3
    Keywords: IN-VIVO ; MICROSCOPY ; VIVO ; DNA ; NUCLEI ; CLEAVAGE ; STAGE ; EMBRYO ; SECTIONS ; EMBRYOS ; Biomphalaria straminea ; CLSM ; embryonic development ; GLAND ; snail
    Abstract: Biomphalaria straminea is a freshwater snail and one of the intermediate hosts of the trematode parasite which causes schistosomiasis in Brazil. The main stages of embryonic development were analyzed with confocal laser scanning microscopy (CLSM), using the fluorescent probe DiOC and Nile Red as a vital stain in in vivo preparations. In fixed preparations nuclei were stained by the Feulgen reaction or the fluorescent DNA probe, Hoechst 33342. Results obtained from the analysis of embryos at the stages of early cleavage, morula, blastula, gastrula, early trocophore and veliger showed that these stages are similar to those described for Biomphalaria glabrata and Biomphalaria tenagophila. CLSM optical sections of early trochophore showed important morphological structures such as the blastopore, stomodeum and shell gland; and in early veliger, internal organs such as the esophagus, stomach and male and female ducts were also clearly identified
    Type of Publication: Journal article published
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  • 4
    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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  • 5
    Keywords: drug delivery, carrier molecules, facilitated transport, glioblastoma multiforme, temozolomide
    Abstract: Recurrent glioblastoma multiforme (GBM), insensitive against most therapeutic interventions, has low response and survival rates. Temozolomide (TMZ) was approved for second-line therapy of recurrent anaplastic astrocytoma. However, TMZ therapy in GBM patients reveals properties such as reduced tolerability and inauspicious hemogram. The solution addressed here concerning GBM therapy consolidates and uses the potential of organic and peptide chemistry with molecular medicine. We enhanced the pharmacologic potency with simultaneous reduction of unwanted adverse reactions of the highly efficient chemotherapeutic TMZ. The TMZ connection to transporter molecules (TMZ-BioShuttle) was investigated, resulting in a much higher pharmacological effect in glioma cell lines and also with reduced dose rate. From this result we can conclude that a suitable chemistry could realize the ligation of pharmacologically active, but sensitive and highly unstable pharmaceutical ingredients without functional deprivation. The TMZ-BioShuttle dramatically enhanced the potential of TMZ for the treatment of brain tumors and is an attractive drug for combination chemotherapy.
    Type of Publication: Journal article published
    PubMed ID: 19920915
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  • 6
    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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  • 7
    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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  • 8
    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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  • 9
    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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  • 10
    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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